ID A0A3B3UP62_9TELE Unreviewed; 770 AA.
AC A0A3B3UP62;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Vav guanine nucleotide exchange factor 3 {ECO:0000313|Ensembl:ENSPLAP00000015160.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000015160.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000015160.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B3UP62; -.
DR STRING; 48699.ENSPLAP00000015160; -.
DR Ensembl; ENSPLAT00000023710.1; ENSPLAP00000015160.1; ENSPLAG00000018999.1.
DR GeneTree; ENSGT00940000155252; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11978; SH3_VAV3_2; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 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; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037832; PH_Vav.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035734; VAV3_SH3_2.
DR PANTHER; PTHR45818:SF1; GUANINE NUCLEOTIDE EXCHANGE FACTOR VAV3; 1.
DR PANTHER; PTHR45818; PROTEIN VAV; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF07653; SH3_2; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 129..308
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 337..439
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 450..499
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 516..582
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 594..688
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 710..770
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
SQ SEQUENCE 770 AA; 89252 MW; 9AB8D442EC041662 CRC64;
MQFLCLKNIR TFLVACSDSF GMKKSELFDA FDLFDVRNFG KVMDTLSKLS HTSIAQQTGI
RHFPTEERVE DEDIYNHLED LIDENGVEDE EDLYACVYED EEGGEIYEDL MKTEAIPPPA
FQKQAEIDIR SCCLTEIKQT EEKYTETLES IEKHFMMPLT MFFSTVEMEK VFVNIPELVK
VHKGLLLEIQ ESVHQRGSQN LYQIFISFKE RLLIYGKYCS HVETAITTLD DICKHREDVR
MKLEECSKRA NYGKFTLRDL LVVPMQRVLK YHLLLQELVK HTHDASEKSN LRTALDAMKD
LAQYVNEVKR DNETLREIEQ YQRSIENLNQ PLSNYGRPKG DGEVRVTSVD KRAKQDRHIF
LFDAAVIVCK RRGDNYEMKE VIDLHLFKIT NNPTSDKENR KWSYGFYLTH NQGQNGFEFF
FKTKELKKKW LEQFGMAISN IRPENATNNF HEFRMHTFER ITSCNSCHML LRGVFYQGYL
CSKCGLGAHK ECLGRFGCCG KTDSGSVRTQ SKHRDPGLPK MLVIRNYFGV PSPASGPALS
IQTGDIIELI CADLHSPWWQ GRILSTKEAG FFPSDAVRPC PCVPKPVDYS SQLWFAGPIE
RFQAEAELIN RVNSTYLVRH RSKEFTEYAI SIKYNNDVKH IKILTKEGCY YIAENKKFRS
ILELIEYYKH HSLREGFKSL DTTLQFPYRE PENAAVHRFN RSGSNMLTPK VIGVAIARYD
FSSRDTRELS LQEGDVVKIY TKSGANGWWR GEVNGRVGWF PSTYVEEGEE
//