ID   AMOL1_HUMAN             Reviewed;         956 AA.
AC   Q8IY63; Q63HK7; Q8NDN0; Q8TEN8; Q8WXD1; Q96CM5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Angiomotin-like protein 1;
GN   Name=AMOTL1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skeletal muscle, and Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle, and Skin;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-557 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12406577; DOI=10.1016/s0378-1119(02)00928-9;
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA   Holmgren L.;
RT   "Angiomotin belongs to a novel protein family with conserved coiled-coil
RT   and PDZ binding domains.";
RL   Gene 298:69-77(2002).
RN   [6]
RP   ERRATUM OF PUBMED:12406577.
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R., Van Meir E.G.,
RA   Holmgren L.;
RL   Gene 310:231-231(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-295; SER-720 AND
RP   SER-906, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [10]
RP   UBIQUITINATION BY NEDD4.
RX   PubMed=22385262; DOI=10.1042/bj20111983;
RA   Wang C., An J., Zhang P., Xu C., Gao K., Wu D., Wang D., Yu H., Liu J.O.,
RA   Yu L.;
RT   "The Nedd4-like ubiquitin E3 ligases target angiomotin/p130 to ubiquitin-
RT   dependent degradation.";
RL   Biochem. J. 444:279-289(2012).
RN   [11]
RP   FUNCTION.
RX   PubMed=22362771; DOI=10.1074/jbc.m112.347419;
RA   Li Z., Wang Y., Zhang M., Xu P., Huang H., Wu D., Meng A.;
RT   "The Amotl2 gene inhibits Wnt/beta-catenin signaling and regulates
RT   embryonic development in zebrafish.";
RL   J. Biol. Chem. 287:13005-13015(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-295; SER-793;
RP   SER-805; SER-828; SER-900; THR-902 AND SER-906, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-805; SER-828 AND SER-906, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Inhibits the Wnt/beta-catenin signaling pathway, probably by
CC       recruiting CTNNB1 to recycling endosomes and hence preventing its
CC       translocation to the nucleus. {ECO:0000269|PubMed:22362771}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IY63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IY63-2; Sequence=VSP_015710;
CC   -!- PTM: Polyubiquitinated by NEDD4, leading to proteasomal degradation.
CC       {ECO:0000269|PubMed:22385262}.
CC   -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB84910.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB84910.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK074084; BAB84910.1; ALT_SEQ; mRNA.
DR   EMBL; AL833833; CAD38693.1; -; mRNA.
DR   EMBL; AP001152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX648729; CAH56180.1; -; mRNA.
DR   EMBL; BC014126; AAH14126.1; -; mRNA.
DR   EMBL; BC037539; AAH37539.1; -; mRNA.
DR   EMBL; AF453742; AAL49764.1; -; mRNA.
DR   CCDS; CCDS44712.1; -. [Q8IY63-1]
DR   CCDS; CCDS73368.1; -. [Q8IY63-2]
DR   RefSeq; NP_001287936.1; NM_001301007.1. [Q8IY63-2]
DR   RefSeq; NP_570899.1; NM_130847.2. [Q8IY63-1]
DR   AlphaFoldDB; Q8IY63; -.
DR   SMR; Q8IY63; -.
DR   BioGRID; 127559; 93.
DR   CORUM; Q8IY63; -.
DR   DIP; DIP-50682N; -.
DR   IntAct; Q8IY63; 28.
DR   MINT; Q8IY63; -.
DR   STRING; 9606.ENSP00000387739; -.
DR   iPTMnet; Q8IY63; -.
DR   PhosphoSitePlus; Q8IY63; -.
DR   BioMuta; AMOTL1; -.
DR   DMDM; 74728292; -.
DR   EPD; Q8IY63; -.
DR   jPOST; Q8IY63; -.
DR   MassIVE; Q8IY63; -.
DR   MaxQB; Q8IY63; -.
DR   PaxDb; 9606-ENSP00000387739; -.
DR   PeptideAtlas; Q8IY63; -.
DR   ProteomicsDB; 71115; -. [Q8IY63-1]
DR   ProteomicsDB; 71116; -. [Q8IY63-2]
DR   Pumba; Q8IY63; -.
DR   Antibodypedia; 654; 149 antibodies from 26 providers.
DR   DNASU; 154810; -.
DR   Ensembl; ENST00000317829.12; ENSP00000320968.8; ENSG00000166025.18. [Q8IY63-2]
DR   Ensembl; ENST00000433060.3; ENSP00000387739.2; ENSG00000166025.18. [Q8IY63-1]
DR   GeneID; 154810; -.
DR   KEGG; hsa:154810; -.
DR   MANE-Select; ENST00000433060.3; ENSP00000387739.2; NM_130847.3; NP_570899.1.
DR   UCSC; uc001pfb.4; human. [Q8IY63-1]
DR   AGR; HGNC:17811; -.
DR   CTD; 154810; -.
DR   DisGeNET; 154810; -.
DR   GeneCards; AMOTL1; -.
DR   HGNC; HGNC:17811; AMOTL1.
DR   HPA; ENSG00000166025; Tissue enhanced (skeletal).
DR   MIM; 614657; gene.
DR   neXtProt; NX_Q8IY63; -.
DR   OpenTargets; ENSG00000166025; -.
DR   PharmGKB; PA24774; -.
DR   VEuPathDB; HostDB:ENSG00000166025; -.
DR   eggNOG; ENOG502QVI5; Eukaryota.
DR   GeneTree; ENSGT00940000160158; -.
DR   HOGENOM; CLU_009937_1_0_1; -.
DR   InParanoid; Q8IY63; -.
DR   OMA; GMPEYNA; -.
DR   OrthoDB; 4175527at2759; -.
DR   PhylomeDB; Q8IY63; -.
DR   TreeFam; TF333368; -.
DR   PathwayCommons; Q8IY63; -.
DR   Reactome; R-HSA-2028269; Signaling by Hippo.
DR   SignaLink; Q8IY63; -.
DR   SIGNOR; Q8IY63; -.
DR   BioGRID-ORCS; 154810; 14 hits in 1159 CRISPR screens.
DR   ChiTaRS; AMOTL1; human.
DR   GeneWiki; AMOTL1; -.
DR   GenomeRNAi; 154810; -.
DR   Pharos; Q8IY63; Tbio.
DR   PRO; PR:Q8IY63; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8IY63; Protein.
DR   Bgee; ENSG00000166025; Expressed in tibialis anterior and 190 other cell types or tissues.
DR   ExpressionAtlas; Q8IY63; baseline and differential.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR   GO; GO:0003365; P:establishment of cell polarity involved in ameboidal cell migration; IBA:GO_Central.
DR   GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR   GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR009114; Angiomotin.
DR   InterPro; IPR024646; Angiomotin_C.
DR   PANTHER; PTHR14826; ANGIOMOTIN; 1.
DR   PANTHER; PTHR14826:SF12; ANGIOMOTIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF12240; Angiomotin_C; 1.
DR   PRINTS; PR01807; ANGIOMOTIN.
DR   Genevisible; Q8IY63; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Phosphoprotein;
KW   Reference proteome; Tight junction; Ubl conjugation; Wnt signaling pathway.
FT   CHAIN           1..956
FT                   /note="Angiomotin-like protein 1"
FT                   /id="PRO_0000190670"
FT   REGION          197..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          259..279
FT                   /evidence="ECO:0000255"
FT   COILED          438..639
FT                   /evidence="ECO:0000255"
FT   COILED          665..694
FT                   /evidence="ECO:0000255"
FT   COILED          729..762
FT                   /evidence="ECO:0000255"
FT   MOTIF           953..956
FT                   /note="PDZ-binding"
FT   COMPBIAS        197..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..427
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         269
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         793
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         828
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         900
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         902
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         906
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         17..66
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_015710"
FT   VARIANT         847
FT                   /note="P -> L (in dbSNP:rs11020968)"
FT                   /id="VAR_033498"
FT   CONFLICT        459..460
FT                   /note="LQ -> HE (in Ref. 4; AAH14126)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        649
FT                   /note="K -> E (in Ref. 2; CAH56180)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   956 AA;  106574 MW;  6F47AE3A13816E95 CRC64;
     MWRAKLRRGT CEPAVKGSPS ACYSPSSPVQ VLEDSTYFSP DFQLYSGRHE TSALTVEATS
     SIREKVVEDP LCNFHSPNFL RISEVEMRGS EDAAAGTVLQ RLIQEQLRYG TPTENMNLLA
     IQHQATGSAG PAHPTNNFSS TENLTQEDPQ MVYQSARQEP QGQEHQVDNT VMEKQVRSTQ
     PQQNNEELPT YEEAKAQSQF FRGQQQQQQQ QGAVGHGYYM AGGTSQKSRT EGRPTVNRAN
     SGQAHKDEAL KELKQGHVRS LSERIMQLSL ERNGAKQHLP GSGNGKGFKV GGGPSPAQPA
     GKVLDPRGPP PEYPFKTKQM MSPVSKTQEH GLFYGDQHPG MLHEMVKPYP APQPVRTDVA
     VLRYQPPPEY GVTSRPCQLP FPSTMQQHSP MSSQTSSASG PLHSVSLPLP LPMALGAPQP
     PPAASPSQQL GPDAFAIVER AQQMVEILTE ENRVLHQELQ GYYDNADKLH KFEKELQRIS
     EAYESLVKST TKRESLDKAM RNKLEGEIRR LHDFNRDLRD RLETANRQLS SREYEGHEDK
     AAEGHYASQN KEFLKEKEKL EMELAAVRTA SEDHRRHIEI LDQALSNAQA RVIKLEEELR
     EKQAYVEKVE KLQQALTQLQ SACEKREQME RRLRTWLERE LDALRTQQKH GNGQPANMPE
     YNAPALLELV REKEERILAL EADMTKWEQK YLEESTIRHF AMNAAATAAA ERDTTIINHS
     RNGSYGESSL EAHIWQEEEE VVQANRRCQD MEYTIKNLHA KIIEKDAMIK VLQQRSRKDA
     GKTDSSSLRP ARSVPSIAAA TGTHSRQTSL TSSQLAEEKK EEKTWKGSIG LLLGKEHHEH
     ASAPLLPPPP TSALSSIAST TAASSAHAKT GSKDSSTQTD KSAELFWPSM ASLPSRGRLS
     TTPAHSPVLK HPAAKGTAEK LENSPGHGKS PDHRGRVSSL LHKPEFPDGE MMEVLI
//