ID Q8UUX5_CHICK Unreviewed; 839 AA. AC Q8UUX5; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 02-OCT-2024, entry version 142. DE SubName: Full=GDP/GTP exchange factor VAV2 {ECO:0000313|EMBL:AAL06250.1}; GN Name=VAV2 {ECO:0000313|EMBL:AAL06250.1}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAL06250.1}; RN [1] {ECO:0000313|EMBL:AAL06250.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11805146; DOI=10.1084/jem.20011571; RA Inabe K., Ishiai M., Scharenberg A.M., Freshney N., Downward J., RA Kurosaki T.; RT "Vav3 modulates B cell receptor responses by regulating phosphoinositide 3- RT kinase activation."; RL J. Exp. Med. 195:189-200(2002). 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 EMBL; AY046916; AAL06250.1; -; mRNA. DR RefSeq; NP_989473.1; NM_204142.1. DR AlphaFoldDB; Q8UUX5; -. DR GeneID; 373938; -. DR KEGG; gga:373938; -. DR CTD; 7410; -. DR VEuPathDB; HostDB:geneid_373938; -. DR PhylomeDB; Q8UUX5; -. 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; cd20868; C1_VAV2; 1. DR CDD; cd21263; CH_VAV2; 1. DR CDD; cd01223; PH_Vav; 1. DR CDD; cd00160; RhoGEF; 1. DR CDD; cd10406; SH2_Vav2; 1. DR CDD; cd11980; SH3_VAV2_1; 1. DR CDD; cd11977; SH3_VAV2_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; IPR035880; VAV2_SH2. DR InterPro; IPR035733; VAV2_SH3_1. DR InterPro; IPR035732; VAV2_SH3_2. DR PANTHER; PTHR45818:SF4; GUANINE NUCLEOTIDE EXCHANGE FACTOR VAV2; 1. DR PANTHER; PTHR45818; PROTEIN 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; PF00017; SH2; 1. DR Pfam; PF07653; SH3_2; 2. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00109; C1; 1. DR SMART; SM00033; CH; 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; PS50021; CH; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50890; PUA; 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 2: Evidence at transcript level; 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 1..119 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000259|PROSITE:PS50021" FT DOMAIN 193..371 FT /note="DH" FT /evidence="ECO:0000259|PROSITE:PS50010" FT DOMAIN 400..502 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 513..562 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 576..642 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 663..757 FT /note="SH2" FT /evidence="ECO:0000259|PROSITE:PS50001" FT DOMAIN 777..838 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" SQ SEQUENCE 839 AA; 97501 MW; 6C1322ABAC23A530 CRC64; MEEWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL SPGSIDLKDI NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SDLFDPFDLF DVRDFGKVIS AVSRLSFHSI AQTKGIRPFP SEETTENDDD VYRSLEELAD EHDLGEDIYD CVPCEDEGDD IYEDIIRVEV QQPMKMGMTE DDKRNCCLLE IQETEAKYYK TLEDIEKNYM NPLKLVLTPQ DMEAIFINLE DLIKVHFNFL RAIDVSMMSG GSSLAKVFLE FKERLLIYGK YCSHMEYAQN TLNHLIANRD DVRQKVEECT LKVQDGKFKL QDLLVVPMQR VLKHYLLLKE LLSHSSDRPE KQQLKEALEA MQDLAMYINE VKRDKETLKK ISEFQSSIEN LQVKLEEFGR PKIDGELKVR SIVNHTKQDR YLFLFDKVVI VCKRKGYNYE LKEIIELLFH KMTDDPMNNK DIKKWSYGFY LIHLQGKQGF QFFCKTEEMK RKWMEQFEMA MSNIKPEKAN ANHHSFQMYT FEKTTNCKAC KMFLRGTFYQ GYLCPKCGAG AHKECLEIIP PCKMGSSADQ DLLSAGPGPK MVAVQNYHGN PAPPGKPVLT FQIGDVIELL RGDPDSPWWE GRLLQTKKSG YFPSSSVKPC PVDARPPNSR PPSREIDYTV YPWFAGNMER QQTDNLLKTH VSGTYLIRER PAEAERFAIS IKFNEEVKHI KVVEKDNWIH ITEAKKFESL LELVEYYQNH SLKESFKQLD TTLKYPYKSR ERSTSRTFTR SPVFTPRVIG TAVARYNFAA RDMRELSLRE GDVVKIYSRI GGDQGWWKGE TNGRVGWFPS TYVEEEGVQ //