GENTAUR Molecular Products.

 BCAR3_HUMAN             Reviewed;         825 AA.
 O75815; D3DT43; Q5TEW3; Q6UW40; Q9BR50;
 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1998, sequence version 1.
 23-MAY-2018, entry version 151.
 RecName: Full=Breast cancer anti-estrogen resistance protein 3;
 AltName: Full=Novel SH2-containing protein 2;
 AltName: Full=SH2 domain-containing protein 3B;
 Name=BCAR3; Synonyms=NSP2, SH2D3B; ORFNames=UNQ271/PRO308;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
 FUNCTION.
 TISSUE=Testis;
 PubMed=9582273; DOI=10.1093/emboj/17.10.2799;
 van Agthoven T., van Agthoven T.L.A., Dekker A., van der Spek P.J.,
 Vreede L., Dorssers L.C.J.;
 "Identification of BCAR3 by a random search for genes involved in
 antiestrogen resistance of human breast cancer cells.";
 EMBO J. 17:2799-2808(1998).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
 TISSUE=Kidney;
 PubMed=10187783; DOI=10.1074/jbc.274.15.10047;
 Lu Y., Brush J., Stewart T.A.;
 "NSP1 defines a novel family of adaptor proteins linking integrin and
 tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-
 activated protein kinase signaling pathway.";
 J. Biol. Chem. 274:10047-10052(1999).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
 PubMed=12975309; DOI=10.1101/gr.1293003;
 Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
 Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
 Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
 Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
 Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
 Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
 Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
 Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
 Wood W.I., Godowski P.J., Gray A.M.;
 "The secreted protein discovery initiative (SPDI), a large-scale
 effort to identify novel human secreted and transmembrane proteins: a
 bioinformatics assessment.";
 Genome Res. 13:2265-2270(2003).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
 TISSUE=Heart;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16710414; DOI=10.1038/nature04727;
 Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
 Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
 Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
 McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
 Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
 Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
 Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
 Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
 Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
 Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
 Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
 Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
 Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
 Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
 Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
 Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
 Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
 Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
 Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
 Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
 Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
 Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
 Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
 Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
 Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
 Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
 Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
 Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
 Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
 Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
 Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
 Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence and biological annotation of human chromosome 1.";
 Nature 441:315-321(2006).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 TISSUE=Lung;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [8]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-375, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=16964243; DOI=10.1038/nbt1240;
 Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
 "A probability-based approach for high-throughput protein
 phosphorylation analysis and site localization.";
 Nat. Biotechnol. 24:1285-1292(2006).
 [9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-83; SER-290;
 SER-358; SER-363 AND SER-375, AND IDENTIFICATION BY MASS SPECTROMETRY
 [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [10]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Leukemic T-cell;
 PubMed=19690332; DOI=10.1126/scisignal.2000007;
 Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
 Rodionov V., Han D.K.;
 "Quantitative phosphoproteomic analysis of T cell receptor signaling
 reveals system-wide modulation of protein-protein interactions.";
 Sci. Signal. 2:RA46-RA46(2009).
 [11]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=20068231; DOI=10.1126/scisignal.2000475;
 Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
 Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
 Mann M.;
 "Quantitative phosphoproteomics reveals widespread full
 phosphorylation site occupancy during mitosis.";
 Sci. Signal. 3:RA3-RA3(2010).
 [12]
 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
 METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
 SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22814378; DOI=10.1073/pnas.1210303109;
 Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
 Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
 Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
 Aldabe R.;
 "N-terminal acetylome analyses and functional insights of the N-
 terminal acetyltransferase NatB.";
 Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
 [13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-375, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [14]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
 Wang L., Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human
 liver phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [15]
 METHYLATION [LARGE SCALE ANALYSIS] AT LYS-334 AND ARG-442, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Colon carcinoma;
 PubMed=24129315; DOI=10.1074/mcp.O113.027870;
 Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
 Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
 Vemulapalli V., Bedford M.T., Comb M.J.;
 "Immunoaffinity enrichment and mass spectrometry analysis of protein
 methylation.";
 Mol. Cell. Proteomics 13:372-387(2014).
 -!- FUNCTION: May act as an adapter protein and couple activated
     growth factor receptors to a signaling pathway that regulates the
     proliferation in breast cancer cells. When overexpressed, it
     confers anti-estrogen resistance in breast cancer cell lines. May
     also be regulated by cellular adhesion to extracellular matrix
     proteins. {ECO:0000269|PubMed:9582273}.
 -!- SUBUNIT: Interacts with BCAR1, NEDD9, PTK2/FAK1 and PTPN1.
     {ECO:0000250}.
 -!- INTERACTION:
     P56945:BCAR1; NbExp=3; IntAct=EBI-15953103, EBI-702093;
     P04626:ERBB2; NbExp=2; IntAct=EBI-702336, EBI-641062;
     P35568:IRS1; NbExp=3; IntAct=EBI-702336, EBI-517592;
     P10721:KIT; NbExp=3; IntAct=EBI-702336, EBI-1379503;
     Q14511:NEDD9; NbExp=3; IntAct=EBI-702336, EBI-2108053;
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=O75815-1; Sequence=Displayed;
     Name=2;
       IsoId=O75815-2; Sequence=VSP_017814;
       Note=No experimental confirmation available.;
     Name=3;
       IsoId=O75815-3; Sequence=VSP_046716, VSP_046717;
       Note=No experimental confirmation available.;
 -!- TISSUE SPECIFICITY: Ubiquitously expressed. Found in several
     cancer cell lines, but not in nonmalignant breast tissue.
     {ECO:0000269|PubMed:10187783, ECO:0000269|PubMed:9582273}.
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 EMBL; U92715; AAC39777.1; -; mRNA.
 EMBL; AF124250; AAD28245.1; -; mRNA.
 EMBL; AY358996; AAQ89355.1; -; mRNA.
 EMBL; AL833121; -; NOT_ANNOTATED_CDS; mRNA.
 EMBL; AL049796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL109613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL359820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL512488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471097; EAW73065.1; -; Genomic_DNA.
 EMBL; CH471097; EAW73066.1; -; Genomic_DNA.
 EMBL; CH471097; EAW73068.1; -; Genomic_DNA.
 EMBL; BC039895; AAH39895.1; -; mRNA.
 CCDS; CCDS58010.1; -. [O75815-3]
 CCDS; CCDS745.1; -. [O75815-1]
 CCDS; CCDS76181.1; -. [O75815-2]
 RefSeq; NP_001248337.1; NM_001261408.1. [O75815-1]
 RefSeq; NP_001248338.1; NM_001261409.1. [O75815-1]
 RefSeq; NP_001248339.1; NM_001261410.1. [O75815-3]
 RefSeq; NP_001295180.1; NM_001308251.1. [O75815-2]
 RefSeq; NP_003558.1; NM_003567.3. [O75815-1]
 RefSeq; XP_016857969.1; XM_017002480.1. [O75815-1]
 UniGene; Hs.36958; -.
 PDB; 3T6A; X-ray; 2.40 A; A/B/C/D=502-825.
 PDBsum; 3T6A; -.
 ProteinModelPortal; O75815; -.
 SMR; O75815; -.
 BioGrid; 114000; 38.
 DIP; DIP-33857N; -.
 IntAct; O75815; 38.
 MINT; O75815; -.
 STRING; 9606.ENSP00000260502; -.
 iPTMnet; O75815; -.
 PhosphoSitePlus; O75815; -.
 BioMuta; BCAR3; -.
 EPD; O75815; -.
 MaxQB; O75815; -.
 PaxDb; O75815; -.
 PeptideAtlas; O75815; -.
 PRIDE; O75815; -.
 DNASU; 8412; -.
 Ensembl; ENST00000260502; ENSP00000260502; ENSG00000137936. [O75815-1]
 Ensembl; ENST00000370243; ENSP00000359263; ENSG00000137936. [O75815-1]
 Ensembl; ENST00000370244; ENSP00000359264; ENSG00000137936. [O75815-1]
 Ensembl; ENST00000370247; ENSP00000359267; ENSG00000137936. [O75815-3]
 Ensembl; ENST00000539242; ENSP00000441343; ENSG00000137936. [O75815-2]
 GeneID; 8412; -.
 KEGG; hsa:8412; -.
 UCSC; uc001dpx.6; human. [O75815-1]
 CTD; 8412; -.
 DisGeNET; 8412; -.
 EuPathDB; HostDB:ENSG00000137936.16; -.
 GeneCards; BCAR3; -.
 HGNC; HGNC:973; BCAR3.
 HPA; HPA014858; -.
 MIM; 604704; gene.
 neXtProt; NX_O75815; -.
 OpenTargets; ENSG00000137936; -.
 PharmGKB; PA25283; -.
 eggNOG; ENOG410IFQG; Eukaryota.
 eggNOG; ENOG410XTJR; LUCA.
 GeneTree; ENSGT00390000008976; -.
 HOGENOM; HOG000231595; -.
 HOVERGEN; HBG053174; -.
 InParanoid; O75815; -.
 OMA; NYCELNP; -.
 OrthoDB; EOG091G01KG; -.
 PhylomeDB; O75815; -.
 TreeFam; TF323756; -.
 SignaLink; O75815; -.
 ChiTaRS; BCAR3; human.
 GeneWiki; BCAR3; -.
 GenomeRNAi; 8412; -.
 PRO; PR:O75815; -.
 Proteomes; UP000005640; Chromosome 1.
 Bgee; ENSG00000137936; -.
 CleanEx; HS_BCAR3; -.
 Genevisible; O75815; HS.
 GO; GO:0005622; C:intracellular; IEA:GOC.
 GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
 GO; GO:0005070; F:SH3/SH2 adaptor activity; IBA:GO_Central.
 GO; GO:0002089; P:lens morphogenesis in camera-type eye; IEA:Ensembl.
 GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
 GO; GO:0042493; P:response to drug; TAS:ProtInc.
 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
 GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
 CDD; cd00155; RasGEF; 1.
 Gene3D; 1.10.840.10; -; 1.
 Gene3D; 3.30.505.10; -; 1.
 InterPro; IPR028849; BCAR3.
 InterPro; IPR023578; Ras_GEF_dom_sf.
 InterPro; IPR001895; RASGEF_cat_dom.
 InterPro; IPR036964; RASGEF_cat_dom_sf.
 InterPro; IPR000980; SH2.
 InterPro; IPR036860; SH2_dom_sf.
 PANTHER; PTHR14247:SF10; PTHR14247:SF10; 1.
 Pfam; PF00617; RasGEF; 1.
 Pfam; PF00017; SH2; 1.
 SMART; SM00147; RasGEF; 1.
 SMART; SM00252; SH2; 1.
 SUPFAM; SSF48366; SSF48366; 1.
 SUPFAM; SSF55550; SSF55550; 1.
 PROSITE; PS50009; RASGEF_CAT; 1.
 PROSITE; PS50001; SH2; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Alternative splicing; Complete proteome;
 Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
 Polymorphism; Reference proteome; SH2 domain.
 INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
 CHAIN         2    825       Breast cancer anti-estrogen resistance
                              protein 3.
                              /FTId=PRO_0000230284.
 DOMAIN      154    253       SH2. {ECO:0000255|PROSITE-
                              ProRule:PRU00191}.
 DOMAIN      548    818       Ras-GEF. {ECO:0000255|PROSITE-
                              ProRule:PRU00168}.
 COMPBIAS    479    482       Poly-Asp.
 MOD_RES       2      2       N-acetylalanine.
                              {ECO:0000244|PubMed:22814378}.
 MOD_RES      32     32       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES      78     78       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES      83     83       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     182    182       Phosphoserine.
                              {ECO:0000244|PubMed:16964243}.
 MOD_RES     290    290       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     334    334       N6-methyllysine.
                              {ECO:0000244|PubMed:24129315}.
 MOD_RES     358    358       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     363    363       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     375    375       Phosphoserine.
                              {ECO:0000244|PubMed:16964243,
                              ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     442    442       Omega-N-methylarginine.
                              {ECO:0000244|PubMed:24129315}.
 MOD_RES     471    471       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q9QZK2}.
 VAR_SEQ       1    324       Missing (in isoform 2).
                              {ECO:0000303|PubMed:12975309}.
                              /FTId=VSP_017814.
 VAR_SEQ       1     91       Missing (in isoform 3).
                              {ECO:0000303|PubMed:17974005}.
                              /FTId=VSP_046716.
 VAR_SEQ      92    117       ESPWQDRHGETFTFRDPHLLDPTVEY -> MPKECSAFHAL
                              SAALCCFYHRKSFIG (in isoform 3).
                              {ECO:0000303|PubMed:17974005}.
                              /FTId=VSP_046717.
 VARIANT     464    464       E -> G (in dbSNP:rs12062278).
                              /FTId=VAR_050689.
 VARIANT     593    593       Q -> H (in dbSNP:rs17110107).
                              /FTId=VAR_050690.
 CONFLICT    519    519       E -> G (in Ref. 4; AL833121).
                              {ECO:0000305}.
 CONFLICT    543    543       L -> P (in Ref. 4; AL833121).
                              {ECO:0000305}.
 HELIX       517    519       {ECO:0000244|PDB:3T6A}.
 HELIX       534    546       {ECO:0000244|PDB:3T6A}.
 HELIX       549    563       {ECO:0000244|PDB:3T6A}.
 HELIX       571    577       {ECO:0000244|PDB:3T6A}.
 STRAND      578    580       {ECO:0000244|PDB:3T6A}.
 HELIX       582    585       {ECO:0000244|PDB:3T6A}.
 HELIX       589    591       {ECO:0000244|PDB:3T6A}.
 HELIX       592    614       {ECO:0000244|PDB:3T6A}.
 HELIX       620    639       {ECO:0000244|PDB:3T6A}.
 HELIX       644    655       {ECO:0000244|PDB:3T6A}.
 HELIX       657    660       {ECO:0000244|PDB:3T6A}.
 HELIX       663    672       {ECO:0000244|PDB:3T6A}.
 HELIX       674    682       {ECO:0000244|PDB:3T6A}.
 HELIX       684    692       {ECO:0000244|PDB:3T6A}.
 HELIX       696    698       {ECO:0000244|PDB:3T6A}.
 HELIX       711    717       {ECO:0000244|PDB:3T6A}.
 HELIX       724    726       {ECO:0000244|PDB:3T6A}.
 HELIX       732    734       {ECO:0000244|PDB:3T6A}.
 HELIX       737    752       {ECO:0000244|PDB:3T6A}.
 HELIX       754    764       {ECO:0000244|PDB:3T6A}.
 TURN        765    767       {ECO:0000244|PDB:3T6A}.
 HELIX       772    777       {ECO:0000244|PDB:3T6A}.
 HELIX       780    792       {ECO:0000244|PDB:3T6A}.
 HELIX       797    815       {ECO:0000244|PDB:3T6A}.
 SEQUENCE   825 AA;  92566 MW;  C55D61BB4AC7D0F2 CRC64;
 MAAGKFASLP RNMPVNHQFP LASSMDLLSS RSPLAEHRPD AYQDVSIHGT LPRKKKGPPP
 IRSCDDFSHM GTLPHSKSPR QNSPVTQDGI QESPWQDRHG ETFTFRDPHL LDPTVEYVKF
 SKERHIMDRT PEKLKKELEE ELLLSSEDLR SHAWYHGRIP RQVSENLVQR DGDFLVRDSL
 SSPGNFVLTC QWKNLAQHFK INRTVLRLSE AYSRVQYQFE MESFDSIPGL VRCYVGNRRP
 ISQQSGAIIF QPINRTVPLR CLEEHYGTSP GQAREGSLTK GRPDVAKRLS LTMGGVQARE
 QNLPRGNLLR NKEKSGSQPA CLDHMQDRRA LSLKAHQSES YLPIGCKLPP QSSGVDTSPC
 PNSPVFRTGS EPALSPAVVR RVSSDARAGE ALRGSDSQLC PKPPPKPCKV PFLKVPSSPS
 AWLNSEANYC ELNPAFATGC GRGAKLPSCA QGSHTELLTA KQNEAPGPRN SGVNYLILDD
 DDRERPWEPA AAQMEKGQWD KGEFVTPLLE TVSSFRPNEF ESKFLPPENK PLETAMLKRA
 KELFTNNDPK VIAQHVLSMD CRVARILGVS EEMRRNMGVS SGLELITLPH GHQLRLDIIE
 RHNTMAIGIA VDILGCTGTL EDRAATLSKI IQVAVELKDS MGDLYSFSAL MKALEMPQIT
 RLEKTWTALR HQYTQTAILY EKQLKPFSKL LHEGRESTCV PPNNVSVPLL MPLVTLMERQ
 AVTFEGTDMW EKNDQSCEIM LNHLATARFM AEAADSYRMN AERILAGFQP DEEMNEICKT
 EFQMRLLWGS KGAQVNQTER YEKFNQILTA LSRKLEPPPV KQAEL

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