VAV_MOUSE
ID VAV_MOUSE Reviewed; 845 AA.
AC P27870; Q8BTV7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Proto-oncogene vav;
DE AltName: Full=p95vav;
GN Name=Vav1; Synonyms=Vav;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-529;
RP CYS-532 AND HIS-554.
RX PubMed=2069873;
RA Coppola J., Bryant S., Koda T., Conway D., Barbacid M.;
RT "Mechanism of activation of the vav protooncogene.";
RL Cell Growth Differ. 2:95-105(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1565462;
RA Adams J.M., Houston H., Allen J., Lints T., Harvey R.;
RT "The hematopoietically expressed vav proto-oncogene shares homology with
RT the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24)
RT involved in cytoskeletal organization.";
RL Oncogene 7:611-618(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
RX PubMed=2005887; DOI=10.1128/mcb.11.4.1912-1920.1991;
RA Katzav S., Cleveland J.L., Heslop H.E., Pulido D.;
RT "Loss of the amino-terminal helix-loop-helix domain of the vav proto-
RT oncogene activates its transforming potential.";
RL Mol. Cell. Biol. 11:1912-1920(1991).
RN [5]
RP INTERACTION WITH TEC.
RX PubMed=8877094;
RA Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.;
RT "Tec protein tyrosine kinase is involved in the signaling mechanism of
RT granulocyte colony-stimulating factor receptor.";
RL Cell Growth Differ. 7:1135-1139(1996).
RN [6]
RP INTERACTION WITH HCK, AND PHOSPHORYLATION.
RX PubMed=9400828; DOI=10.1002/jlb.62.6.859;
RA English B.K., Orlicek S.L., Mei Z., Meals E.A.;
RT "Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in
RT macrophages: evidence for involvement of the hck tyrosine kinase.";
RL J. Leukoc. Biol. 62:859-864(1997).
RN [7]
RP INTERACTION WITH SLA.
RX PubMed=10662792; DOI=10.1084/jem.191.3.463;
RA Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
RT "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor
RT signaling.";
RL J. Exp. Med. 191:463-474(2000).
RN [8]
RP PHOSPHORYLATION, AND INTERACTION WITH CBLB.
RX PubMed=10646609; DOI=10.1038/35003235;
RA Chiang Y.J., Kole H.K., Brown K., Naramura M., Fukuhara S., Hu R.-J.,
RA Jang I.K., Gutkind J.S., Shevach E., Gu H.;
RT "Cbl-b regulates the CD28 dependence of T-cell activation.";
RL Nature 403:216-220(2000).
RN [9]
RP PHOSPHORYLATION, AND INTERACTION WITH CBLB.
RX PubMed=10646608; DOI=10.1038/35003228;
RA Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
RA Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A.,
RA Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.;
RT "Negative regulation of lymphocyte activation and autoimmunity by the
RT molecular adaptor Cbl-b.";
RL Nature 403:211-216(2000).
RN [10]
RP INTERACTION WITH CLNK.
RX PubMed=11463797; DOI=10.1074/jbc.m106390200;
RA Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
RT "MIST functions through distinct domains in immunoreceptor signaling in the
RT presence and absence of LAT.";
RL J. Biol. Chem. 276:36043-36050(2001).
RN [11]
RP POSSIBLE INTERACTION WITH CCPG1.
RX PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT guanine nucleotide exchange factor Dbs.";
RL Mol. Cell. Biol. 26:8964-8975(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [13]
RP INTERACTION WITH ANKRD54.
RX PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA Samuels A.L., Klinken S.P., Ingley E.;
RT "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT influences erythropoietin-induced differentiation.";
RL Blood 113:3845-3856(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP INTERACTION WITH THEMIS2.
RX PubMed=20644716; DOI=10.1371/journal.pone.0011465;
RA Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A.,
RA Notley C., Hussell T., Cope A.P., Wait R.;
RT "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage
RT Toll-like receptor signaling and cytokine production.";
RL PLoS ONE 5:E11465-E11465(2010).
RN [16]
RP INTERACTION WITH CD6.
RX PubMed=24584089; DOI=10.1038/ni.2843;
RA Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
RA Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R., Yamasaki S.,
RA Saito T., Malissen M., Aebersold R., Gstaiger M., Malissen B.;
RT "Quantitative proteomics analysis of signalosome dynamics in primary T
RT cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR
RT signaling hub.";
RL Nat. Immunol. 15:384-392(2014).
CC -!- FUNCTION: Couples tyrosine kinase signals with the activation of the
CC Rho/Rac GTPases, thus leading to cell differentiation and/or
CC proliferation.
CC -!- SUBUNIT: Interacts with SHB (By similarity). Interacts with APS, DOCK2,
CC GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2;
CC without leading to its degradation. Associates with BLNK, PLCG1, GRB2
CC and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with
CC CBLB; which inhibits tyrosine phosphorylation and down-regulates
CC activity (PubMed:10646609, PubMed:10646608). May interact with CCPG1
CC (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts
CC with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this
CC interaction is prolactin-dependent. Interacts with ITK. Interacts with
CC PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with
CC PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity).
CC Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6
CC (PubMed:24584089). Interacts with isoform 2 of CRACR2A (By similarity).
CC {ECO:0000250|UniProtKB:P15498, ECO:0000269|PubMed:10646608,
CC ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:10662792,
CC ECO:0000269|PubMed:11463797, ECO:0000269|PubMed:19064729,
CC ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:24584089,
CC ECO:0000269|PubMed:8877094, ECO:0000269|PubMed:9400828}.
CC -!- INTERACTION:
CC P27870; P19878: NCF2; Xeno; NbExp=4; IntAct=EBI-1697, EBI-489611;
CC -!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but not in
CC other cell types. Found in the spleen and lung.
CC {ECO:0000269|PubMed:2069873}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC -!- PTM: Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine
CC residues by HCK in response to IFNG and bacterial lipopolysaccharide
CC (LPS). {ECO:0000250, ECO:0000269|PubMed:10646608,
CC ECO:0000269|PubMed:10646609, ECO:0000269|PubMed:9400828}.
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DR EMBL; X64361; CAA45713.1; -; mRNA.
DR EMBL; AK088586; BAC40436.1; -; mRNA.
DR EMBL; M59833; AAA63402.1; -; mRNA.
DR CCDS; CCDS28931.1; -.
DR PIR; A61187; TVMSVV.
DR RefSeq; NP_035821.3; NM_011691.4.
DR PDB; 1F5X; NMR; -; A=170-375.
DR PDB; 1GCP; X-ray; 2.10 A; A/B/C/D=595-660.
DR PDB; 1GCQ; X-ray; 1.68 A; C=595-660.
DR PDB; 1K1Z; NMR; -; A=583-660.
DR PDB; 2KBT; NMR; -; A=784-844.
DR PDB; 2VRW; X-ray; 1.85 A; B=170-575.
DR PDBsum; 1F5X; -.
DR PDBsum; 1GCP; -.
DR PDBsum; 1GCQ; -.
DR PDBsum; 1K1Z; -.
DR PDBsum; 2KBT; -.
DR PDBsum; 2VRW; -.
DR AlphaFoldDB; P27870; -.
DR SMR; P27870; -.
DR BioGRID; 204500; 28.
DR DIP; DIP-31010N; -.
DR IntAct; P27870; 14.
DR MINT; P27870; -.
DR STRING; 10090.ENSMUSP00000005889; -.
DR iPTMnet; P27870; -.
DR PhosphoSitePlus; P27870; -.
DR EPD; P27870; -.
DR jPOST; P27870; -.
DR PaxDb; P27870; -.
DR PeptideAtlas; P27870; -.
DR PRIDE; P27870; -.
DR ProteomicsDB; 298277; -.
DR Antibodypedia; 665; 764 antibodies from 42 providers.
DR DNASU; 22324; -.
DR Ensembl; ENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
DR GeneID; 22324; -.
DR KEGG; mmu:22324; -.
DR UCSC; uc008dep.2; mouse.
DR CTD; 7409; -.
DR MGI; MGI:98923; Vav1.
DR VEuPathDB; HostDB:ENSMUSG00000034116; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000159125; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; P27870; -.
DR OMA; PYISRPT; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; P27870; -.
DR TreeFam; TF316171; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9027284; Erythropoietin activates RAS.
DR Reactome; R-MMU-912631; Regulation of signaling by CBL.
DR Reactome; R-MMU-9748787; Azathioprine ADME.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 22324; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Vav1; mouse.
DR EvolutionaryTrace; P27870; -.
DR PRO; PR:P27870; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P27870; protein.
DR Bgee; ENSMUSG00000034116; Expressed in skin of snout and 156 other tissues.
DR ExpressionAtlas; P27870; baseline and differential.
DR Genevisible; P27870; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IGI:MGI.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IGI:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IGI:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IGI:MGI.
DR GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
DR GO; GO:0043087; P:regulation of GTPase activity; IGI:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR GO; GO:0030217; P:T cell differentiation; IGI:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10405; SH2_Vav1; 1.
DR CDD; cd11979; SH3_VAV1_1; 1.
DR CDD; cd11976; SH3_VAV1_2; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR001715; CH-domain.
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; IPR028530; Vav1.
DR InterPro; IPR035879; VAV1_SH2.
DR InterPro; IPR035730; VAV1_SH3_1.
DR InterPro; IPR035729; VAV1_SH3_2.
DR PANTHER; PTHR45818:SF2; PTHR45818:SF2; 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; PF00018; SH3_1; 2.
DR PRINTS; PR00401; SH2DOMAIN.
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; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
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 1: Evidence at protein level;
KW 3D-structure; Guanine-nucleotide releasing factor; Metal-binding;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; SH2 domain;
KW SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..845
FT /note="Proto-oncogene vav"
FT /id="PRO_0000080981"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 194..373
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 402..504
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 592..660
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 671..765
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 782..842
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 515..564
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT MOD_RES 826
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15498"
FT MOD_RES 844
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MUTAGEN 529
FT /note="C->S: Abolishes transforming activity."
FT /evidence="ECO:0000269|PubMed:2069873"
FT MUTAGEN 532
FT /note="C->S: Abolishes transforming activity."
FT /evidence="ECO:0000269|PubMed:2069873"
FT MUTAGEN 554
FT /note="H->D: Abolishes transforming activity."
FT /evidence="ECO:0000269|PubMed:2069873"
FT CONFLICT 29
FT /note="Q -> E (in Ref. 4; AAA63402)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="R -> L (in Ref. 3; BAC40436)"
FT /evidence="ECO:0000305"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1F5X"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1F5X"
FT HELIX 191..219
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 279..300
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 350..389
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 402..412
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 420..437
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 489..506
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 509..512
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:2VRW"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:2VRW"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:2VRW"
FT TURN 585..587
FT /evidence="ECO:0007829|PDB:1K1Z"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:1GCQ"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 624..629
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 635..641
FT /evidence="ECO:0007829|PDB:1GCQ"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:1GCQ"
FT HELIX 652..654
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:1GCQ"
FT STRAND 786..791
FT /evidence="ECO:0007829|PDB:2KBT"
FT STRAND 796..800
FT /evidence="ECO:0007829|PDB:2KBT"
FT STRAND 808..813
FT /evidence="ECO:0007829|PDB:2KBT"
FT STRAND 817..825
FT /evidence="ECO:0007829|PDB:2KBT"
FT STRAND 828..833
FT /evidence="ECO:0007829|PDB:2KBT"
FT STRAND 836..841
FT /evidence="ECO:0007829|PDB:2KBT"
SQ SEQUENCE 845 AA; 98137 MW; 3666DCCD1C5229DA CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPQAINLREV
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNKGIMPFP TEDSALNDED IYSGLSDQID DTAEEDEDLY DCVENEEAEG DEIYEDLMRL
ESVPTPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI
EELFSVHTHF LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA TEKENLRLAL
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY GRPKIDGELK ITSVERRSKT
DRYAFLLDKA LLICKRRGDS YDLKASVNLH SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
YQGYRCYRCR APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF PCNRVHPYVH
GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK DTAEFAISIK YNVEVKHIKI
MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL KDCFKSLDTT LQFPYKEPER RAISKPPAGS
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED
YSEYC
