AMOL2_BOVIN
ID AMOL2_BOVIN Reviewed; 766 AA.
AC F1MRK3; Q0V8J3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 3.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Angiomotin-like protein 2;
GN Name=AMOTL2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-579.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Regulates the translocation of phosphorylated SRC to
CC peripheral cell-matrix adhesion sites. Required for proper architecture
CC of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway,
CC probably by recruiting CTNNB1 to recycling endosomes and hence
CC preventing its translocation to the nucleus. Participates in
CC angiogenesis. May play a role in the polarity, proliferation and
CC migration of endothelial cells. Selectively promotes FGF-induced MAPK
CC activation through SRC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SRC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-107 is necessary for efficient binding to
CC SRC and synergistically functioning with SRC to activate the downstream
CC MAPK pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the angiomotin family. {ECO:0000305}.
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DR EMBL; DAAA02003049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT026225; ABG67064.1; -; mRNA.
DR RefSeq; XP_010799902.1; XM_010801600.2.
DR RefSeq; XP_010822763.2; XM_010824461.2.
DR AlphaFoldDB; F1MRK3; -.
DR SMR; F1MRK3; -.
DR STRING; 9913.ENSBTAP00000000988; -.
DR PaxDb; F1MRK3; -.
DR PRIDE; F1MRK3; -.
DR Ensembl; ENSBTAT00000000988; ENSBTAP00000000988; ENSBTAG00000000742.
DR Ensembl; ENSBTAT00000077451; ENSBTAP00000060697; ENSBTAG00000000742.
DR GeneID; 538514; -.
DR KEGG; bta:538514; -.
DR CTD; 51421; -.
DR VEuPathDB; HostDB:ENSBTAG00000000742; -.
DR VGNC; VGNC:25872; AMOTL2.
DR eggNOG; ENOG502QR7W; Eukaryota.
DR GeneTree; ENSGT00940000156577; -.
DR HOGENOM; CLU_009937_2_0_1; -.
DR InParanoid; F1MRK3; -.
DR OMA; YRFYQPQ; -.
DR OrthoDB; 369983at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000000742; Expressed in omental fat pad and 103 other tissues.
DR ExpressionAtlas; F1MRK3; baseline.
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:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Coiled coil; Endosome; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..766
FT /note="Angiomotin-like protein 2"
FT /id="PRO_0000418837"
FT REGION 64..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..575
FT /evidence="ECO:0000255"
FT MOTIF 763..766
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphotyrosine; by FGFR1"
FT /evidence="ECO:0000250"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J4"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K371"
SQ SEQUENCE 766 AA; 84727 MW; 60083B4F8CA40B39 CRC64;
MRTLEDSSGT VLHRLIQEQL RYGNLTETRT LLAIQQQALR GGAGAGGTGS PQAPMEIMAP
EDSQVLQQAT RQEPQGQEHQ GTETHLAENG LYRLCPQPGK GEELPTYEEA KAHSQYYASQ
QAGPWPHVGD RDPRGPPGGS RRQDEALREL RHGHVRSLSE RLLQLSLERN GARTPSHMSA
SHSFPQLARN QQGPPARGAP TAEGPEPRGP PPQYPHVMLA HETTSAVTDP RYRARGSPHF
QHAEVRILQA QVPPVFLPQQ QQQYQYLQQP QERHPPPHLA ALSPPGVEGP ASTQASLATS
GSTHLAQMET VLRENARLQR DNERLQRELE STAEKAGRIE KLESEIQRLS EAHESLTRAS
SKREALEKTM RNKMDSEMRR LQDFNRDLRE RLESANRRLA SKTQEAQAGS QDMVAKLLAQ
SYEQQQEQEK LEREMALLRG AIEDQRRRAE LLEQALSNAQ GRAARAEEEL RKKQAYVEKV
ERLQQALGQL QAACEKREQL ELRLRTRLEQ ELKALRAQQR QAGTPGGGGG SGGTPELSAL
RLSEQLREKE EQVLALEADM TKWEQKYLEE RAMRQFAMDA AATAAAQRDT TLIRHSPQPS
PSSSFNEGLL TGGHRHQEME SRLKVLHAQI LEKDAVIKVL QQRSRKDPGK VTPGSLRPAK
SVPSIFVAAA AGTQGWQGHS SSERQVDASA QLAADRAPLE EPVAVAPLAA HAKHGSRDGS
TQTDGPPDSL EPDSLLGCSS GQRTASLDSI ATSRVQDFSD MVEILI
