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Database: UniProt
Entry: A0A493T424_ANAPP
LinkDB: A0A493T424_ANAPP
Original site: A0A493T424_ANAPP 
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
//
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