ID   ANS1A_MOUSE             Reviewed;        1150 AA.
AC   P59672; Q6ZQG0;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Ankyrin repeat and SAM domain-containing protein 1A;
DE   AltName: Full=Odin {ECO:0000303|PubMed:29749928};
GN   Name=Anks1a;
GN   Synonyms=Anks1, Kiaa0229, Odin {ECO:0000303|PubMed:29749928};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=12439753; DOI=10.1038/sj.onc.1205988;
RA   Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M.,
RA   Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F.,
RA   Mann M.;
RT   "Cloning of a novel phosphotyrosine binding domain containing molecule,
RT   Odin, involved in signaling by receptor tyrosine kinases.";
RL   Oncogene 21:8029-8036(2002).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   FUNCTION IN EFNA5-EPHA8 SIGNALING PATHWAY, INTERACTION WITH EPHA8, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17875921; DOI=10.1128/mcb.00794-07;
RA   Shin J., Gu C., Park E., Park S.;
RT   "Identification of phosphotyrosine binding domain-containing proteins as
RT   novel downstream targets of the EphA8 signaling function.";
RL   Mol. Cell. Biol. 27:8113-8126(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-642, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-644; SER-663;
RP   SER-677; SER-679; SER-682 AND SER-903, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8] {ECO:0007744|PDB:5ZRY}
RP   X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 707-779 IN COMPLEX WITH EPHA6.
RX   PubMed=29749928; DOI=10.7554/elife.35677;
RA   Wang Y., Shang Y., Li J., Chen W., Li G., Wan J., Liu W., Zhang M.;
RT   "Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM
RT   domain interactions.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Regulator of different signaling pathways. Regulates EPHA8
CC       receptor tyrosine kinase signaling to control cell migration and
CC       neurite retraction. {ECO:0000269|PubMed:17875921}.
CC   -!- SUBUNIT: Interacts (via SAM domain) with EPHA2 (via SAM domain) (By
CC       similarity). Interacts with EPHA8; EPHA8 kinase activity-independent
CC       but stimulated by EPHA8 ubiquitination (PubMed:17875921). Interacts
CC       (via SAM domain) with EPHA6 (via SAM domain) (PubMed:29749928).
CC       {ECO:0000250|UniProtKB:Q92625, ECO:0000269|PubMed:17875921,
CC       ECO:0000269|PubMed:29749928}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection
CC       {ECO:0000269|PubMed:17875921}. Note=Cytoplasmic before and after growth
CC       factor treatment. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P59672-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P59672-2; Sequence=VSP_012704, VSP_012705, VSP_012706;
CC   -!- PTM: Phosphorylated on tyrosine residues in response to EGF and PDGF.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK129094; BAC97904.1; ALT_INIT; mRNA.
DR   EMBL; BC050847; AAH50847.1; -; mRNA.
DR   CCDS; CCDS37525.1; -. [P59672-1]
DR   CCDS; CCDS70778.1; -. [P59672-2]
DR   RefSeq; NP_001272970.1; NM_001286041.1. [P59672-2]
DR   RefSeq; NP_852078.1; NM_181413.4. [P59672-1]
DR   PDB; 5ZRY; X-ray; 1.30 A; A/B=707-779.
DR   AlphaFoldDB; P59672; -.
DR   SMR; P59672; -.
DR   BioGRID; 230297; 2.
DR   FunCoup; P59672; 2361.
DR   IntAct; P59672; 2.
DR   MINT; P59672; -.
DR   STRING; 10090.ENSMUSP00000025058; -.
DR   GlyGen; P59672; 1 site.
DR   iPTMnet; P59672; -.
DR   PhosphoSitePlus; P59672; -.
DR   jPOST; P59672; -.
DR   PaxDb; 10090-ENSMUSP00000025058; -.
DR   PeptideAtlas; P59672; -.
DR   ProteomicsDB; 282005; -. [P59672-1]
DR   ProteomicsDB; 282006; -. [P59672-2]
DR   Pumba; P59672; -.
DR   Antibodypedia; 29433; 103 antibodies from 20 providers.
DR   DNASU; 224650; -.
DR   Ensembl; ENSMUST00000088027.7; ENSMUSP00000085344.6; ENSMUSG00000024219.17. [P59672-2]
DR   Ensembl; ENSMUST00000114842.9; ENSMUSP00000110491.2; ENSMUSG00000024219.17. [P59672-1]
DR   GeneID; 224650; -.
DR   KEGG; mmu:224650; -.
DR   UCSC; uc008bpw.2; mouse. [P59672-2]
DR   UCSC; uc008bpx.2; mouse. [P59672-1]
DR   AGR; MGI:2446180; -.
DR   CTD; 224650; -.
DR   MGI; MGI:2446180; Anks1.
DR   VEuPathDB; HostDB:ENSMUSG00000024219; -.
DR   eggNOG; KOG0507; Eukaryota.
DR   GeneTree; ENSGT00940000155806; -.
DR   InParanoid; P59672; -.
DR   OMA; VIYRQHA; -.
DR   OrthoDB; 10039052at2759; -.
DR   BioGRID-ORCS; 224650; 1 hit in 78 CRISPR screens.
DR   PRO; PR:P59672; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P59672; protein.
DR   Bgee; ENSMUSG00000024219; Expressed in interventricular septum and 213 other cell types or tissues.
DR   ExpressionAtlas; P59672; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
DR   GO; GO:1901187; P:regulation of ephrin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IDA:UniProtKB.
DR   CDD; cd01274; PTB_Anks; 1.
DR   CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR   CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR   FunFam; 1.25.40.20:FF:000304; Ankyrin repeat and sterile alpha motif domain containing 1A; 1.
DR   FunFam; 2.30.29.30:FF:000045; Ankyrin repeat and sterile alpha motif domain-containing protein 1B; 1.
DR   FunFam; 1.10.150.50:FF:000015; ankyrin repeat and sterile alpha motif domain-containing protein 1B; 1.
DR   FunFam; 1.25.40.20:FF:000099; ankyrin repeat and sterile alpha motif domain-containing protein 1B isoform X5; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR   InterPro; IPR033635; ANKS1/Caskin.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041880; SAM_ANKS1_repeat1.
DR   InterPro; IPR041882; SAM_ANKS1_repeat2.
DR   PANTHER; PTHR24174:SF4; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 1A; 1.
DR   PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00454; SAM; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PDBsum; 5ZRY; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ANK repeat;
KW   Cell projection; Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   CHAIN           2..1150
FT                   /note="Ankyrin repeat and SAM domain-containing protein 1A"
FT                   /id="PRO_0000066922"
FT   REPEAT          75..104
FT                   /note="ANK 1"
FT   REPEAT          108..137
FT                   /note="ANK 2"
FT   REPEAT          165..194
FT                   /note="ANK 3"
FT   REPEAT          198..227
FT                   /note="ANK 4"
FT   REPEAT          231..260
FT                   /note="ANK 5"
FT   REPEAT          263..292
FT                   /note="ANK 6"
FT   DOMAIN          712..778
FT                   /note="SAM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          786..853
FT                   /note="SAM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          952..1107
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   REGION          33..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..51
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..924
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1150
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         335
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         642
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         644
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         663
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         677
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         679
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         693
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92625"
FT   MOD_RES         903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         142..162
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_012704"
FT   VAR_SEQ         1117
FT                   /note="A -> AVPVPPDSRCCHCHTCTTHRPSYLPLPSVSPGVK (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_012705"
FT   VAR_SEQ         1150
FT                   /note="N -> KYETTIF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_012706"
FT   HELIX           712..716
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           717..723
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           727..729
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           730..735
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           741..743
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   TURN            746..748
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           751..756
FT                   /evidence="ECO:0007829|PDB:5ZRY"
FT   HELIX           762..773
FT                   /evidence="ECO:0007829|PDB:5ZRY"
SQ   SEQUENCE   1150 AA;  125242 MW;  551AF44D1DB02D1B CRC64;
     MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGSG SGGGSGGGGL GSSSHPLSSL
     LSMWRGPNVN CVDSTGYTPL HHAALNGHRD VVEVLLRNDA LTNVADSKGC YPLHLAAWKG
     DAQIVRLLIQ QGPSHTRVNE QNALEIRELK KYGPFDPYIN AKNNDNETAL HCAAQYGHTE
     VVKALLEELT DPTMRNNKFE TPLDLAALYG RLEVVKLLLG AHPNLLSCST RKHTPLHLAA
     RNGHKAVVQV LLDAGMDSNY QTEMGSALHE AALFGKTDVV QILLAAGIDV NIKDNRGLTA
     LDTVRDLPSQ KSQQIAALIE DHMTGKRSVK EVDRTSTAQL PLLSNTDAIA PMSQGSMEKT
     VTELILHFDT HADEEGPYEA LYNAVSCHSL DSTASGRSSD RDSMNKEAEA TGTRAAGVRP
     RERPPPPAKP PPDEEEEERV DKKYFPLAAS EGLAVRPRIQ SSAPQEEEEH PYELLLTAET
     KKLGTTDGRT EDHRQSGSGR SQDSVEGQDG QVPEQFSGLL HGSSPVCEVG QDPFQLLTAP
     SQSHPESSQQ DACHEASMQL EEPGVQGTEP PQPGVPDQSK RVGLPAGLTA LASRTYLDAL
     THTVPLRPAG AEEEDQSGPR SRAPPTSKPK AELKLSRSLS KSDSDLLTCS PTEDATMGSR
     SESLSNCSIG KKRLEKSPSF ASEWDEIEKI MSSIGEGIDF SQEQQKISGS RTLEQSVGEW
     LESIGLQQYE SKLLLNGFDD VRFLGSNVME EQDLREIGIS DPQHRRKLLQ AARSLPKVKA
     LGYDGVSPTS VPSWLDSLGL QDYVHSFLSS GYSSIDTVKN LWELELVNVL KVHLLGHRKR
     IIASLADRPY EEPPQKPPRF SQLRCQDLIS QTSSPLSQND SCTGRSADLL LPSADTSRRR
     HDSLPDPGTA SRADRFRVQE EPSETKLTLR PPSLAAPYAP VQSWQHQPEK LIFESCGYEA
     NYLGSMLIKD LRGTESTQDA CAKMRKSTEH MKKIPTIILS ITYKGVKFID ASNKNVIAEH
     EIRNISCAAQ DPEDLCTFAY ITKDLQTSHH YCHVFSTVDV NLTYEIILTL GQAFEVAYQL
     ALQAQKSRTM AASAASMIET KSSKPVPKPR VGMRKSALEP PDSDQEAPSH ASVSWIVDPK
     PDSKRSLSTN
//