ID A0A493T424_ANAPP Unreviewed; 1526 AA.
AC A0A493T424;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|Ensembl:ENSAPLP00000020674.1};
GN Name=ARHGEF12 {ECO:0000313|Ensembl:ENSAPLP00000020674.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000020674.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000020674.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000020674.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR Ensembl; ENSAPLT00000034405.1; ENSAPLP00000020674.1; ENSAPLG00000014925.2.
DR GeneTree; ENSGT00940000157662; -.
DR Proteomes; UP000016666; Chromosome 25.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13390; PH_LARG; 1.
DR CDD; cd08754; RGS_LARG; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR037801; ARHGEF12_PH.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR037884; LARG_RGS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF3; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 12; 1.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 54..118
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 765..955
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 997..1110
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..234
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1481..1511
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1526 AA; 171091 MW; CF1F156B88F7C7B2 CRC64;
MSGTQSTITD RFPLKKPTRH GSILSRESPA DKKQKVERCS STHDFDPTGL VQRCVIIQRD
ENGFGLTVSG DNPVFVQSVK EDGAAMRAGV QTGDRIIKVN GTLVTHSNHL EVVKLIKSGS
YVALTVQGRP PGSPQIPLAE SEVDLAAFGH MCPVMTSPHS PGTSGNTERI TSPVLMGEEN
NIVHNQKVEI LRKMLQKEQE RLQSLQEEYS RSSSSRLLKE IQETKKHITQ LQEQLSKATG
CTQDGVLSSR SVTESLQISE VEAESGDGLC KLDYSSDSPS RPNSDIADSP RSGLKERVYL
DESPEKTEVQ DTDSQSSVGS PSSRIGPQII GAEDDDFDTE QEQINGQCSC FQNIELLKSR
PAHLAVLLHH VVSQFDPAAL LCYLYTDLYK QTNSKETRRV FLEFYQFFLD RTANLKVPVP
DEISVDLDKR RPELIPEELH RHYIQTMQDK VCPEVQRNLE DFRQKRSMGL TLAEGELTKL
DAERVRDRNA VEKERACAEQ IIAKIEEVLM TSQPLEEEKS STMQYVILTY MKHLGVKVKE
PRNLEQKRGR IGFLPKIKQS IKKEKEGDEK GKRRGFPNIL GPPRRPSRHD SSAIGRAMEM
QKQRHPKHLP TASSVSPEPP DSGKMRQSGS SSDGTDAPYA PANPMSPLAT GPFSSPEGSK
DSEAGSKQTG EAPPANDCVD GTPRTPNNTF EFLSPLENLP EEEGESERVV DMGTPKPFRK
MDSVGFADVQ SEDELYDFDT DMDPPNWQQL VSREVLMGLK PYEIKRQEVI NELFYTERAH
VRTLKVLHNV FYQRVTREGI LNSSDKRKIF SNLEDILGLH VALNDQMKAV RKRNETSVID
QIGEDLLSWF SGAAEEKIKH ATATFCSNQP FALEVIKSRQ KKDSRFQTFV QDAESNPLCR
RLQLKDIIPT EMQRLTKYPL LLDNIAKYTE LPEEKEKVKK AADHCRQVLN HVNQAVKESE
NKQHLEDYQR RLDLSYLKQS EDPMMDEFRN LDLTKRKMLH EGPLTWKVNR DKTIDLYTLL
LEDILVLLQK QDDKLVLKCH SKILASTADS KHTFSPVIKL NTVLVRQVAT DNKAFFVISM
SENGAHIYEL VAQTVSEKNV WQDLIAQMAG TVKMESTRRV IPLPQSGPGE EEREEEEQQK
LKEQHDIPAS SLQSPDKDLG LDSSLILNAQ TSSPTMSEKS EVESLLVTER QFDKVQQADL
TLKDTSTCYE HAATDLPSVP GGQWALDALR NLDLLKKLLV QQLGFSEKGT LEDRQRFPRF
RTVSQEAQTG SGSELGLQHS DDSKFHQPGT DRMLPRTETH ESTASYGLRT SAESPASGDA
MQLIGRDPRS SSNSAIDRMS MNLEISTAEL EGVGADESGE HFFDAREAHS DENPSESELM
ERKEDEDVQI RISGNYLILD GYGTVQESST DEEVSSLVLQ CTAGGHTSLD SAQQQPLSPR
DTQSDGGSSP FAEEMLVSRW GGVEESCSVV ASPHFLSLES RVQMMQYIQK IENNLEKLKE
VEEDYIILRR QGLAGSASTG EHSEKS
//