AMOL2_RAT
ID AMOL2_RAT Reviewed; 773 AA.
AC G3V735;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Angiomotin-like protein 2;
GN Name=Amotl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH473954; EDL77397.1; -; Genomic_DNA.
DR RefSeq; NP_113905.1; NM_031717.1.
DR AlphaFoldDB; G3V735; -.
DR SMR; G3V735; -.
DR STRING; 10116.ENSRNOP00000011347; -.
DR PaxDb; G3V735; -.
DR PRIDE; G3V735; -.
DR Ensembl; ENSRNOT00000011347; ENSRNOP00000011347; ENSRNOG00000008487.
DR GeneID; 65157; -.
DR KEGG; rno:65157; -.
DR CTD; 51421; -.
DR RGD; 70977; Amotl2.
DR eggNOG; ENOG502QR7W; Eukaryota.
DR GeneTree; ENSGT00940000156577; -.
DR HOGENOM; CLU_009937_2_0_1; -.
DR InParanoid; G3V735; -.
DR Reactome; R-RNO-2028269; Signaling by Hippo.
DR PRO; PR:G3V735; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000008487; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; G3V735; baseline and differential.
DR Genevisible; G3V735; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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 Coiled coil; Endosome; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..773
FT /note="Angiomotin-like protein 2"
FT /id="PRO_0000418838"
FT REGION 41..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..577
FT /evidence="ECO:0000255"
FT MOTIF 770..773
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..754
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 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2J4"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K371"
SQ SEQUENCE 773 AA; 85587 MW; 9F4E80FCD2E3ABA9 CRC64;
MRTLEDSSGT VLHRLIQEQL RYGNLTETRT LLAIQQQALR GGAGAGGTGS PQASLEIGAP
EDSQVLQQAT RQEPQGQEHQ GGETHLAENR LYRLCPQPSK GEELPTYEEA KAHSQYYAAQ
QAGSRLHGGD RDPRGASGGS RRQDEALREL RHGHVRSLSE RLLQLSLERN GARVPSHMSS
SHSFPQLARS QQGPQPRGPP AEGPEPRGPP PQYPHAVMAQ ETAAVNDPRY RPRSSPHFQH
AEVRILQAQV PPVFLQQQQY QYLQQPQEHS PPLHPAALGH GPPSSFSPPA LEGPPGAQAT
SGSAHLAQME SVLRENARLQ RDNERLQREL ESTSEKASCI EKLENEIQRL SEAHESLMRT
SSKREALEKT MRNKMDSEMR RLQDFNRDLR ERLESANRHL ASKTQEAQAG SQDMVAKLLA
QSYEQQQEQE KLEREMALLR GAIEDQRRRA ELLEQALGNA QSRAARAEEE LRKKQAYVEK
VERLQQALGQ LQAACEKREQ LELRLRTRLE QELKALRAQQ RQTGTLTGGG GSHTGSTELS
ALRLSEQLRE KEEQILALEA DMTKWEQKYL EERAMRQFAM DAAATAAAQR DTTLIRHSPQ
PSPSSSFNEG LLAGNHRHQE MESRLKVLHA QILEKDAVIK VLQQRSRKDP GKATQGTLRP
AKSVPSIFAA AVGTQGWQGF STSERQTDAP ARQTVDRGPA EEPPATPPLP AHTKHGSRDG
STQTDGPADS TSACLASEPD SLLGCNGSQR TTSLDSIAAT RVQDLSDMVE ILI
