LOCUS       NP_082577                655 aa            linear   ROD 01-MAY-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 3 [Mus musculus].
ACCESSION   NP_082577
VERSION     NP_082577.2
DBSOURCE    REFSEQ: accession NM_028301.5
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 655)
  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   2  (residues 1 to 655)
  AUTHORS   Rothe,B., Ikawa,Y., Zhang,Z., Katoh,T.A., Kajikawa,E.,
            Minegishi,K., Xiaorei,S., Fortier,S., Dal Peraro,M., Hamada,H. and
            Constam,D.B.
  TITLE     Bicc1 ribonucleoprotein complexes specifying organ laterality are
            licensed by ANKS6-induced structural remodeling of associated ANKS3
  JOURNAL   PLoS Biol 21 (9), e3002302 (2023)
   PUBMED   37733651
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Schlimpert,M., Lagies,S., Budnyk,V., Muller,B., Walz,G. and
            Kammerer,B.
  TITLE     Metabolic Phenotyping of Anks3 Depletion in mIMCD-3 cells - a
            Putative Nephronophthisis Candidate
  JOURNAL   Sci Rep 8 (1), 9022 (2018)
   PUBMED   29899363
  REMARK    GeneRIF: Combined metabolomics successfully identified 155
            metabolites; 48 metabolites were identified to be significantly
            altered by decreasing Ankyrin repeat and sterile alpha motif domain
            containing 3 protein (Anks3) levels.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Nakajima,Y., Kiyonari,H., Mukumoto,Y. and Yokoyama,T.
  TITLE     The Inv compartment of renal cilia is an intraciliary
            signal-activating center to phosphorylate ANKS6
  JOURNAL   Kidney Int 93 (5), 1108-1117 (2018)
   PUBMED   29395339
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Delestre,L., Bakey,Z., Prado,C., Hoffmann,S., Bihoreau,M.T.,
            Lelongt,B. and Gauguier,D.
  TITLE     ANKS3 Co-Localises with ANKS6 in Mouse Renal Cilia and Is
            Associated with Vasopressin Signaling and Apoptosis In Vivo in Mice
  JOURNAL   PLoS One 10 (9), e0136781 (2015)
   PUBMED   26327442
  REMARK    GeneRIF: ANKS3-ANKS6 direct interaction through their SAM domain.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Ramachandran,H., Engel,C., Muller,B., Dengjel,J., Walz,G. and
            Yakulov,T.A.
  TITLE     Anks3 alters the sub-cellular localization of the Nek7 kinase
  JOURNAL   Biochem Biophys Res Commun 464 (3), 901-907 (2015)
   PUBMED   26188091
  REMARK    GeneRIF: Anks3 N-terminal ankyrin repeats, but not SAM domain
            required for Nek7 interaction.Nek7 increased Ser/Thr
            phosphorylation of Anks3 primarily within ankyrin domain.
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Yakulov,T.A., Yasunaga,T., Ramachandran,H., Engel,C., Muller,B.,
            Hoff,S., Dengjel,J., Lienkamp,S.S. and Walz,G.
  TITLE     Anks3 interacts with nephronophthisis proteins and is required for
            normal renal development
  JOURNAL   Kidney Int 87 (6), 1191-1200 (2015)
   PUBMED   25671767
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Tamplin,O.J., Cox,B.J. and Rossant,J.
  TITLE     Integrated microarray and ChIP analysis identifies multiple Foxa2
            dependent target genes in the notochord
  JOURNAL   Dev Biol 360 (2), 415-425 (2011)
   PUBMED   22008794
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
            Saga,Y., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: III. the complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 10 (4), 167-180 (2003)
   PUBMED   14621295
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Phan,L.K., Lin,F., LeDuc,C.A., Chung,W.K. and Leibel,R.L.
  TITLE     The mouse mahoganoid coat color mutation disrupts a novel C3HC4
            RING domain protein
  JOURNAL   J Clin Invest 110 (10), 1449-1459 (2002)
   PUBMED   12438443
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163723.3 and AC240849.2.
            
            On May 17, 2008 this sequence version replaced NP_082577.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050929.1, AK012494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164139 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 2.48 cM"
     Protein         1..655
                     /product="ankyrin repeat and SAM domain-containing protein
                     3"
                     /calculated_mol_wt=71951
     Region          1..421
                     /region_name="Interaction with NEK7.
                     /evidence=ECO:0000269|PubMed:26188091"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5M9H0; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Region          <39..221
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          39..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          69..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(70,74..75,78..80,82..83,87,90,99,101,103,107..108,
                     111..113,115..116,120,123,132,134,136,140..141,144..146,
                     148..149,153,156)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Site            96
                     /site_type="hydroxylation"
                     /note="3-hydroxyasparagine.
                     /evidence=ECO:0000269|PubMed:25671767; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Region          101..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          134..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          168..199
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Region          314..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     Region          423..486
                     /region_name="SAM_ANKS3"
                     /note="SAM domain of ANKS3 subfamily; cd09519"
                     /db_xref="CDD:188918"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26188091; propagated from
                     UniProtKB/Swiss-Prot (Q9CZK6.2)"
     CDS             1..655
                     /gene="Anks3"
                     /gene_synonym="2700067D09Rik; mKIAA1977"
                     /coded_by="NM_028301.5:95..2062"
                     /db_xref="CCDS:CCDS27928.1"
                     /db_xref="GeneID:72615"
                     /db_xref="MGI:MGI:1919865"
ORIGIN      
        1 mselsdease pellkrslsm whglgaqgsp eeldvpldlh taasigqhev vkecvqrgel
       61 dlnkkngggw talmyasyig hdtivhllle agvsvnvptp egqtplmlas scgnesiayf
      121 llqqgaelem kdihgwtalf hctsaghqqm vkfllesgan anvrepvygy tplmeaaasg
      181 heiivqyfln hgvkvdtrdh sgatacmlar qfghmkival methspvlpk slyrspekye
      241 dlsssdeswp vpqrqrpcrk kglsihegpr alakitaigl ggktqttyeq vpprgyvtft
      301 ssdentmese glcyrdvtsp ineqdvesss sssreeptfc aslgpvwrss ssdglaraqg
      361 lsseasiesn edsdharkss vrkqtrsylk nksrhgnsdg hwpsstgpas ipgsepqtek
      421 spysgpqdla tlleqigclk ylqvfeeqdi dlrifltlte sdlkeigitl fgpkrkmtsa
      481 iarwhssarp psdalelaya drletemqel aiqlhkccee aealrgqvsq eqelravves
      541 clleqdsark dihaqlqeaq tlaqdaalvl dqlracqael sarlrqhhsp regtpnphfl
      601 sadskgwpip lqalslpels galedrvhem gqalcsvtqs leklqmlnak kwrep
//
