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 27-MAR-2024, entry version 166.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 1A;
DE AltName: Full=Odin {ECO:0000303|PubMed:29749928};
GN Name=Anks1a; 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, Pancreas,
RC 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 PDBsum; 5ZRY; -.
DR AlphaFoldDB; P59672; -.
DR SMR; P59672; -.
DR BioGRID; 230297; 2.
DR IntAct; P59672; 2.
DR MINT; P59672; -.
DR STRING; 10090.ENSMUSP00000025058; -.
DR iPTMnet; P59672; -.
DR PhosphoSitePlus; P59672; -.
DR EPD; P59672; -.
DR jPOST; P59672; -.
DR MaxQB; P59672; -.
DR PaxDb; 10090-ENSMUSP00000110491; -.
DR PeptideAtlas; P59672; -.
DR ProteomicsDB; 282005; -. [P59672-1]
DR ProteomicsDB; 282006; -. [P59672-2]
DR Pumba; P59672; -.
DR Antibodypedia; 29433; 128 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; REGWSEC; -.
DR OrthoDB; 25046at2759; -.
DR TreeFam; TF320582; -.
DR BioGRID-ORCS; 224650; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Anks1; mouse.
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 Genevisible; P59672; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 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.
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 426..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..924
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 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
//
