ID A0A3Q3GME6_9LABR Unreviewed; 1198 AA.
AC A0A3Q3GME6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000034531.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000034531.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3Q3GME6; -.
DR STRING; 56723.ENSLBEP00000034531; -.
DR Ensembl; ENSLBET00000036015.1; ENSLBEP00000034531.1; ENSLBEG00000025882.1.
DR GeneTree; ENSGT00940000157662; -.
DR InParanoid; A0A3Q3GME6; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 2.
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; 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; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 2.
DR Pfam; PF00621; RhoGEF; 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.
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:UP000261660};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1198
FT /note="DH domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018677750"
FT DOMAIN 641..831
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 121..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 134462 MW; 29C3102894535FF9 CRC64;
RTGKQDNLAD FVFALLSVCL LRTPSILNHD PTDKKPKNEK SPVSLKHEFD PTGLVQRCVI
IQRDENGFGL TVSGDNPVFV QLVKEGKVNG SLVTHSNHIE VVKLIKSGSY VALTVLGRPP
GLPQIPLGEE EEEVKEDGAE VSTPSSLSAP HSPALPGGEK GNPACSPSLA DGVSKKEDRN
PRPKLLKEIQ EVKKHISVLQ EQLSKAVFQI HGSPLPESPG NRDTPCQSPD ISRRDGLNFC
SSPDTEETPD TESSAQCIVG SPPYLLNPQI IGAEDDYFDS QQEQINGPCS SFETLDLLKS
RPAHLAVFLH HVVSQFDPVP LVCMQTHQPV DTSLERQVKM TDCNRKKLEL IPEDVCKQYT
QTLQDSLLPD LNKNLEDFRQ KRSMGLTLAE DELSKLDSER GENQQVLEKE CSCAEHILSK
IEDILLTSQP TEEEKCQTMQ YVILTYMKHL GVKVKEPRGL EHKRARINFL PKIKVRSEVK
KSTSKRKKYL DADNTHQIYS YNAVEINKQR SPKQLPQPTV CIPEQSDSSS SSNSGRTRGN
QLSEGSDTNL SPFCIQTRPS EGLQSGDHQD AVSSPTSTQF DFSPSNLEQL QEEDQDAFSS
GDIQSEDDLG GEVEGSEEDP LNWQSLVSRG VLASLTPLEI KRQEVINELF YTERAHLRML
KVLDSVFYQR LSRDGILPPE DLKHVFINLE EIIQLHVSVT EQMTSIRKRS ETSVIGQIAD
DLLAWFSGEE EEKIKRAVGT FCSNQPSALE LIKSRKKKDQ RFTLFMREAE SNRLCRRLQL
KDIIPVEMQR VTKYPLLLDN IAKYTEDGEE REKVRRAAEC CKKILNHVNQ AVKEAENKQR
LIEYQRRLDI SSLKQSDNPM ILELKNLDLT KRKMVHEGPL SWKINKDKII ELYTLLLEDI
LVLLQKQDER LVLKLHGKNP ASAADTKNIF SPVIKLNTVL VRPVATDNRS FFVLSMSENG
AQIYKVKSQT VSDQRITNPF DGMKSEDEEE ELEEEGGDEE IDEAELEAFL DGQLPFLQEE
TPQSVAAENQ ELNAFDSASS SKGEEALRTC KSHTQRRTLR PSEQIFRPKQ NSLWRFKIQD
FYLSHAHTDV QESRQLKDRK AFQNQTFNLT SSVCSASPPP GGFVVLDFGG SEESSTDDDG
GVGVDVGIDM SKLLSSSSQT GGVSGPNLSR QLMTHLRLLQ ADLQYLKVLH MLSLVSTL
//
