LOCUS       NP_001186065            7355 aa            linear   ROD 11-MAR-2025
DEFINITION  microtubule-actin cross-linking factor 1 isoform 1 [Mus musculus].
ACCESSION   NP_001186065
VERSION     NP_001186065.1
DBSOURCE    REFSEQ: accession NM_001199136.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 7355)
  AUTHORS   Zou,L., Xiang,C. and Lu,M.
  TITLE     MSI1 Stabilizes MACF1 to Inhibit Apoptosis of MC3T3-E1 Cells
            Induced by High Glucose and Promote Osteogenic Differentiation
            Through Wnt/beta-Catenin Signaling Pathway
  JOURNAL   Mol Biotechnol 65 (7), 1085-1095 (2023)
   PUBMED   36443618
  REMARK    GeneRIF: MSI1 Stabilizes MACF1 to Inhibit Apoptosis of MC3T3-E1
            Cells Induced by High Glucose and Promote Osteogenic
            Differentiation Through Wnt/beta-Catenin Signaling Pathway.
REFERENCE   2  (residues 1 to 7355)
  AUTHORS   Chen,Z., Huai,Y., Chen,G., Liu,S., Zhang,Y., Li,D., Zhao,F.,
            Chen,X., Mao,W., Wang,X., Yin,C., Yang,C., Xu,X., Ru,K., Deng,X.,
            Hu,L., Li,Y., Peng,S., Zhang,G., Lin,X. and Qian,A.
  TITLE     MiR-138-5p Targets MACF1 to Aggravate Aging-related Bone Loss
  JOURNAL   Int J Biol Sci 18 (13), 4837-4852 (2022)
   PUBMED   35982896
  REMARK    GeneRIF: MiR-138-5p Targets MACF1 to Aggravate Aging-related Bone
            Loss.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 7355)
  AUTHORS   Su,P., Tian,Y., Yin,C., Wang,X., Li,D., Yang,C., Pei,J., Deng,X.,
            King,S., Li,Y. and Qian,A.
  TITLE     MACF1 promotes osteoblastic cell migration by regulating MAP1B
            through the GSK3beta/TCF7 pathway
  JOURNAL   Bone 154, 116238 (2022)
   PUBMED   34700040
  REMARK    GeneRIF: MACF1 promotes osteoblastic cell migration by regulating
            MAP1B through the GSK3beta/TCF7 pathway.
REFERENCE   4  (residues 1 to 7355)
  AUTHORS   Gilbert,B.L., Zhu,S., Salameh,A., Sun,S., Alagramam,K.N. and
            McDermott,B.M. Jr.
  TITLE     Actin Crosslinking Family Protein 7 Deficiency Does Not Impair
            Hearing in Young Mice
  JOURNAL   Front Cell Dev Biol 9, 709442 (2021)
   PUBMED   34917607
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 7355)
  AUTHORS   Ghasemizadeh,A., Christin,E., Guiraud,A., Couturier,N., Abitbol,M.,
            Risson,V., Girard,E., Jagla,C., Soler,C., Laddada,L., Sanchez,C.,
            Jaque-Fernandez,F.I., Jacquemond,V., Thomas,J.L., Lanfranchi,M.,
            Courchet,J., Gondin,J., Schaeffer,L. and Gache,V.
  TITLE     MACF1 controls skeletal muscle function through the
            microtubule-dependent localization of extra-synaptic myonuclei and
            mitochondria biogenesis
  JOURNAL   Elife 10, e70490 (2021)
   PUBMED   34448452
  REMARK    GeneRIF: MACF1 controls skeletal muscle function through the
            microtubule-dependent localization of extra-synaptic myonuclei and
            mitochondria biogenesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 7355)
  AUTHORS   Ye,T.Z., Gordon,C.T., Lai,Y.H., Fujiwara,Y., Peters,L.L.,
            Perkins,A.C. and Chui,D.H.
  TITLE     Ermap, a gene coding for a novel erythroid specific
            adhesion/receptor membrane protein
  JOURNAL   Gene 242 (1-2), 337-345 (2000)
   PUBMED   10721728
REFERENCE   7  (residues 1 to 7355)
  AUTHORS   Leung,C.L., Sun,D., Zheng,M., Knowles,D.R. and Liem,R.K.
  TITLE     Microtubule actin cross-linking factor (MACF): a hybrid of dystonin
            and dystrophin that can interact with the actin and microtubule
            cytoskeletons
  JOURNAL   J Cell Biol 147 (6), 1275-1286 (1999)
   PUBMED   10601340
REFERENCE   8  (residues 1 to 7355)
  AUTHORS   Tomotsune,D., Takihara,Y., Berger,J., Duhl,D., Joo,S., Kyba,M.,
            Shirai,M., Ohta,H., Matsuda,Y., Honda,B.M., Simon,J., Shimada,K.,
            Brock,H.W. and Randazzo,F.
  TITLE     A novel member of murine Polycomb-group proteins, Sex comb on
            midleg homolog protein, is highly conserved, and interacts with
            RAE28/mph1 in vitro
  JOURNAL   Differentiation 65 (4), 229-239 (1999)
   PUBMED   10653359
REFERENCE   9  (residues 1 to 7355)
  AUTHORS   Wan,M., Cravatt,B.F., Ring,H.Z., Zhang,X. and Francke,U.
  TITLE     Conserved chromosomal location and genomic structure of human and
            mouse fatty-acid amide hydrolase genes and evaluation of clasper as
            a candidate neurological mutation
  JOURNAL   Genomics 54 (3), 408-414 (1998)
   PUBMED   9878243
REFERENCE   10 (residues 1 to 7355)
  AUTHORS   Bernier,G., Mathieu,M., De Repentigny,Y., Vidal,S.M. and Kothary,R.
  TITLE     Cloning and characterization of mouse ACF7, a novel member of the
            dystonin subfamily of actin binding proteins
  JOURNAL   Genomics 38 (1), 19-29 (1996)
   PUBMED   8954775
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606932.10 and AL606918.9.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            RefSeq Select criteria    :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..7355
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 57.42 cM"
     Protein         1..7355
                     /product="microtubule-actin cross-linking factor 1 isoform
                     1"
                     /note="microtubule-actin cross-linking factor 1; actin
                     cross-linking family 7; actin-crosslinking protein 7;
                     trabeculin alpha"
                     /calculated_mol_wt=831750
     Region          1..295
                     /region_name="Actin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZHV2; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          77..181
                     /region_name="CH_PLEC-like_rpt1"
                     /note="first calponin homology (CH) domain found in the
                     plectin/dystonin/MACF1 family; cd21188"
                     /db_xref="CDD:409037"
     Site            order(80,84,134,136..137,140..141,143,152..160,165,
                     167..168,170..171,174..175,178)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409037"
     Region          192..298
                     /region_name="CH_MACF1_rpt2"
                     /note="second calponin homology (CH) domain found in
                     microtubule-actin cross-linking factor 1, isoforms 1/2/3/5
                     (MACF1) and similar proteins; cd21240"
                     /db_xref="CDD:409089"
     Site            order(196,200,250,252..253,256..257,259,267..275,282,
                     284..285,287..288,291..292,295)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409089"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15345747,
                     ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          377..399
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          441..464
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          586..784
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          857..923
                     /region_name="SH3_10"
                     /note="SH3 domain; pfam17902"
                     /db_xref="CDD:407754"
     Region          958..1035
                     /region_name="Spectrin_like"
                     /note="Spectrin like domain; pfam18373"
                     /db_xref="CDD:465730"
     Region          1050..1073
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            1122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1128..1154
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1164..1343
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          1187..1210
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1257..1282
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            1273..1278
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Site            1367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            1376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1577..1619
                     /region_name="Plectin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1579..1617
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          1654..1696
                     /region_name="Plectin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1656..1694
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          1769..1809
                     /region_name="Plectin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1770..1805
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          1808..1846
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          1811..1848
                     /region_name="Plectin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          1855..1885
                     /region_name="Plectin 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          <1855..1884
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Site            2051
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            2077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            2081
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2120..2155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2276..2316
                     /region_name="Plectin 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2278..2315
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2352..2393
                     /region_name="Plectin 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2359..2391
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2391..2429
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2394..2425
                     /region_name="Plectin 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2487..2528
                     /region_name="Plectin 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2487..2525
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2671..2715
                     /region_name="Plectin 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2673..2711
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2715..2746
                     /region_name="Plectin"
                     /note="Plectin repeat; pfam00681"
                     /db_xref="CDD:459901"
     Region          2806..2841
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          2951..2978
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          3058..3099
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            3082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            3085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          3225..3244
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          <3343..3715
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          3592..4347
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          3656..3680
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          3843..4071
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          3843..3918
                     /region_name="Spectrin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            3887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          3896..3918
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            order(3957..3958,3960..3963)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          3960..4068
                     /region_name="Spectrin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4085..4110
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4221..4247
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4426..4534
                     /region_name="Spectrin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4428..4647
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            4456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4471..4494
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            4481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            4535..4540
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          4653..4867
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          4729..4752
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            order(4756..4759,4761..4762)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          4760..4864
                     /region_name="Spectrin 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          4842..5663
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            4922
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5011..5036
                     /region_name="LRR 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5132..5154
                     /region_name="LRR 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5196..5301
                     /region_name="Spectrin 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5241..5264
                     /region_name="LRR 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5308..5521
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5308..5410
                     /region_name="Spectrin 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            5395
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            5411..5416
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5415..5507
                     /region_name="Spectrin 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5632..5736
                     /region_name="Spectrin 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5634..5847
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5655..5679
                     /region_name="LRR 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            5738..5743
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5743..5845
                     /region_name="Spectrin 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          5744..5960
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5764..5788
                     /region_name="LRR 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            order(5846..5849,5851..5852)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          5962..6179
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          5962..6067
                     /region_name="Spectrin 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            5989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6068..6073
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6072..6176
                     /region_name="Spectrin 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6167
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          6182..6398
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          6182..6285
                     /region_name="Spectrin 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6287..6292
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6290..6396
                     /region_name="Spectrin 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          6401..6504
                     /region_name="Spectrin 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          6403..6617
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          6453..6476
                     /region_name="LRR 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6506..6511
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6509..6615
                     /region_name="Spectrin 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          6622..6834
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Region          6622..6723
                     /region_name="Spectrin 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6724..6729
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          6727..6831
                     /region_name="Spectrin 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          6844..6968
                     /region_name="SPEC"
                     /note="Spectrin repeats; smart00150"
                     /db_xref="CDD:197544"
     Region          6905..6938
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            6924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          <7006..7076
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          7078..7355
                     /region_name="C-terminal tail"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          7081..7159
                     /region_name="GAS2"
                     /note="Growth-Arrest-Specific Protein 2 Domain;
                     smart00243"
                     /db_xref="CDD:128539"
     Region          7172..7355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          <7180..>7353
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            7221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            7246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            7259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UPN3; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Region          7280..7295
                     /region_name="4 X 4 AA tandem repeats of [GS]-S-R-[AR]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            7297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     Site            7300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9QXZ0.2)"
     CDS             1..7355
                     /gene="Macf1"
                     /gene_synonym="ABP620; Acf7; Aclp7; D830031N03Rik; MACF;
                     mKIAA0465; mKIAA0754"
                     /coded_by="NM_001199136.2:178..22245"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS57295.1"
                     /db_xref="GeneID:11426"
                     /db_xref="MGI:MGI:108559"
ORIGIN      
        1 msssdeetls erscrsersc rsersyrser sgslspcppg dtlpwnlplh eqkkrksqds
       61 vldpaeravv rvaderdrvq kktftkwvnk hlmkvrkhin dlyedlrdgh nlisllevls
      121 giklprekgr mrfhrlqnvq ialdflkqrq vklvnirndd itdgnpkltl gliwtiilhf
      181 qisdiyisge sgdmsakekl llwtqkvtag ytgvkctnfs scwsdgkmfn alihryrpdl
      241 vdmervqvqs nrenleqafe vaerlgvtrl ldaedvdvps pdeksvityv ssiydafpkv
      301 peggegisat evdsrwqeyq srvdslipwi rqhtilmsdk sfpqnpvelk alynqyihfk
      361 eteilakere kgrikelykl levwiefgri klpqgyhpnh veeewgkliv emlerekslr
      421 paverlelll qiankiqnga lnceekltla kntlqadaah lesgqpvqce sdvimyiqec
      481 eglirqlqvd lqilrdekyy qleelafrvm rlqdelvtlr lectnlyrkg hfsslelvpp
      541 stlttthlka eplnktthss stswfrkpmt rtelvsisss edegnlrfvy ellswveemq
      601 mkleraewgn dlpsvelqle tqqhihtsve elgssvkear lyegkmsqnf htsyvetlgk
      661 letqycklke tssfrmrhlq slhkfvsrat aeliwlngke eeelacdwsd snpnisakkt
      721 yfseltmele gkqdvfrslq dtaevlslen hpakqtveay saavqsqlqw mkqlclcveq
      781 hvkenaayfq ffsdardles flrnlqdsik rkytcdrsts lsrledllqd smdekeqliq
      841 skssvaslvg rsktivqlkp rnpdhvlkst lsvkaicdyr qieiticknd ecvlednsqr
      901 tkwkvisptg neamvpsvcf lipppnkeai emasrveqsy qkvmalwhql hintkslisw
      961 nylrkdldtv qtwsleklrs lapgechqvm knlqahyedf lqdshdsalf svadrlriee
     1021 eveackahfq hlmkslened keetlakvyi selknirlll eeceqrllkq iqspassktd
     1081 rdarqditlr iaeqehtqed lqhlrsdlda ismkcnvflq qspsgssatt lrselnlmve
     1141 kmdhvyglst vylnklktid vivrsmqdae llvkgyeikl sqeeavpadl saleshrttl
     1201 qhwlsdvkdk nsvfsvldee itkakkvaeq lrhpasepnl dleryqekgs qlqerwhrvi
     1261 aqletrqsev esiqevlrdy rachgtlikw ieettaqqem mkpgqaedsr vlseqlsqqt
     1321 elfaeiernq tkldqcqkfs qqystivkdy elqlmtykaf vesqqkspgk rrrmisssda
     1381 itqefmdlrt rytalvtltt qhvkyisdal rrleeeekvv eeekqehvek vkdllgwvst
     1441 larntqgttt sshtsasadi ekaileqqvl aeelttkkeq vseaiktsqi flakhghkls
     1501 egekeqiseq lrvlnktyhd lcdgsanqlq qlqselaqqt eqkgcravag vidlgtveif
     1561 piframqkgl idqdtglvll esqiimsgli dpenseklsl eegltrnfin lpiyqqllgl
     1621 rdslslvsrl tgtlgslsvv eaiekkiise rlglkvlevh latggfslpp sencinleea
     1681 fhqgfiassl hselqshlrs sknlidpnta ekvglldlmq rciihqesgl kllpvkqlag
     1741 gmvslksgrk vsifravqeg lidrqvtvrl leaqlfaggi vdprtghrlt veeavrhnli
     1801 dqdmacaili rqlqtggiid tvtgdrmtid eavtnnlvaa kialvilesl wsfmglllpe
     1861 sgeilpitda leqgivstel ahkilhnrqq iealflptlt eiwswekate sgildkdlvn
     1921 nlrsvcipdm mphiqladsa eqskvgfaag kppvsgpree gsshgekllf qlmthsyiha
     1981 htgqrlllld qelvemltsr ddcqvilpev feiqhqrlnt sealqelytg tisqissakh
     2041 prkpcesqfl sqnkdypsqe ncteakgers vvgiecspae sperelflke qeaiienvgs
     2101 lkvinkvklk lqrpllgsrk eeqaetlree nisgdpllve cpeesegkdl stekskcqtp
     2161 tkcsftchke qvktikdips etgtsliksq nqmsqfqvdt svglrsefks ehdmnvnsle
     2221 kelkeellvk dghkqsqegq svadgqtval ektdtednad epallhsspf edatlstlsa
     2281 qlqdggifne etgqklllne aiaqglvssh tavklmgkln mfrgffdsqt cesltteevi
     2341 deglmdekll ynvlmsdkai sgildprths lcsvkeavaa glldketatr ilegqvitgg
     2401 ivdlkrgkkl svtlasnlgl vdtadqteli nlekatkgrg aekavkerli elqmetaglm
     2461 dpeskapltv lqsidrgile reaavylltk qvldggiihh isglrlsvdn afkhgliged
     2521 marqlrkven fihyqffhpq tkealsfsea ikldlvspdl kreiqeiqdf sgnlgdfiyg
     2581 qkltlaktnk eeslanktel psgvmhgvid penctiipys elvkkcridt esgwrylevi
     2641 pfsdikdeag nnvltppeai qlgkvdfasa lkvleaqant ggiidmatgk rvtlasalek
     2701 klldenmari iashqmlsgg iidiysdqrv tlndavekrl ispelaamiq vdplaeqggt
     2761 gvcelkgdfl rkellsessk tpresyskek heavlqagsl capekagirg sngekaekgr
     2821 kisvemegqr qdekassdnk vsasilspfg fegessyqvs vthpcsescd lkpreetrsc
     2881 mkkcavverd kvvtqikmvs hvkqstsgld aeearerqgr mvskeqgshy etagnllser
     2941 svrvdrrvrr emggeqsvqm sreaavlsee eldqevtigd epdsfvksqs mkmigndkgk
     3001 eagiekdisv vckiegfpsq mtskdasltn qdalpfyteg etktvnlcsi lkpgeklsqe
     3061 tastvqkepl sseiprperl nsqesdeepq isdvphiskg dmaaqittrq ettdvqdlyi
     3121 tskssetkdk ifpsknyiek lhqeipmdpt rshklkeati stletegisy ldssdikslc
     3181 edskadhksc ghqkskvttt qakkslevvd llvrdteegs sedrvgqrgp rvlasllpek
     3241 lptrtvqsen irqhdavipa iseireemal slpcsvvkvd gkipkekhke ilgdeqgpfm
     3301 aipsgkgieg vnpepcratq nvftrrlcle hdeklvsyls llrdiemrtk qiqplelnva
     3361 elqdllgqak eldrelkdls tvvsqelecv drivisqpqe vpaqllkale kdaknlqksl
     3421 dsvsdswssr flhlqsavev kkatvlnrhk elqgklqdlr awvgrasltl nskgcdtetd
     3481 adslshtlqp ykdmkqsmae rksqldalal diqlfisehp qdlslqqnqe mlqflselqr
     3541 sfqglvehta aqkdvvqghl qqvqqevqvk tlqkqqdtch kkledlcnwv gqaeralerh
     3601 qggasrqelp alqqnqsdlk dlqgdiqshs tsfatavkdi egfleenqtk lspqeltalr
     3661 eklhqakeqy evlqertrva qkeleeavts alqqeteksk aatelaenkr kidalldwva
     3721 svgsserkpq aslpgmeqfs gaclekqtla atdghvdvnq vpetldrqye lmkarhqell
     3781 sqqqnfivat qsvqsfldqh shnltpeerq klqeklgelk eqyaaslars eaelkqtqal
     3841 rdelqkflqd hkefenwlqq seneldsmhk ggsspealns llkrqgsfse dvishkgdlr
     3901 fvtisgqkvl etennfeegq epsatrnlvn eklkdatery ttlhskcirl gshlsmllgq
     3961 yqqfqssads lqawvltcea svgkllsdtv asdpgvlqqq lattkqlqee laehqvpvek
     4021 lqkaahdlld iegepaldcr piqettdsis srfqnlscsl dersallqka iaqsqsvqes
     4081 mesllqsire veqnlerdqv aslssgviqe alannmklkq diarqkssle athdmvtrfm
     4141 etadsnsasv lqgklaelsq rfqqlqlqqq ekesnlkkll pqaemfeqls nklqqfmenk
     4201 srllasgnqp dqdiahfsqq iqeltlamed qkenldtleh lvttlgscgf aldlsqhqdk
     4261 iqnlkkdfte lqktvqerek dastcqeqld efrklirtfq kwlketegnv ppaktfvsak
     4321 elekqiehlk dlisdweskg allgeinakg taleslimdi tapdsqaktg silppvgssv
     4381 gsvngyhtck dlteiqcdmf dvnskyeklw evlrerqesl qtvfsrmeev qkeassvlqw
     4441 leskeevlka mdatlsptkt etvkaqaesn kaflaeleqn spkiqkvkea lagllktypn
     4501 sqeaenwkkm qedlnsrwek atevtvarqk qleesashla cfqaaesqlr pwlmekelmm
     4561 gvlgplsidp nmlnaqkqqv qfmlkefear rqqheqlnea aqgiltgpgd mspsasqvhk
     4621 dlqsisqkwv eltdklnsrs sqidqaivks tqyqdllqdl sekvkaigqr lsgqsaistq
     4681 peavkqqlee tseirsdlgq ldneikeaqt lcqelsllig eqylkdelkk rletvalplq
     4741 gledlaadrm nrlqaalast qqfqqmfdel rtwldekqsq qakncpisak lerlqcqlqe
     4801 neefqknlnq hsgsyeviva egealllsvp pgeekktlqn qlvelrshwe dlskktanrq
     4861 srlkdcmqka qkyqghvedl vpwidecksk mselqvtldp vqlessllrs kamlneaekr
     4921 rslleilnsa adilinssei dedeirdeka glnqnmdait eelqaktssl eemtqrlkef
     4981 qesfkniekk vegakhqlei fdalgsqacs nknleklkaq qevlqalepq vdylrnftqg
     5041 lvedapdgsd asplvhqaev aqqeflevkq rvssscltme nklegigqfh crvremfsql
     5101 adlddeldgm gaigrdtdsl qsqiedvrlf lnkiqalrfd iedseaecrk mleeegtldl
     5161 lglkreleal nkqcgklter gkvrqeqlel tlgrvedfyr klkalndaat aaeegealqw
     5221 ivgtevdvin qqladfklfq kdqvdplqvk lqqvnglgqg liqsagkncd vqglehdmde
     5281 intrwntlnk kvaqriaqlq eallhcgkfq dalepllswl tdteelianq kppsaeykvv
     5341 kaqiqeqkll qrllddrkat vdmlqaeggr iaqsaeladr ekitgqlesl errwtdllsk
     5401 aaarqkqled ilvlakqfhe taepisdfls vtekklanse pvgtqtakih qqiirhkaln
     5461 eeiinrkknv dqaikngqal lkqttgeevl liqekldgik tryaditlts skalrtleqa
     5521 rqlatkfhst yeeltgwlre aeeelaasgg qsptgeqipq fqqrqkelkk evmehrlvld
     5581 tvnevshall elvpwrareg ldklvsdane qyklisdtvg qrvdeidaai qrsqqyeqaa
     5641 daelawvaet krklmalgpi rleqdqttaq lqvqkafsid iirhkdsmde lfshrgeifs
     5701 tcgeeqkavl qektecliqq yeavsllnse ryarleraqv lvnqfwetye elspwaeetl
     5761 aliaqlpppa vdheqlrqqq eemrqlresi aehkphidki lkigpqlkel npeegkmvee
     5821 kyqkaenmya qikdevrqra laldeavsqs aqfhdkiepm letlenlssr lrmpplipae
     5881 vdkirecisd nksatvelek lqpsfealkr rgeeligrsq gadkdlaake iqdkldqmvf
     5941 fwedikarse ereikfldvl elaekfwydm aallttikdt qdivhdlesp gidpsiikqq
     6001 veaaetikee tdglheelef irilgadlif acgetekpev kksidemnna wenlnktwke
     6061 rlekledamq aavqyqdtlq amfdwldntv iklctmppvg tdlntvkdql nemkefkvev
     6121 yqqqiemekl nhqgelmlkk atdetdrdii repltelkhl wenlgekiah rqhklegall
     6181 algqfqhale elmswlthte elldaqrpis gdpkvievel akhhvlkndv lahqatvatv
     6241 nkagselles sagddasslr srletmnqcw esvlqkteer eqqlqstlqq aqgfhseied
     6301 fllelnrmen qlsaskptgg lpetareqld thmelhsqlr akeeiynqll dkgrlmllsr
     6361 gdsgsgskte qsvalleqkw havsskveer kskleealsl atefqnslqe finwltlaeq
     6421 slniasppsl ilntvlsqie ehkvfanevn dhrdqiield qtgnqlkfls qkqdvvlikn
     6481 llvsvqsrwe kvvqrsierg rslddarkra kqfheawkkl idwledaesh ldseleisnd
     6541 pdkiklqlsk hkefqktlgg kqpvydttir tgralkektl lagdtqkldn llgevrdkwd
     6601 tvcgksverq hkleeallfs gqfmdalqal vdwlykvepq laedqpvhgd ldlvmnlmda
     6661 hkvfqkelgk rtgtvqvlkr sgreliegsr ddttwvkgql qelstrwdtv cklsvskqsr
     6721 leqalkqaee frdtvhmlle wlseaeqtlr frgalpddte alqslidthk efmkkveekr
     6781 vdvntavamg eailavchpd cittikhwit iirarfeevl twakqhqqrl etalselvan
     6841 aelleellaw iqwaettliq rdqepipqni drvkaliteh qsfmeemtrk qpdvdrvtkt
     6901 ykrksvepth apfmeksrsg srkslnqptp ppmpilsqse aknprinqls arwqqvwlla
     6961 lerqrklnda ldrleelcpe lkefanfdfd vwrkkymrwm nhkksrvmdf frridkdqdg
     7021 kitrqefidg ilaskfpttk lemtavadif drdgdgyidy yefvaalhpn kdayrpttda
     7081 dkiedevtrq vaqckcakrf qveqigenky rfflgnqfgd sqqlrlvril rstvmvrvgg
     7141 gwmaldeflv kndpcrargr tnielrekfi lpegasqgmt pfrsrgrrsk pssraasptr
     7201 ssssasqsnh sctsmpsspa tpasgtkvis ssgsklkrpt pafhssrtsl agdtsnsssp
     7261 astgakanra dpkksasrpg sragsragsr assrrgsdas dfdlletqsa csdtsessaa
     7321 ggqgssrrgl tkpskiptms kktttasprt pgpkr
//
