ID A0A2K6FL06_PROCO Unreviewed; 774 AA.
AC A0A2K6FL06;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Vav guanine nucleotide exchange factor 1 {ECO:0000313|Ensembl:ENSPCOP00000014648.1};
GN Name=VAV1 {ECO:0000313|Ensembl:ENSPCOP00000014648.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000014648.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000014648.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6FL06; -.
DR Ensembl; ENSPCOT00000025258.1; ENSPCOP00000014648.1; ENSPCOG00000019002.1.
DR GeneTree; ENSGT00940000159125; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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:0007166; P:cell surface receptor signaling pathway; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd20867; C1_VAV1; 1.
DR CDD; cd21262; CH_VAV1; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11979; SH3_VAV1_1; 1.
DR CDD; cd11976; SH3_VAV1_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; IPR022613; CAMSAP-like_CH_dom.
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; IPR003096; SM22_calponin.
DR InterPro; IPR035730; VAV1_SH3_1.
DR InterPro; IPR035729; VAV1_SH3_2.
DR PANTHER; PTHR45818; PROTEIN VAV; 1.
DR PANTHER; PTHR45818:SF2; PROTO-ONCOGENE VAV; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 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; PS50021; CH; 1.
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; PS00479; ZF_DAG_PE_1; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000233160};
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 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 154..341
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 370..472
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 483..532
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 560..628
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 587..694
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 711..771
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 537..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 90182 MW; 18B26384C56DBC97 CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNKGIMPFP TDEDNVGDED VYSGLSDQID DTVEDDEDLY DCVENEETEG DEIYEDLMRS
EPVPMPHFLK PLQRFLKPQD IEIIFINIED LLRVHTHFLK EMKEALATPG ASTLYQVFIK
YKERFLIYGR YCSQVESASK HLDHVAAARE DVQMKLEECS QRANNGRFTL RDLLMVPMQR
VLKYHLLLQE LVKHTQDAME KENLRLSLDA MRDLAQCVNE VKRDNETLRQ ITNFQLSIEN
LDQSLAHYGR PKIDGELKIT SVERRSKMDR YAFLLDKALL ICKRRGDSYD LKDFVNLHSF
QVRDDSSGDK DNKKWSHMFL LIEDQGAQGY ELFFKTRELK KKWMEQFEMA ISNIYPENAA
ANGHDFQMFS FEETTSCKAC QMLLRGTFYQ GYRCHRCRAP AHKECLGRVP PCGRHGQDFS
GTMKKDKPHR RAQDKKRNDL GLPKMEVFQE YYGLPPPPGA FGPFLRLNPG DIVELTKAEA
EQNWWEGRNT ATNEVGWFPC NRVKPYVHGP PQDLSVHLWY NVEVKHIKIM TAEGLYRITE
KKAFRGLTEL VEFYQQNSLK DCFKSLDTTL QFPFKEPERR AISKPPAGST KYFGTAKARY
DFCARDRSEL SLKEGDIIKI LNKKGQQGWW RGEIYGRVGW FPSNYVEEDY SEYC
//
