ID A0A3P8T2A2_AMPPE Unreviewed; 1414 AA.
AC A0A3P8T2A2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Rho guanine nucleotide exchange factor (GEF) 12a {ECO:0000313|Ensembl:ENSAPEP00000018368.1};
GN Name=ARHGEF12 {ECO:0000313|Ensembl:ENSAPEP00000018368.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000018368.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000018368.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000018368.1}
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; ENSAPET00000018877.1; ENSAPEP00000018368.1; ENSAPEG00000013091.1.
DR GeneTree; ENSGT00940000157662; -.
DR OMA; TVSDQRW; -.
DR Proteomes; UP000265080; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080}.
FT DOMAIN 54..131
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 772..961
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1003..1116
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1414 AA; 157728 MW; 8D87006F4F7CB1B5 CRC64;
MSDTQSSFTD RFPKKANRTS SILSKDHPPD KKPKSDKTSL PSNEFDPTGL VQRCVIIQKD
ENGFGLTVSG DNPVFVQLVK EDGAAMRAGV QTGDRIIKVN GTLVTHSNHI EVVKLIKSGS
YVALTVLGRP PGLAQIPLPE AEPEMLGVSI SSPNSPAAER PYSPQDRLSS AHSPWDENSV
CNQKADILQK MLSKEQQELQ AMKEEYSRNP SPKLLKDIQE AKKHIPQLQG QLFRVTGTTQ
EAVPGGEADD GSMLETERTF AMKGDNSTDL SWTSSPISRI FGPGSPDSQC PRDSSCPSPK
STPRNSFNSC HSPETEDTTD LDSLSPTTVS SPSSSRLVSQ IIGAEDDYFD SDQEQTNGQC
NSFNSIEQLK SRPAHLAAFL HHVISQFDPA PVLCYLYADL YKQTNSKETR RVFMDLHTFF
IDRGANLKVA VPESVSSDLD RRRTELIPEE INRQHVQTLQ DSLLPDIQRN LEDFRQKRSM
GLTVAEVELA RLDQERVRDR VTLERERSYA ENIITKIEDI LLTTQTAEEE KCTTMQYVIY
TYMKHLGVRV KEPRSLESKR VRISFLPKIK KSIKTEKEGE EKVKKPRFPS ILGPQRRPSR
NEAASVSKAL DGRPRPQKQL SQPTLGASEH METGHLRGSQ SSEGSELTHS MSVNASSPNS
AFYSTESSRD ADIGGTPTSG PSRLSDGLQS DPLDGFSSHF DLYSLDQLQE DDRESDRAHE
GTPKAIRRLE GLGAADVQSE DDQGTDSEHD PPNWQQLVGR EVLAGLRPHE IKRQEVINEL
FYTERAHVRM LKVLDHVFYQ KLSKEAILPP ADIKNIFTNL EEILQLHVSI LEQMAAIRKR
NESSVIDQIG DDLLSWFGSG EEEKIKQAVG TFCSNQPFAL EIIKTKKKDS RFTSFIQEAE
SNRLCRRLQL KDLIPIEMQR LTKYPLLLDN IVKYTDNAVE KDKVKQAADC CRKILSHVNQ
AVKESEDKQR LEDYQRRLDL SSLKQTDNPM ILELKNLDLT KRTMVHEGPL SWKVNKDKTI
ELYTLLLEDI LVLLQKQDER LILKCHSKNL AGTADTKHIF SPIIKLNTVL VRSVATDNKS
FFVLSMSDNG AQIYELMAPT VSDQRTWQRL ITQRADAMKV KPHSVIPLPQ TDGERDGVEI
ITAGVSRLSR DPDRTSTGST QSTDKESGPA CRSALQTSLP GSNPFEGVKA EEEEEEGFVD
PELPYQVAED GREGDSFSMF PLRADEALKT LAALKQVLVT QLMSQEAAEQ TKRSTGARLL
RTTSLRTPID SRARVMVHNG SEKNSSQTED LAQDLGSGDT GFFDSPEDYA GYLVLEGYGG
PGESSTDDDI LASTTGKQLR TSQGCAADSG INLRFSSTSQ AGSLSSFSRQ VLSHLRNLQA
NLNYLKEVEA KYNNLIHQRP ERSAADTDGN KDKR
//