ID A0A3B3YDZ6_9TELE Unreviewed; 1408 AA.
AC A0A3B3YDZ6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rho guanine nucleotide exchange factor (GEF) 12a {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000025581.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000025581.1}
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 RefSeq; XP_014845665.1; XM_014990179.1.
DR Ensembl; ENSPMET00000004741.1; ENSPMEP00000025581.1; ENSPMEG00000008724.1.
DR GeneID; 106919658; -.
DR CTD; 562455; -.
DR OrthoDB; 2875542at2759; -.
DR Proteomes; UP000261480; 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}.
FT DOMAIN 54..131
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 766..956
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 998..1111
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..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1408
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 230..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1408 AA; 157551 MW; 274BB1CC97F7040D CRC64;
MSDPQFSSTD RFTKKATRTS SILSKDHPPD KKPKSDKASI PSNEFDPTGL VQRCVIIQKD
ENGFGLTVSG DNPVFVQLVK EDGAAMRAGV QTGDRIIKVN GTLVTHSNHT EVVKLIKSGS
YVALTVLGRP PGLAQIPLPE ADPDILGVSL SSPNSPATER PYNPQDRLSP FQPSWEENGS
ACKQRTDVLQ KKLSKEQQDL QAMKEEYSRN PSPKLLKDIQ EAKKHIPQLQ GQLLKSTETT
QEAVSGGDAD DSSTYETDRA LTPKADSSTD LSWSSTPIFR PATPESHCPK ELSYPSPKST
PRNSFNSCHS PETEDTTDLD SLSPPALSSP SSSRVISQII GAEDDYFGRD QEQTNGQCDS
FNSIEQLKSR PAHLAAFLHY VISQFEPAPV LCYLYTELYK QTNSKETRRV FMDLHTFFMD
RGANLKVPVP ESVSSDLDRR RTELIPEEIN RQHVQTLQDS LLADVEKHLE DFRQKRNMGL
TVAEAELARL DQERVRDRVT LERERSYAEN IISKIDDILL TTQTTEEDKC STIQFVIYTY
MKHLGVRVKE PRNLESKRGL NRLFPKMKKS IKTDKEVDDR LKKKFLNLVP QRRPSRIEAA
GKNPENRPRP QKQLSQPTLG AVELMDSSRL RGSQSSEGPE LTHSLSVSSP SNTTYSAEAN
RDADIVSGGT PTSAPSRLSD GLQPDPLDGL AFPDSTELYH MEKLQEDDRE SDRAHDGTPK
AVRRLEPLGI GDVQSEDDQG TDSELHNWQQ LVGREVLAGL RPQEIKRQEV INELFYTERA
HVGMLKVLDD VFYQRLSKDA ILPPADIKNI FTNLEEVLQL HVSILEQMTA IRKRNDSLVV
DLRGDDLLSW FSGAEEEKIK QAVGTFCSNQ PFALEIIKTK QKKDSRFTSF IQEAESNRQC
RRLQLKDIIP VEMLRLTKYP LLLDNIVRYT DDPVEKHKVK QAADCCRKIL SHVNQALKES
EDKQKLEDYQ RRLDLSSLKQ TDNPVIVELK NLDLTKKTLI HEGPLSWKMN KDKTIELYTL
LLEDILVLLQ KQDERLILKC HSKILAGTPD TKHTFSPIIK LNTVLVRSVA TDNKSFFVLS
MSDNVAQIYE LMAPTVSDQK TWQTLISQRA DTMKVKPHSI IPLPQTDGER DGVEIITAGV
SRLSRERDRT STGSTQSTDK ESGPASRSTL QGSLPAGNPF EEGKADVEEE EGFLDPELSC
EVSEVDREGD SFDVFPSRAD EALKTLAALK QVLVNQLMSQ EAAQQTKRST GVRLLRTTSL
RTPTDNRAKV MVHNGSEKSS SKAEDLAQDL GSGDTGFFDS PEDYGCLVLD GYGGQGESST
DGDILASTEG KQLRTSQGCA ADSGINLRFS STSQFGSLST FSRQVLSHLR HLQTSLGYLK
EVETKYNNLI RQRTDRPSTD TDGNKDKR
//
