ID VAV2_HUMAN Reviewed; 878 AA.
AC P52735; A2RUM4; A8MQ12; B6ZDF5; Q5SYV3; Q5SYV4; Q5SYV5; Q6N012;
AC Q6PIJ9; Q6Q317;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 29-MAY-2013, entry version 139.
DE RecName: Full=Guanine nucleotide exchange factor VAV2;
DE Short=VAV-2;
GN Name=VAV2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-594.
RC TISSUE=Brain;
RX PubMed=7762982; DOI=10.1111/j.1469-1809.1995.tb01603.x;
RA Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S.,
RA Haines J.L., Kwiatkowski D.J.;
RT "Identification of VAV2 on 9q34 and its exclusion as the tuberous
RT sclerosis gene TSC1.";
RL Ann. Hum. Genet. 59:25-37(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
RP VAL-594.
RC TISSUE=Kidney;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-878 (ISOFORM 3).
RC TISSUE=Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 453-506 (ISOFORMS 2/3).
RA Mancini U.M., Tajara E.H.;
RT "Transcript variant of VAV2 gene in tumoral cell lines (FaDu, HEp2,
RT HeLa and SiHa).";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.
RX PubMed=12454019; DOI=10.1074/jbc.M207555200;
RA Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A.,
RA Farago A., Downward J., Buday L.;
RT "Mechanism of epidermal growth factor regulation of Vav2, a guanine
RT nucleotide exchange factor for Rac.";
RL J. Biol. Chem. 278:5163-5171(2003).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
RA Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
RA Lowell C.A., Berton G.;
RT "The proto-oncogene Fgr regulates cell migration and this requires its
RT plasma membrane localization.";
RL Exp. Cell Res. 302:253-269(2005).
RN [9]
RP INTERACTION WITH NEK3 AND PRLR.
RX PubMed=15618286; DOI=10.1210/me.2004-0443;
RA Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.;
RT "Novel association of Vav2 and Nek3 modulates signaling through the
RT human prolactin receptor.";
RL Mol. Endocrinol. 19:939-949(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 (ISOFORM 3), AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP STRUCTURE BY NMR OF 663-878.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH2 domain and of the second SH3 domain of
RT human protein VAV-2.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Guanine nucleotide exchange factor for the Rho family of
CC Ras-related GTPases. Plays an important role in angiogenesis. Its
CC recruitment by phosphorylated EPHA2 is critical for EFNA1-induced
CC RAC1 GTPase activation and vascular endothelial cell migration and
CC assembly (By similarity).
CC -!- SUBUNIT: Interacts (via SH2 domains) with the phosphorylated form
CC of EPHA2 (By similarity). Interacts with NEK3 and PRLR and this
CC interaction is prolactin-dependent.
CC -!- INTERACTION:
CC P51956:NEK3; NbExp=3; IntAct=EBI-297549, EBI-476041;
CC O75674:TOM1L1; NbExp=2; IntAct=EBI-297549, EBI-712991;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P52735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52735-2; Sequence=VSP_034900, VSP_034901;
CC Name=3;
CC IsoId=P52735-3; Sequence=VSP_034900, VSP_034901, VSP_034902;
CC Note=Contains a phosphoserine at position 769;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- PTM: Phosphorylated on tyrosine residues in response to FGR
CC activation.
CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC -!- SIMILARITY: Contains 1 SH2 domain.
CC -!- SIMILARITY: Contains 2 SH3 domains.
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DR EMBL; S76992; AAB34377.1; -; mRNA.
DR EMBL; AL590710; CAI12279.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI12279.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI12279.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI13722.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI13722.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI13722.1; JOINED; Genomic_DNA.
DR EMBL; AL357934; CAI15783.1; -; Genomic_DNA.
DR EMBL; AL445931; CAI15783.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI15783.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI12278.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI12278.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI12278.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI13723.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI13723.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI13723.1; JOINED; Genomic_DNA.
DR EMBL; AL357934; CAI15781.1; -; Genomic_DNA.
DR EMBL; AL445931; CAI15781.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI15781.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI12280.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI12280.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI12280.1; JOINED; Genomic_DNA.
DR EMBL; AL445931; CAI13724.1; -; Genomic_DNA.
DR EMBL; AL357934; CAI13724.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI13724.1; JOINED; Genomic_DNA.
DR EMBL; AL357934; CAI15782.1; -; Genomic_DNA.
DR EMBL; AL445931; CAI15782.1; JOINED; Genomic_DNA.
DR EMBL; AL590710; CAI15782.1; JOINED; Genomic_DNA.
DR EMBL; CH471090; EAW88108.1; -; Genomic_DNA.
DR EMBL; BC033187; AAH33187.1; -; mRNA.
DR EMBL; BC132965; AAI32966.1; -; mRNA.
DR EMBL; BC132967; AAI32968.1; -; mRNA.
DR EMBL; BX640754; CAE45861.1; -; mRNA.
DR EMBL; AY563001; AAS75591.1; -; mRNA.
DR IPI; IPI00004977; -.
DR IPI; IPI00472451; -.
DR IPI; IPI00872160; -.
DR PIR; I51940; I51940.
DR RefSeq; NP_001127870.1; NM_001134398.1.
DR RefSeq; NP_003362.2; NM_003371.3.
DR UniGene; Hs.369921; -.
DR UniGene; Hs.689325; -.
DR PDB; 2DLZ; NMR; -; A=663-767.
DR PDB; 2DM1; NMR; -; A=819-878.
DR PDB; 2LNW; NMR; -; A=659-771.
DR PDB; 2LNX; NMR; -; A=659-771.
DR PDBsum; 2DLZ; -.
DR PDBsum; 2DM1; -.
DR PDBsum; 2LNW; -.
DR PDBsum; 2LNX; -.
DR ProteinModelPortal; P52735; -.
DR IntAct; P52735; 48.
DR MINT; MINT-1494337; -.
DR PhosphoSite; P52735; -.
DR DMDM; 212287930; -.
DR PaxDb; P52735; -.
DR PRIDE; P52735; -.
DR Ensembl; ENST00000371850; ENSP00000360916; ENSG00000160293.
DR Ensembl; ENST00000371851; ENSP00000360917; ENSG00000160293.
DR Ensembl; ENST00000406606; ENSP00000385362; ENSG00000160293.
DR GeneID; 7410; -.
DR KEGG; hsa:7410; -.
DR UCSC; uc004cer.3; human.
DR UCSC; uc004ces.3; human.
DR CTD; 7410; -.
DR GeneCards; GC09M136627; -.
DR HGNC; HGNC:12658; VAV2.
DR HPA; HPA003224; -.
DR MIM; 600428; gene.
DR neXtProt; NX_P52735; -.
DR PharmGKB; PA37281; -.
DR eggNOG; NOG326494; -.
DR HOVERGEN; HBG018066; -.
DR InParanoid; P52735; -.
DR KO; K05730; -.
DR OMA; WFAGNME; -.
DR OrthoDB; EOG41NTKH; -.
DR Pathway_Interaction_DB; bcr_5pathway; BCR signaling pathway.
DR Pathway_Interaction_DB; epha_fwdpathway; EPHA forward signaling.
DR Pathway_Interaction_DB; epha2_fwdpathway; EPHA2 forward signaling.
DR Pathway_Interaction_DB; epopathway; EPO signaling pathway.
DR Pathway_Interaction_DB; pdgfrbpathway; PDGFR-beta signaling pathway.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P52735; -.
DR ChiTaRS; VAV2; human.
DR EvolutionaryTrace; P52735; -.
DR GenomeRNAi; 7410; -.
DR NextBio; 29012; -.
DR Bgee; P52735; -.
DR Genevestigator; P52735; -.
DR GermOnline; ENSG00000160293; Homo sapiens.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:Compara.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0016477; P:cell migration; IEA:Compara.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Compara.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Compara.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
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; IPR001715; CH-domain.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR011511; SH3_2.
DR InterPro; IPR001452; SH3_domain.
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; 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; 1.
DR SUPFAM; SSF48065; DH-domain; 1.
DR SUPFAM; SSF50044; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Complete proteome;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Repeat; SH2 domain; SH3 domain;
KW Zinc; Zinc-finger.
FT CHAIN 1 878 Guanine nucleotide exchange factor VAV2.
FT /FTId=PRO_0000080984.
FT DOMAIN 1 119 CH.
FT DOMAIN 198 376 DH.
FT DOMAIN 405 512 PH.
FT DOMAIN 586 652 SH3 1.
FT DOMAIN 673 767 SH2.
FT DOMAIN 816 877 SH3 2.
FT ZN_FING 523 572 Phorbol-ester/DAG-type.
FT MOD_RES 142 142 Phosphotyrosine; by EGFR.
FT MOD_RES 159 159 Phosphotyrosine; by EGFR.
FT MOD_RES 172 172 Phosphotyrosine; by EGFR.
FT MOD_RES 576 576 Phosphoserine.
FT MOD_RES 626 626 Phosphoserine.
FT VAR_SEQ 185 189 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_034900.
FT VAR_SEQ 470 474 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_034901.
FT VAR_SEQ 783 811 Missing (in isoform 3).
FT /FTId=VSP_034902.
FT VARIANT 594 594 M -> V (in dbSNP:rs602990).
FT /FTId=VAR_045690.
FT CONFLICT 241 241 F -> L (in Ref. 5; CAE45861).
FT CONFLICT 254 254 F -> L (in Ref. 5; CAE45861).
FT CONFLICT 877 877 I -> T (in Ref. 5; CAE45861).
FT STRAND 661 664
FT HELIX 668 670
FT STRAND 674 677
FT HELIX 680 689
FT STRAND 694 698
FT STRAND 707 712
FT STRAND 714 725
FT STRAND 728 731
FT STRAND 737 739
FT HELIX 740 747
FT TURN 752 755
FT STRAND 767 769
FT STRAND 819 825
FT STRAND 842 844
FT STRAND 847 854
FT STRAND 856 860
FT STRAND 863 867
FT STRAND 869 874
SQ SEQUENCE 878 AA; 101289 MW; C186911605FD5B73 CRC64;
MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL SPGSIDLKDI
NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF DVRDFGKVIS AVSRLSLHSI
AQNKGIRPFP SEETTENDDD VYRSLEELAD EHDLGEDIYD CVPCEDGGDD IYEDIIKVEV
QQPMIRYMQK MGMTEDDKRN CCLLEIQETE AKYYRTLEDI EKNYMSPLRL VLSPADMAAV
FINLEDLIKV HHSFLRAIDV SVMVGGSTLA KVFLDFKERL LIYGEYCSHM EHAQNTLNQL
LASREDFRQK VEECTLKVQD GKFKLQDLLV VPMQRVLKYH LLLKELLSHS AERPERQQLK
EALEAMQDLA MYINEVKRDK ETLRKISEFQ SSIENLQVKL EEFGRPKIDG ELKVRSIVNH
TKQDRYLFLF DKVVIVCKRK GYSYELKEII ELLFHKMTDD PMNNKDVKKS HGKMWSYGFY
LIHLQGKQGF QFFCKTEDMK RKWMEQFEMA MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC
KMFLRGTFYQ GYMCTKCGVG AHKECLEVIP PCKFTSPADL DASGAGPGPK MVAMQNYHGN
PAPPGKPVLT FQTGDVLELL RGDPESPWWE GRLVQTRKSG YFPSSSVKPC PVDGRPPISR
PPSREIDYTA YPWFAGNMER QQTDNLLKSH ASGTYLIRER PAEAERFAIS IKFNDEVKHI
KVVEKDNWIH ITEAKKFDSL LELVEYYQCH SLKESFKQLD TTLKYPYKSR ERSASRASSR
SPASCASYNF SFLSPQGLSF ASQGPSAPFW SVFTPRVIGT AVARYNFAAR DMRELSLREG
DVVRIYSRIG GDQGWWKGET NGRIGWFPST YVEEEGIQ
//
