ID W5M1S2_LEPOC Unreviewed; 1053 AA.
AC W5M1S2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Rho guanine nucleotide exchange factor (GEF) 11 {ECO:0000313|Ensembl:ENSLOCP00000002330.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002330.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002330.1}
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 EMBL; AHAT01035095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01035102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000002335.1; ENSLOCP00000002330.1; ENSLOCG00000001976.1.
DR GeneTree; ENSGT00940000158350; -.
DR HOGENOM; CLU_003962_1_0_1; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000001976; Expressed in camera-type eye and 12 other cell types or tissues.
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:SF1; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11; 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:UP000018468}.
FT DOMAIN 6..70
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 718..897
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 933..1045
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 84..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 117697 MW; D2A1A1FF209ADC87 CRC64;
GLVQRCVIVQ RDQLGFGFTV CGERIKLVQN VRPGGAAVKA GVQEGDRIIK VNGSLVSSMS
HQEVVKLIKS GTYVALTLQG PTPSNASLPL QPLPTDTSPN HRAAPGGVAP PPPLPPAPAS
VSLTSSQRIT GPRPLQXSFV EQGKIQGMAK IQLSWKNKVS PLVAIRQHNV MTESDEHRKR
KKKTLQVIFL QKKNNNILSQ MGNPLTCALS VCHRKEILMP GFVPFFLTGR LSMDSQDGDF
EGFESPRSSP SLSARASQHR RQGSETIFMS DQVRTLWAIT STSTYTRVRD PRSSAQRKRK
TTKILKHRTR KMQADCCFVF PPLPKPRQLF YLSVEAYLSA SPKDARHMAS QIYANFLDKE
APLKIRVSDD FMADIDGRLH AQEDIRGPLS DMQLQVLPEI QEQIQDYRNK QMIGLGSLFG
EGDLQLLDGD PAKEKQIVDR QVTALWEILF LTLCSLSLSP PSAPIASAIL LYLRHAGIKL
RDSRVFSMLD KSQEKDKWLP FFPKTKKPNT TKKEREKEKD AEEKKRNPIL KYIAKPRSTS
QSSKSPARAP SPPLRLSFAQ KSPFHVPLSP TEVLGGMWVK HRARCASPGW KSCRAPGATW
TWTTRPRRGR GRGPGCTSPP PPLPPASLPG QPSALPRRRS HLPGFLFFRS LENPTPPYTP
RSRRKRLSTK NSCLPDCPPA SHCVFTNLKC LETPAGPESR NPAGFLDLSK PVLSFSPELF
TTESSHLRTL RVLDQVFLQK MKGVLNQEEL GCIFPNLPEV LEAHSSLCES MKKLRESLIV
NTIGDIMLAR FEGPAGQEFQ EKVSQFCSRQ AQALELIKSK QQKDPRFQQL IQECEANPQC
RRLQLKDLLV SEMQRLTKYP LLLGNIIKYT DTSSSDLPSL QRAQDCCRGI LKNVNEAVKE
TENRHRLCQY QRRLDLIPRG GLGNQNLDLT TKRMIHEGPL TWRVSKDKAL EIQALLLEDI
LVLLQRVDDR LILRCPSRNL GGGNNDVKMS FSPIVSLDSL LVRSVATDNK ALYVISTSER
QIYELVAGTS SEKNTWKDLL EKAIALASRS PGP
//
