ID Q8UUX5_CHICK Unreviewed; 839 AA. AC Q8UUX5; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 23-OCT-2007, entry version 32. DE GDP/GTP exchange factor VAV2. GN Name=VAV2; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21663967; 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 RT phosphoinositide 3-kinase activation."; RL J. Exp. Med. 195:189-200(2002). CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 2 SH3 domains. 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; -. DR UniGene; Gga.4341; -. DR HSSP; P27870; 1F5X. DR Ensembl; ENSGALG00000002699; Gallus gallus. DR GeneID; 373938; -. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. DR InterPro; IPR001715; Calponin_act_bd. DR InterPro; IPR002219; DAG_PE_bd. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR001849; PH. DR InterPro; IPR011993; PH_type. DR InterPro; IPR000219; RhoGEF. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3. DR InterPro; IPR011511; SH3_2. DR InterPro; IPR003096; SM22_calponin. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Gene3D; G3DSA:1.20.900.10; RhoGEF; 1. DR Gene3D; G3DSA:3.30.505.10; SH2; 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; PF00018; SH3_1; 1. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00888; SM22CALPONIN. DR ProDom; PD000093; SH2; 1. DR ProDom; PD000066; SH3; 1. 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 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 2: Evidence at transcript level; KW Metal-binding; SH2 domain; SH3 domain; Zinc; Zinc-finger. 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 //