ID A0A3B3VQD2_9TELE Unreviewed; 1152 AA.
AC A0A3B3VQD2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|Ensembl:ENSPLAP00000027029.1};
GN Name=ARHGEF12 {ECO:0000313|Ensembl:ENSPLAP00000027029.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000027029.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000027029.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3B3VQD2; -.
DR Ensembl; ENSPLAT00000019652.1; ENSPLAP00000027029.1; ENSPLAG00000015394.1.
DR GeneTree; ENSGT00940000157662; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
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; PF17820; PDZ_6; 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; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 60..95
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 522..711
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 128906 MW; 00FFD298D8A4B6B8 CRC64;
MSDPQFSSTD ILSKDHPPDK KPKSDKASLS SNEFDPTALV VEKSGNNSVL AEGKPESCGA
AMRAGVQTGD RIIKVNGTLV THSNHTEVVK LIKGSYVALT VLGRPPGLAQ IPLPEAEPDI
LGVSLSSPNS PATERPYSPQ DRLSPFQPSW PATPESHCPK ELSYPSPKST PRNSFNSCHS
PETEDTTDLD SLSPPALSSP SSSRVISQII GAEDDYFGRD QEQTNGQCDS FNSIEQLKSR
PAHLAAFLHY VISQFEPAPV LCYLYTELYK QTNSKETRRV FMDLHTFFMD RGAVPVPESV
SSDLRWRGEV HTAEINRQHV QTLQDSLLAD VEKHLEDFQK RNMGLTVAEA ELARLDQERV
RDRVTLERER SYAENIISKI DDVLTTQTTE EDKSTIQFVI YTYMKHLGVR VKEPRNLESK
RGLNRLFPKM KPQKQLSQPT LGAVELMDSS RLRGSQSSEG PELTHSLSVS SPSNTTYSVE
ANRDADIDVQ SEDDQGTDSE LHNWQQLVGR EVLAGLRPQE IKRQEVINEL FYTERAHVGM
LKVLDDVFYQ RLSKDAILPP ADIKNIFTNL EEVLQLHSIL EQMTAIRKRN DLLVIDLRGD
DLLSWFSGAE EEKIKQAVGT FCSNQPFALE IIKTKQKKDS RFTSFIQEAE SNRQCRRLQL
KDIIPVEMLR LTKYPLLLDN IVRYTDDPVE KHKVKQAADC CRKILSHVNQ ALKESEDKQK
LEDYQRRLDL SSLKQTDNPV ILELKNLDLT KKTLIHEGPL SWKMNKDKTI LYTLLLEDIL
VLLQKQDERL ILKCHSKILA GTPDTKHTFS PIIKLNTVLV RSVATNKSFF VLSMSDNVAQ
IYELMAPTVS DQKWQTLISQ RADTMKVKPH SIIPLPQTGE RDGVEIITAG VSRLSRERDR
TSTGSTQSTK ESGPASRSTL QGSLPASNPF EEGKADVEEE EGFLDPELSC EVSEVDREGD
SFDVFPSRAD EALKTAALKQ VLVNQLMSQE AAQQTKRSTG VRLLRTTSLR TPTDNRAKVM
VHNGSEKSSS KTEDLAQDLG SGDTGFFDSP EDYLDGYGGQ GESSTDGDIL ASAEGKQLRT
SQGCAADSGI NLRFSSTSQF GSLSTFSRQV LSHLRHLQTS LGYLKEVETK YNNLIRQRTD
RPSTDTDGNK LR
//
