VAV3_MOUSE
ID VAV3_MOUSE Reviewed; 847 AA.
AC Q9R0C8; A2CFD7; Q7TS85; Q8BRV2; Q8CCF5; Q8R076; Q9JLS6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Guanine nucleotide exchange factor VAV3;
DE Short=VAV-3;
GN Name=Vav3;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-789 (ISOFORM 3).
RC TISSUE=Skin;
RX PubMed=10713454; DOI=10.1016/s0378-1119(00)00026-3;
RA Trenkle T., McClelland M., Adlkofer K., Welsh J.;
RT "Major transcript variants of VAV3, a new member of the VAV family of
RT guanine nucleotide exchange factors.";
RL Gene 245:139-149(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-731 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stomach, and Embryonic testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 143-152, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15711558; DOI=10.1038/nm1194;
RA Faccio R., Teitelbaum S.L., Fujikawa K., Chappel J., Zallone A.,
RA Tybulewicz V.L., Ross F.P., Swat W.;
RT "Vav3 regulates osteoclast function and bone mass.";
RL Nat. Med. 11:284-290(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH EPHA2.
RX PubMed=16782872; DOI=10.1128/mcb.02215-05;
RA Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
RA Chen J.;
RT "Essential role of Vav family guanine nucleotide exchange factors in EphA
RT receptor-mediated angiogenesis.";
RL Mol. Cell. Biol. 26:4830-4842(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19147786; DOI=10.1182/blood-2008-07-166702;
RA Sindrilaru A., Peters T., Schymeinsky J., Oreshkova T., Wang H., Gompf A.,
RA Mannella F., Wlaschek M., Sunderkotter C., Rudolph K.L., Walzog B.,
RA Bustelo X.R., Fischer K.D., Scharffetter-Kochanek K.;
RT "Wound healing defect of Vav3-/- mice due to impaired {beta}2-integrin-
RT dependent macrophage phagocytosis of apoptotic neutrophils.";
RL Blood 113:5266-5276(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: Exchange factor for GTP-binding proteins RhoA, RhoG and, to a
CC lesser extent, Rac1. Binds physically to the nucleotide-free states of
CC those GTPases (By similarity). Plays an important role in angiogenesis.
CC Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced
CC RAC1 GTPase activation and vascular endothelial cell migration and
CC assembly. May be important for integrin-mediated signaling, at least in
CC some cell types. In osteoclasts, along with SYK tyrosine kinase,
CC required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a
CC crucial event for osteoclast proper cytoskeleton organization and
CC function. This signaling pathway involves RAC1, but not RHO,
CC activation. Necessary for proper wound healing. In the course of wound
CC healing, required for the phagocytotic cup formation preceding
CC macrophage phagocytosis of apoptotic neutrophils. Responsible for
CC integrin beta-2-mediated macrophage adhesion and, to a lesser extent,
CC contributes to beta-3-mediated adhesion. Does not affect integrin beta-
CC 1-mediated adhesion. {ECO:0000250, ECO:0000269|PubMed:15711558,
CC ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:19147786}.
CC -!- SUBUNIT: Interacts with the PH domain of APS. Interacts with ROS1;
CC constitutive interaction that mediates VAV3 phosphorylation (By
CC similarity). Interacts (via SH2 domains) with the phosphorylated form
CC of EPHA2. {ECO:0000250, ECO:0000269|PubMed:16782872}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9R0C8-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9R0C8-2; Sequence=Not described;
CC Name=3; Synonyms=VAV3.1;
CC IsoId=Q9R0C8-3; Sequence=VSP_042360, VSP_042361;
CC Name=4;
CC IsoId=Q9R0C8-4; Sequence=VSP_042362, VSP_042363;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in osteoclasts and mature
CC osteoblasts. Also expressed in bone marrow macrophages (at protein
CC level):.
CC -!- PTM: Phosphorylated. Phosphorylation can be mediated by ROS1 (By
CC similarity). In osteoclasts, undergoes tyrosine phosphorylation in
CC response to CSF1. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice exhibit increased bone density, due
CC to diminished bone resorption, including following parathyroid hormone
CC treatment. This phenotype is due to defective terminal osteoclast
CC differentiation. They also show a delayed wound repair program,
CC characterized by a deficit in macrophage emigration to the wound, a
CC reduced myofibroblast-dependent wound contraction and a diminished
CC neovascularization in the restoration tissue.
CC {ECO:0000269|PubMed:15711558, ECO:0000269|PubMed:19147786}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC {ECO:0000305}.
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DR EMBL; AF067816; AAF09171.1; -; mRNA.
DR EMBL; AF140280; AAF20330.2; -; mRNA.
DR EMBL; AK033253; BAC28212.1; -; mRNA.
DR EMBL; AK041249; BAC30879.2; -; mRNA.
DR EMBL; AK147053; BAE27637.1; -; mRNA.
DR EMBL; AL671857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR938729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027242; AAH27242.1; -; mRNA.
DR EMBL; BC052739; AAH52739.1; -; mRNA.
DR CCDS; CCDS17773.1; -. [Q9R0C8-1]
DR CCDS; CCDS59650.1; -. [Q9R0C8-3]
DR RefSeq; NP_065251.2; NM_020505.2. [Q9R0C8-1]
DR RefSeq; NP_666251.1; NM_146139.2. [Q9R0C8-3]
DR AlphaFoldDB; Q9R0C8; -.
DR SMR; Q9R0C8; -.
DR BioGRID; 208227; 2.
DR STRING; 10090.ENSMUSP00000036270; -.
DR iPTMnet; Q9R0C8; -.
DR PhosphoSitePlus; Q9R0C8; -.
DR EPD; Q9R0C8; -.
DR MaxQB; Q9R0C8; -.
DR PaxDb; Q9R0C8; -.
DR PeptideAtlas; Q9R0C8; -.
DR PRIDE; Q9R0C8; -.
DR ProteomicsDB; 298274; -. [Q9R0C8-1]
DR ProteomicsDB; 298275; -. [Q9R0C8-3]
DR ProteomicsDB; 298276; -. [Q9R0C8-4]
DR Antibodypedia; 4549; 358 antibodies from 37 providers.
DR DNASU; 57257; -.
DR Ensembl; ENSMUST00000046864; ENSMUSP00000036270; ENSMUSG00000033721. [Q9R0C8-1]
DR Ensembl; ENSMUST00000106576; ENSMUSP00000102186; ENSMUSG00000033721. [Q9R0C8-3]
DR GeneID; 57257; -.
DR KEGG; mmu:57257; -.
DR UCSC; uc008raf.1; mouse. [Q9R0C8-4]
DR UCSC; uc008rag.1; mouse. [Q9R0C8-1]
DR UCSC; uc008rah.1; mouse. [Q9R0C8-3]
DR CTD; 10451; -.
DR MGI; MGI:1888518; Vav3.
DR VEuPathDB; HostDB:ENSMUSG00000033721; -.
DR eggNOG; KOG2996; Eukaryota.
DR GeneTree; ENSGT00940000155252; -.
DR HOGENOM; CLU_013787_0_0_1; -.
DR InParanoid; Q9R0C8; -.
DR OMA; NEDPVGE; -.
DR OrthoDB; 710582at2759; -.
DR PhylomeDB; Q9R0C8; -.
DR TreeFam; TF316171; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
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-2424491; DAP12 signaling.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 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-9748787; Azathioprine ADME.
DR BioGRID-ORCS; 57257; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Vav3; mouse.
DR PRO; PR:Q9R0C8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R0C8; protein.
DR Bgee; ENSMUSG00000033721; Expressed in habenula and 251 other tissues.
DR Genevisible; Q9R0C8; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0030031; P:cell projection assembly; IGI:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IGI:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; 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:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
DR GO; GO:0006906; P:vesicle fusion; IGI:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd00014; CH; 1.
DR CDD; cd01223; PH_Vav; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd10407; SH2_Vav3; 1.
DR CDD; cd11978; SH3_VAV3_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; IPR035881; VAV3_SH2.
DR InterPro; IPR035734; VAV3_SH3_2.
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 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; 2.
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 Alternative promoter usage; Alternative splicing; Angiogenesis;
KW Direct protein sequencing; Guanine-nucleotide releasing factor;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; SH2 domain;
KW SH3 domain; Zinc; Zinc-finger.
FT CHAIN 1..847
FT /note="Guanine nucleotide exchange factor VAV3"
FT /id="PRO_0000080987"
FT DOMAIN 1..119
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 192..371
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 400..502
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 672..766
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 788..847
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT ZN_FING 513..562
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 560..847
FT /note="Sufficient for interaction with ROS1"
FT /evidence="ECO:0000250"
FT MOD_RES 141
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKW4"
FT VAR_SEQ 1..560
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10713454,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042360"
FT VAR_SEQ 561..568
FT /note="NCGRVNSV -> MPIFTFVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10713454,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042361"
FT VAR_SEQ 569..574
FT /note="EQGPFK -> GKSCLL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042362"
FT VAR_SEQ 575..847
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042363"
FT CONFLICT 355
FT /note="K -> R (in Ref. 2; BAC30879)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="I -> T (in Ref. 2; BAC28212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 97968 MW; 727C9BF50DF8CF19 CRC64;
MEPWKQCAQW LIHSKVLPPN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RPHSINLKEI
NLRPQMSQFL CLKNIRTFLA ACCDTFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI
ALATGIRPFP TEESINDEDI YKGLPDLIDE TRVEDEEDLY DCVYGEDEGG EVYEDLMKAE
EAQQPKSQEN DIRSCCLAEI RQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPD
LVKVHRSLMQ EIHDSIVNKD DQNLYQVFIN YKERLVIYGQ YCSGVESAIS NLDYISKTKE
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTHDPME KANLKLALDA
MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR PQGDGEIRIT TLDKHTKQER
HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY KIANNPTTDK ENKKWSYGFY LIHTQGQNGL
EFYCKTKDLK KKWLEQFEMA LSNIRPDYAD SNFHDFKMHT FTRVTSCRVC QMLLRGTFYQ
GYLCFKCGAK AHKECLGRVD NCGRVNSVEQ GPFKPPEKRT NGLRRASRQV DPGLPKMQVI
RNYTGTPAPG LHEGPPLHIQ AGDTVELLRG DAHSVFWQGR NLASGEVGFF PSDAVKPSPC
VPKPVDYSCQ PWYAGPMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK
ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE QPAGQRGNRT
GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDMVKIYTK MSANGWWRGE VNGRVGWFPS
TYVEEDE
