AMOL1_BOVIN
ID AMOL1_BOVIN Reviewed; 960 AA.
AC E1BEQ5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Angiomotin-like protein 1;
GN Name=AMOTL1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by NEDD4, leading to proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
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DR EMBL; DAAA02040143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BEQ5; -.
DR SMR; E1BEQ5; -.
DR STRING; 9913.ENSBTAP00000025212; -.
DR PaxDb; E1BEQ5; -.
DR PRIDE; E1BEQ5; -.
DR eggNOG; ENOG502QVI5; Eukaryota.
DR HOGENOM; CLU_009937_1_0_1; -.
DR InParanoid; E1BEQ5; -.
DR OrthoDB; 369983at2759; -.
DR TreeFam; TF333368; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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 Pfam; PF12240; Angiomotin_C; 1.
DR PRINTS; PR01807; ANGIOMOTIN.
PE 3: Inferred from homology;
KW Cell junction; Coiled coil; Phosphoprotein; Reference proteome;
KW Tight junction; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..960
FT /note="Angiomotin-like protein 1"
FT /id="PRO_0000418836"
FT REGION 196..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..281
FT /evidence="ECO:0000255"
FT COILED 440..641
FT /evidence="ECO:0000255"
FT COILED 667..697
FT /evidence="ECO:0000255"
FT COILED 731..761
FT /evidence="ECO:0000255"
FT MOTIF 957..960
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 381..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 906
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY63"
SQ SEQUENCE 960 AA; 106671 MW; E97F6E642EA8C1D8 CRC64;
MLMLHVKRNT CEHTFKCPPP ACYSPSSPVQ ILEDPSYFFP DFQLYPGRHE ASLTVEANSS
IREKVVEDPL CNFHPPNFPR IPEVEMRGSE DAAAGTVLQR LIQEQLRYGT PTENMNLLAI
QHQATGSAGP AHPTNFSSTE NLAQEDPQMV YQSARQEPQG QEHQVDNTVM EKQVRSAQPQ
QNNEELPTYE EAKAQSQFFR GQQPPPPPPQ QQPGAVGHSY YMAGGASQKA RTEGRPTVSR
ANSGQAHKDE ALKELKQGHV RSLSERIMQL SLERNGAKQH LPGPGNGKAF KAGGGPSPAQ
PAAKMLDPRG PPPEYPFKTK QMVSPVSKTQ EHGLFYSDQH PGLLHEMVKP YPAPQPARTE
VAVLRYQPPP EYGVTSRPCQ LPFPSTAQQH SPVSSQNSSV SGPLHSVPLP LAPPMALGAA
PPPPAASPSQ QLGPDAFAIV ERAQQMVEIL TEENRVLHQE LQGYYDNADK LHKFEKELQR
ISEAYESLVK STTKRESLDK AMRNKLEGEI RRLHDFNRDL RDRLETANRQ LSSREYDGHE
DRAAEGLYAS QNKEFLKEKE KLEMELAAVR TASEDHRRHI EILDQALSNA QARVIKLEEE
LREKQAYVEK VEKLQQALTQ LQSACEKREQ MERRLRTWLE RELDALRTQQ KHGNSQPASL
PEYNAPALME LVREKEERIL ALEADMTKWE QKYVEESAIR HFAMSAAATA AAERDTTIVN
HSRNGSYGES SLEAHIWQEE EEVVQATRRC QDMEYTIKNL HAKIIEKDAM IKVLQQRSRK
DAGKTDSSSL RPARSVPSIA AATGTHSRQT SLTSSQLAEE RKEEKTWKGS IATGLLLGKE
HNDHASTPLL PTPSAATLSP PTPGTSASSA HAKTGSKDSS TQTDKSAELF WPGVASLPTR
SRLSGTPSNS PVLKHPAAKG TAEKLENSPG HGKSPDHKGR VSNLLHKPEF PDGEMMEVLI
