ID A0A673WZR3_SALTR Unreviewed; 1254 AA.
AC A0A673WZR3;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Guanine nucleotide exchange factor DBS-like {ECO:0000313|Ensembl:ENSSTUP00000014648.1};
GN Name=LOC115192476 {ECO:0000313|Ensembl:ENSSTUP00000014648.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000014648.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000014648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A673WZR3; -.
DR Ensembl; ENSSTUT00000015460.1; ENSSTUP00000014648.1; ENSSTUG00000006677.1.
DR GeneTree; ENSGT00940000161734; -.
DR InParanoid; A0A673WZR3; -.
DR OMA; LKPMQRH; -.
DR Proteomes; UP000472277; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01227; PH_Dbs; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 1.
DR Gene3D; 1.20.58.60; -; 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; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR035534; DBS_PH.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR22826:SF211; GUANINE NUCLEOTIDE EXCHANGE FACTOR MCF2L2-RELATED; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 136..236
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 668..848
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 860..983
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1163..1224
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 566..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 501..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 141842 MW; 93EE1D022B2876D2 CRC64;
MSSADILALC CGGMMDGSSR YQTIPSRCSA CGRHTRGASS MVRISAGEME SYHRFLGVCQ
KTESATGRNE IMQQEIRPLL AVDIIEQLHR QFALLSGGRG KDGAPIITFP EYSGFGDLVA
EDFQNVVTYL TSIPSLDAAS IGFVIIIDRR RDKWSSVKAS LTRIAGAFPG NLQLVLVLRP
SRFFQRAIAD IGIKLHRDDF KMKVPIVMLN SLSDLYGYVD KGQLTCELGG NLDYCHSQWI
HRRTAIENFA VTVKTTAQML QKFGTDLAET ELPNDVQCTK DLLTTHTEKH DKLKDELKLA
MKQGTTLLGC IKEQAAKSEN HQLNPDEMEN HTTVERLLAQ LDETENAFEQ FWSKHHLKLE
QCLQLRHFEH DFREVKVSLD SRMATLTALS DIGDCVTLVE MLLKDLKTLE EKAQESLEKA
QLHALHGDQL IQSNHYSVDS IRPKCVELRR ICDDFTNEAQ KKYDVLSKSR QIHKGIDKVN
QWCESGVYLL ASQAVDKCQS QEGAEAALQD IEKFLETAKE NQLSDLKNIH NQYELVLNVE
VKANVQKALK RLDDVQEMFE KRQVSLKKLS AKQTRPVQPV APRPESSPKR PVPHKTPRTT
CPAPALSRRI SESSSATKQP TEAELAKRKN VSRKVKGSLK IEVMHEASQG GSSHVLVTNE
TEESLSNRRR HIMNELIETE RLYVEELQSI MEGYAAELDN TELSPLIPAA LENKKDVLFG
NLPEIYEFHN RTFFKELENC MERPELVGTC FLKRKEELQI YEKYCQNKPR SEALWRQCGD
SLFFQECQKK LDHKLSLDAY LLKPVQRITK YQLMVKEMLK CSKNQEGTAE LEEALATMLD
IIKSVNDSMH QIAITGFEGN LSELGKLLMQ GSFNVWTDHK KGHSKVKDLA RFKPMQRHLF
LYNKMLLFCK KREETTDGHE KPSASYGFKH SLKMSAVGIT ENVKGDIKKF EIWYNGREEV
YIIQAPSMDV KNMWVSEIRK VLTGQLEACR EASQLHQKIT ENVYHAPMRN IRKMALRQSD
SSSPETGFRR SNPSPNMRQK RAEPPSKETD VTRRFSVASI SVSATSRTKG PPSTNVRKTK
RHEIKSDPTP FGYEDTLRGA IPAASRHKGT TGTDSAVPRS TSQPGWTQRC LPSMDTEDFE
TIHSSAEELS NSSDGEDESS NKNDHDRFRV QLTYESRTAQ DLSLESGDLV QFLEEAEDGH
WLVKNLIPQK TGLVPPSVLQ TAAGDIFSDM CTAALSDSEE NENPTWGDVS QDSR
//
