ID A0A3Q3LKH5_9TELE Unreviewed; 1417 AA.
AC A0A3Q3LKH5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Rho guanine nucleotide exchange factor (GEF) 12a {ECO:0000313|Ensembl:ENSMAMP00000014648.1};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000014648.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000014648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR Ensembl; ENSMAMT00000015054.2; ENSMAMP00000014648.1; ENSMAMG00000009909.2.
DR GeneTree; ENSGT00940000157662; -.
DR Proteomes; UP000261640; Unplaced.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640}.
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 147..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1417
FT /note="Disordered"
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 609..682
FT /note="Polar 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 1417 AA; 158540 MW; 0C1B9AF7945FB9C9 CRC64;
MSDTQSSFTD RFPKKVIRTS SILSKDHPPD KKPKSDKTSL PSNEFDPTGL VQRCVIIQKD
KNGFGLTVSG DNPVFVQLVK EDGAAMRAGV QTGDRIIKVN GTLVTHSNHI EVVKLIKSGS
YVALTVLGRP PGLAQIPLSE AESEMLDVSI SSPNSPAAER PYSPQDRLSS THPPWDENSS
VSNQKVDMLQ KMLSKEQLEL QAMKEEYNRN PSPKLLKDIQ ETKKHIPQLQ GQLFKATGTT
QEAVSGGDAD DGCMFETEHR LASKGNNSTD LSWSSTPISR GFGSPQSLCP RESSLPSPKS
TPRNSFNSCH SPEAEDTTDL DSLSPTTISS PVTRLATHII GAEDDYFDSD QEQTNGQCNS
FNSIEQLKSR PAHLAAFLHH VISQFDPAPV LCYLYADLYK QTNSKETRRV FMYLHTFFID
RGANLKVAVP ESVSADLDRR RTELIPEEIN RQHVQTLQDS LLPDIHKNLE DFRQKRSMGL
TVAEVELSRL DQERVRDRVT LERERSYAEN IITKIFDILL TTQTTEEEKC TTMQYVIYTY
MKHLGVRVKE PRSLESKRVW NFLPKMKKSI KTEKEGEEKV KKPRFPSILG PQRRPSRIEA
GTVGKSLDSR PRPQKQLSQP TLGASEQMDS GRLRGSQSSE GSELTHFMSF STSSPNSATY
SSDTSRDPDI SGTPTSCPPR LSDGLQSDPL DGLLYPASHL DLYSLDQLQE EDRESDRAHE
GTPKILRRLE GLGAVDVQSE DDQGTDSEHD PPNWQQLVGR EVLAGLRPHE IKRQEVINEL
FYTERAHVRM LRVLDNVFYQ KLSKEAILPP ADIKNIFTNL EEILQLHVSI LEQMAAVRKR
NESSVIDQIG DDLLSWFSIE EEKIKQAVGT FCSNQPFALE IIKTKQKKDS RFTSFIQEAE
SNRLCRRLQL KDIIPVEMQR LTKYPLLLDN IAKYTDNAVE KDKVKQAADC CRKILNHVNQ
AVKESEDKQR LEDYQRRLDL SSLKQTDNPM ILELKNLDLT KRTMVHEGPL SWKVNKDKTI
ELYTLLLEDI LVLLQKQDER LILKCHSKNL AGSADTKHIF SPIIKLNTVL VRSVATDNKS
FFVLSMSDNG AQIYELMAPT VSDQRTWQRL ITQRADAMKV KPHSIIPLPQ TDGERDGVEI
ITAGVSRLSR DPDHTSSGST QSMDKVSSLA SRSAMQSSLP GNNPFEGVKA DEEEEEEGFV
DPELPYPVTE DGREGDSFNT FPSRADEALK TLAALKQVLV TQLMSQEAAE QTKRSTGGRL
LRTTSLRTPV DSHARVMVHN GSEKNSSQTE DPVQDLGSGD TGFFDSPEDY AGYLVLEGYG
GPGESSTDDD ILASTTGKQL STSQGCAADS GINLRFSSTS QAGSLSSFSR QVLSHLRNLQ
ANLNYLKEIE AKYNNLQTVR QRPERSAADS DGSKDKR
//
