LOCUS       NP_109615                979 aa            linear   ROD 01-MAY-2025
DEFINITION  ankycorbin isoform 1 [Mus musculus].
ACCESSION   NP_109615
VERSION     NP_109615.1
DBSOURCE    REFSEQ: accession NM_030690.4
KEYWORDS    RefSeq.
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 979)
  AUTHORS   Jeong,W., Kwon,H., Park,S.K., Lee,I.S. and Jho,E.H.
  TITLE     Retinoic acid-induced protein 14 links mechanical forces to Hippo
            signaling
  JOURNAL   EMBO Rep 25 (9), 4033-4061 (2024)
   PUBMED   39160347
REFERENCE   2  (residues 1 to 979)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 979)
  AUTHORS   Kim,S.J., Woo,Y., Kim,H.J., Goo,B.S., Nhung,T.T.M., Lee,S.A.,
            Suh,B.K., Mun,D.J., Kim,J.H. and Park,S.K.
  TITLE     Retinoic acid-induced protein 14 controls dendritic spine dynamics
            associated with depressive-like behaviors
  JOURNAL   Elife 11, e77755 (2022)
   PUBMED   35467532
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 979)
  AUTHORS   Bedogni,F. and Hevner,R.F.
  TITLE     Cell-Type-Specific Gene Expression in Developing Mouse Neocortex:
            Intermediate Progenitors Implicated in Axon Development
  JOURNAL   Front Mol Neurosci 14, 686034 (2021)
   PUBMED   34321999
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 979)
  AUTHORS   Wu,Y., Wang,T., Zhao,Z., Liu,S., Shen,C., Li,H., Liu,M., Zheng,B.,
            Yu,J. and Huang,X.
  TITLE     Retinoic Acid Induced Protein 14 (Rai14) is dispensable for mouse
            spermatogenesis
  JOURNAL   PeerJ 9, e10847 (2021)
   PUBMED   33643708
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 979)
  AUTHORS   Diaz,E., Yang,Y.H., Ferreira,T., Loh,K.C., Okazaki,Y.,
            Hayashizaki,Y., Tessier-Lavigne,M., Speed,T.P. and Ngai,J.
  TITLE     Analysis of gene expression in the developing mouse retina
  JOURNAL   Proc Natl Acad Sci U S A 100 (9), 5491-5496 (2003)
   PUBMED   12702772
REFERENCE   7  (residues 1 to 979)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 979)
  AUTHORS   Kutty,R.K., Kutty,G., Samuel,W., Duncan,T., Bridges,C.C.,
            El-Sherbeeny,A., Nagineni,C.N., Smith,S.B. and Wiggert,B.
  TITLE     Molecular characterization and developmental expression of NORPEG,
            a novel gene induced by retinoic acid
  JOURNAL   J Biol Chem 276 (4), 2831-2840 (2001)
   PUBMED   11042181
REFERENCE   9  (residues 1 to 979)
  AUTHORS   Peng,Y.F., Mandai,K., Sakisaka,T., Okabe,N., Yamamoto,Y.,
            Yokoyama,S., Mizoguchi,A., Shiozaki,H., Monden,M. and Takai,Y.
  TITLE     Ankycorbin: a novel actin cytoskeleton-associated protein
  JOURNAL   Genes Cells 5 (12), 1001-1008 (2000)
   PUBMED   11168586
REFERENCE   10 (residues 1 to 979)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC158921.17.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same protein.
            
            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##
            Transcript exon combination :: BC052458.1, AF274866.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="15"
                     /map="15 5.35 cM"
     Protein         1..979
                     /product="ankycorbin isoform 1"
                     /note="NORPEG-like protein; p125; retinoic acid-induced
                     protein 14; novel retinal pigment epithelial cell protein;
                     ankyrin repeat and coiled-coil structure-containing
                     protein"
                     /calculated_mol_wt=108722
     Region          1..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          18..51
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          23..50
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..83
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..81
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          85..116
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          85..114
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            order(118,120,124..125,128..130,132..133,137,140,149,151,
                     153,157..158,161..163,165..166,170,173,182,184,186,
                     190..191,194..196,198..199,203,206,215)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          118..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          118..147
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          151..182
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..180
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          184..215
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          184..213
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          217..247
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          247..299
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          270..276
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U312; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          392..429
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Region          <432..>933
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          446..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9P0K7; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9EP71.1)"
     CDS             1..979
                     /gene="Rai14"
                     /gene_synonym="1700008J19Rik; 1700020L11Rik; Ankycorbin;
                     mKIAA1334; Norpeg"
                     /coded_by="NM_030690.4:265..3204"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS37043.1"
                     /db_xref="GeneID:75646"
                     /db_xref="MGI:MGI:1922896"
ORIGIN      
        1 mkslkakfrk sdtnewnknd drllqaveng daekvasllg kkgasatkhd segktafhla
       61 aakghveclk vmvthgvdvt aqdssghsal hvaaknghpe cirkllqyks paenidnsgk
      121 talhyaaaqg clqavqllce hkspinlkdl dgnipllvav qnghseachf lldhgadvns
      181 rdkngrtalm lacetgssnt vdalikkgad lslvdslghn alhysklsen agiqnlllsk
      241 isqdadlktp tkpkqhdqvs kissersgtp kkrkappppi sptqlsdvss prsitstpls
      301 gkesvffaea pfkaeissiq enkdrlsdst agadslldis seadqqdllv llqakvaslt
      361 lhnkelqdkl qakspkdkea eadlsfqsfh stqtdlapsp gkasdipssd akssppvehp
      421 agtsttdndv iirqlqdslh dlqkrlesse aekkqlqdel qsqrtdtlcl nnteisengs
      481 dlsqklketq skyeeamkev lsvqkqmklg llsqesadgy shlreapade didtlkqdlq
      541 kaveesarnk ervreletkl aekeqaeatk ppaeaceelr ssycsvienm nkekaflfek
      601 yqqaqeeimk lkdtlksqmp qeapddsgdm keamnrmide lnkqvselsq lyreaqaele
      661 dyrkrksled aaeyihkaeh erlmhvsnls rakseealse mksqyskvln eltqlkqlvd
      721 ahkensvsit ehlqvittlr ttakemeeki saltghlank eaevaklekq laeekaavsd
      781 amvpkssyek lqaslesevn alatklkesv rerekahsev aqvrsevsqa rrekdniqtl
      841 lkakeqevta lvqkfqraqe elagmrrcse tsskleedkd ekinemtrev lklkealnsl
      901 sqlsystsss krqsqqldll qqqvkqlqnq laeckkhhqe visvyrmhll yavqgqmded
      961 vqkvlkqilt mcknqsqkk
//
