ID A0A096MCD3_POEFO Unreviewed; 1040 AA.
AC A0A096MCD3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Rho guanine nucleotide exchange factor 1 {ECO:0000313|Ensembl:ENSPFOP00000029074.1};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000029074.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000029074.1}
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 EMBL; AYCK01005448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007553807.1; XM_007553745.2.
DR AlphaFoldDB; A0A096MCD3; -.
DR STRING; 48698.ENSPFOP00000029074; -.
DR Ensembl; ENSPFOT00000029949.1; ENSPFOP00000029074.1; ENSPFOG00000002537.2.
DR GeneID; 103139232; -.
DR CTD; 557983; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000161180; -.
DR OrthoDB; 2875542at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; cd14679; PH_p115RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 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; 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:SF4; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 1.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 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; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760}.
FT DOMAIN 477..666
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 707..820
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 214..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1008..1035
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 214..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 117241 MW; 8A351551F9FA38D7 CRC64;
MSIIGAEDED FESDLADSAD DKCPHFDSID LLKKRPTHLL VFMQHVILQF DPAPLLCYLH
ADIVKNLNAR DTKKQFPEFY NNFLEKGAIL RVSMPSSLSF ELDRTRPELL SDDTQRRYAA
DVQKFQTAEV AKQLEDFRQK RMMGMTLCEE QVMDVENHYP TDRVPLDMKE KSVAENLLEK
MFDSQLTFVP DEDKCQAVFS AVAAYMKHLE VKNRAGDSKK SKRGFPWIKQ KNHDPQKSKI
RGFHVPTWIG GSIEVKPKDP EVDKDPKGRE IKGVSGRGSL TETPVPSAKK PENTASAPNA
EPAGNNLTPT TTEPTPADGL SGLGSLELPS PPDGPLPEIG PGVSVVEHSS PHDTHPEESD
RERRKPSRKV GRSESARVDR HSSRRRGSSR KQSRSRSDVD LQPPSSATSP APLSPQHLHP
LDGPAFPSEV PGQPPTSPSP QLEEIDPRLQ ELEQDPPSWR VLASSDTLKN LGKKETKRQE
VINELFATEH AHVRMLSVLQ WVFAKPLERE EILSALDLET IFPSLEEIID MHYTFYESLK
KLRVSDNYVV KNISPTLLNR FGGPEGEWFQ KLTARFCSYQ TYALDQIKQR QKKDARFNAF
IQEAESKPQC RRLQLKDIIP TEMQRLTKYP LLLENIAKNT EEKEEKESIQ QSAECCRKIL
NHVNEEVKTM GNMLTLKEYQ KKLDTSGLKA SVELYAEYKS IDLTQRKMLF EGPLVWRVTK
EKAIDVHCLL LDDMLVLAQK QEDKMLLKCQ SKSNMTAQEG KQMLSPIIKL DSVFLREVAT
DRKAFYVIFT WDSGAQIYEL VAQSVAEMKT WHDIIKSTVD VLKKSGASMR LSIPHGVGVT
PLSPTTLIAP LNPSENGSLR GSSDQERDSV TGHNAVHPGL KLIEMLTDRG FVHVLDHSSR
NQEKVADGAL DEVMSLKRLL IGSISLSEDS QPEEEHEEEQ PEKPSDETEA PQPAEESECT
DSGYMQVNAS PSTKEDGAKQ EDEDGSISAP LVLSQERRDE VCRRLDSLLQ MIQRLQAVEE
EHHKLSEVLS EFSLEGANFQ
//
