ID   LG3BP_HUMAN             Reviewed;         585 AA.
AC   Q08380; Q7M4S0; Q9UCH8; Q9UCH9; Q9UCI0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 203.
DE   RecName: Full=Galectin-3-binding protein;
DE   AltName: Full=Basement membrane autoantigen p105;
DE   AltName: Full=Lectin galactoside-binding soluble 3-binding protein;
DE   AltName: Full=Mac-2-binding protein;
DE            Short=MAC2BP;
DE            Short=Mac-2 BP;
DE   AltName: Full=Tumor-associated antigen 90K;
DE   Flags: Precursor;
GN   Name=LGALS3BP; Synonyms=M2BP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-34; 188-191; 193-200;
RP   202-207; 230-242; 244-259; 261-267; 324-328 AND 437-440, INTERACTION WITH
RP   LGALS3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=8390986; DOI=10.1016/s0021-9258(19)85233-x;
RA   Koths K., Taylor E., Halenbeck R., Casipit C., Wang A.;
RT   "Cloning and characterization of a human Mac-2-binding protein, a new
RT   member of the superfamily defined by the macrophage scavenger receptor
RT   cysteine-rich domain.";
RL   J. Biol. Chem. 268:14245-14249(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=8034587; DOI=10.1016/s0021-9258(17)32322-0;
RA   Ullrich A., Sures I., D'Egido M., Jallal B., Powell T.J., Herbst R.,
RA   Dreps A., Azam M., Rubinstein M., Natoli C.;
RT   "The secreted tumor-associated antigen 90K is a potent immune stimulator.";
RL   J. Biol. Chem. 269:18401-18407(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Lung;
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   [4]
RP   PROTEIN SEQUENCE OF 19-40.
RC   TISSUE=Ascites, and Serum;
RX   PubMed=8454062; DOI=10.1016/0014-5793(93)80037-u;
RA   Iacobelli S., Bucci I., D'Egidio M., Giuliani C., Natoli C., Tinari N.,
RA   Rubistein M., Schlessinger J.;
RT   "Purification and characterization of a 90 kDa protein released from human
RT   tumors and tumor cell lines.";
RL   FEBS Lett. 319:59-65(1993).
RN   [5]
RP   PROTEIN SEQUENCE OF 19-38, AND TISSUE SPECIFICITY.
RC   TISSUE=Fibroblast;
RX   PubMed=8757764; DOI=10.1111/1523-1747.ep12329629;
RA   Chan L.S., Woodley D.T.;
RT   "The 105-kDa basement membrane autoantigen p105 is N-terminally homologous
RT   to a tumor-associated antigen.";
RL   J. Invest. Dermatol. 107:209-214(1996).
RN   [6]
RP   PROTEIN SEQUENCE OF 442-446, GLYCOSYLATION, INTERACTION WITH LGALS3, AND
RP   SUBUNIT STRUCTURE.
RX   PubMed=11867635; DOI=10.1074/jbc.m200386200;
RA   Hellstern S., Sasaki T., Fauser C., Lustig A., Timpl R., Engel J.;
RT   "Functional studies on recombinant domains of Mac-2-binding protein.";
RL   J. Biol. Chem. 277:15690-15696(2002).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH LGALS1 AND LGALS3.
RX   PubMed=11146440;
RX   DOI=10.1002/1097-0215(200002)9999:9999<::aid-ijc1022>3.3.co;2-q;
RA   Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S., Liu F.-T.;
RT   "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-
RT   1-induced cell aggregation.";
RL   Int. J. Cancer 91:167-172(2001).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
RC   TISSUE=Bile;
RX   PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA   Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA   Argani P., Goggins M.G., Maitra A., Pandey A.;
RT   "A proteomic analysis of human bile.";
RL   Mol. Cell. Proteomics 3:715-728(2004).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192; ASN-398;
RP   ASN-551 AND ASN-580.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-398; ASN-551 AND
RP   ASN-580.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-551.
RC   TISSUE=Milk;
RX   PubMed=18780401; DOI=10.1002/pmic.200701057;
RA   Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT   "Identification of N-linked glycoproteins in human milk by hydrophilic
RT   interaction liquid chromatography and mass spectrometry.";
RL   Proteomics 8:3833-3847(2008).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-125; ASN-192; ASN-398
RP   AND ASN-551.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   GLYCOSYLATION AT ASN-69; ASN-398; ASN-551 AND ASN-580.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
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., Buerckstuemmer T.,
RA   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   INTERACTION WITH CDK5RAP2; GAMMA-TUBULIN RING COMPLEX AND PDE4DIP.
RX   PubMed=29162697; DOI=10.1073/pnas.1705682114;
RA   Bouguenina H., Salaun D., Mangon A., Muller L., Baudelet E., Camoin L.,
RA   Tachibana T., Cianferani S., Audebert S., Verdier-Pinard P., Badache A.;
RT   "EB1-binding-myomegalin protein complex promotes centrosomal microtubules
RT   functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E10687-E10696(2017).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-133, FUNCTION, SUBCELLULAR
RP   LOCATION, GLYCOSYLATION AT ASN-69, INTERACTION WITH ITGB1; COL4A1; COL5A1;
RP   COL6A1; LGALS3; FN1 AND NID, AND DISULFIDE BONDS.
RX   PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA   Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT   "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT   matrix which self-assembles into ring-like structures and binds beta1
RT   integrins, collagens and fibronectin.";
RL   EMBO J. 17:1606-1613(1998).
CC   -!- FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host
CC       defense against viruses and tumor cells. {ECO:0000269|PubMed:11146440,
CC       ECO:0000269|PubMed:8034587, ECO:0000269|PubMed:9501082}.
CC   -!- SUBUNIT: Homodimers and homomultimers. The multimers form ring-like
CC       structures with a diameter of 30-40 nm. Binds LGALS1 and LGALS3. Binds
CC       ITGB1, COL4A1, COL5A1, COL6A1, FN1 and NID. Interacts with the gamma-
CC       tubulin ring complex (gamma-TuRC), composed of gamma-tubulin, TUBGCP2,
CC       TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 (PubMed:29162697). The
CC       unglycosylated form interacts with PDE4DIP isoform 13/MMG8/SMYLE; this
CC       interaction may connect a pericentrosomal complex, made of AKAP9,
CC       CDK5RAP2, EB1/MAPRE1 and PDE4DIP, to the gamma-tubulin ring complex
CC       (gamma-TuRC) to promote microtubule assembly and acetylation
CC       (PubMed:29162697). {ECO:0000269|PubMed:11867635,
CC       ECO:0000269|PubMed:29162697}.
CC   -!- INTERACTION:
CC       Q08380; Q9BZR8: BCL2L14; NbExp=2; IntAct=EBI-354956, EBI-1385773;
CC       Q08380; P13569: CFTR; NbExp=18; IntAct=EBI-354956, EBI-349854;
CC       Q08380; Q9NRD1: FBXO6; NbExp=2; IntAct=EBI-354956, EBI-3938499;
CC       Q08380; P20591: MX1; NbExp=2; IntAct=EBI-354956, EBI-929476;
CC       Q08380; Q9Y3Z3: SAMHD1; NbExp=2; IntAct=EBI-354956, EBI-1054601;
CC       Q08380; O00220: TNFRSF10A; NbExp=2; IntAct=EBI-354956, EBI-518861;
CC       Q08380; O95183: VAMP5; NbExp=2; IntAct=EBI-354956, EBI-10191195;
CC       Q08380; P40337-2: VHL; NbExp=3; IntAct=EBI-354956, EBI-12157263;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8390986}. Secreted,
CC       extracellular space, extracellular matrix {ECO:0000269|PubMed:9501082}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Detected in body fluids such as semen,
CC       milk, serum, tears, saliva and urine. Expressed by keratinocytes and
CC       fibroblasts. {ECO:0000269|PubMed:8034587, ECO:0000269|PubMed:8390986,
CC       ECO:0000269|PubMed:8757764}.
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DR   EMBL; L13210; AAA36193.1; -; mRNA.
DR   EMBL; X79089; CAA55699.1; -; mRNA.
DR   EMBL; BC002403; AAH02403.1; -; mRNA.
DR   EMBL; BC002998; AAH02998.1; -; mRNA.
DR   EMBL; BC015761; AAH15761.1; -; mRNA.
DR   CCDS; CCDS11759.1; -.
DR   PIR; A47161; A47161.
DR   PIR; A55899; A55899.
DR   RefSeq; NP_005558.1; NM_005567.3.
DR   PDB; 1BY2; X-ray; 2.00 A; A=19-133.
DR   PDB; 6GFB; X-ray; 2.08 A; A/B=124-250.
DR   PDBsum; 1BY2; -.
DR   PDBsum; 6GFB; -.
DR   AlphaFoldDB; Q08380; -.
DR   SMR; Q08380; -.
DR   BioGRID; 110150; 301.
DR   IntAct; Q08380; 162.
DR   MINT; Q08380; -.
DR   STRING; 9606.ENSP00000262776; -.
DR   GlyConnect; 1256; 74 N-Linked glycans (6 sites).
DR   GlyCosmos; Q08380; 9 sites, 88 glycans.
DR   GlyGen; Q08380; 12 sites, 100 N-linked glycans (6 sites), 3 O-linked glycans (5 sites).
DR   iPTMnet; Q08380; -.
DR   PhosphoSitePlus; Q08380; -.
DR   SwissPalm; Q08380; -.
DR   BioMuta; LGALS3BP; -.
DR   DMDM; 47115668; -.
DR   CPTAC; CPTAC-534; -.
DR   CPTAC; CPTAC-535; -.
DR   CPTAC; CPTAC-670; -.
DR   CPTAC; non-CPTAC-1125; -.
DR   CPTAC; non-CPTAC-2670; -.
DR   EPD; Q08380; -.
DR   jPOST; Q08380; -.
DR   MassIVE; Q08380; -.
DR   MaxQB; Q08380; -.
DR   PaxDb; 9606-ENSP00000262776; -.
DR   PeptideAtlas; Q08380; -.
DR   PRIDE; Q08380; -.
DR   ProteomicsDB; 58606; -.
DR   Pumba; Q08380; -.
DR   Antibodypedia; 604; 506 antibodies from 35 providers.
DR   DNASU; 3959; -.
DR   Ensembl; ENST00000262776.8; ENSP00000262776.2; ENSG00000108679.13.
DR   GeneID; 3959; -.
DR   KEGG; hsa:3959; -.
DR   MANE-Select; ENST00000262776.8; ENSP00000262776.2; NM_005567.4; NP_005558.1.
DR   UCSC; uc002jwh.4; human.
DR   AGR; HGNC:6564; -.
DR   CTD; 3959; -.
DR   DisGeNET; 3959; -.
DR   GeneCards; LGALS3BP; -.
DR   HGNC; HGNC:6564; LGALS3BP.
DR   HPA; ENSG00000108679; Low tissue specificity.
DR   MIM; 600626; gene.
DR   neXtProt; NX_Q08380; -.
DR   OpenTargets; ENSG00000108679; -.
DR   PharmGKB; PA30341; -.
DR   VEuPathDB; HostDB:ENSG00000108679; -.
DR   eggNOG; ENOG502QU48; Eukaryota.
DR   GeneTree; ENSGT00940000162516; -.
DR   HOGENOM; CLU_032646_0_0_1; -.
DR   InParanoid; Q08380; -.
DR   OrthoDB; 5397373at2759; -.
DR   PhylomeDB; Q08380; -.
DR   TreeFam; TF331368; -.
DR   PathwayCommons; Q08380; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   SignaLink; Q08380; -.
DR   SIGNOR; Q08380; -.
DR   BioGRID-ORCS; 3959; 18 hits in 1199 CRISPR screens.
DR   ChiTaRS; LGALS3BP; human.
DR   EvolutionaryTrace; Q08380; -.
DR   GeneWiki; LGALS3BP; -.
DR   GenomeRNAi; 3959; -.
DR   Pharos; Q08380; Tbio.
DR   PRO; PR:Q08380; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q08380; Protein.
DR   Bgee; ENSG00000108679; Expressed in right adrenal gland cortex and 198 other cell types or tissues.
DR   ExpressionAtlas; Q08380; baseline and differential.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
DR   GO; GO:0005044; F:scavenger receptor activity; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd18496; BACK_LGALS3BP; 1.
DR   CDD; cd18304; BTB_POZ_M2BP; 1.
DR   Gene3D; 1.25.40.420; -; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   PANTHER; PTHR24410:SF16; GALECTIN-3-BINDING PROTEIN; 1.
DR   PANTHER; PTHR24410; HL07962P-RELATED; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00530; SRCR; 1.
DR   PRINTS; PR00258; SPERACTRCPTR.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00202; SR; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00420; SRCR_1; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   Genevisible; Q08380; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8390986,
FT                   ECO:0000269|PubMed:8454062, ECO:0000269|PubMed:8757764"
FT   CHAIN           19..585
FT                   /note="Galectin-3-binding protein"
FT                   /id="PRO_0000033230"
FT   DOMAIN          24..124
FT                   /note="SRCR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DOMAIN          153..221
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          260..360
FT                   /note="BACK"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15084671,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
FT                   ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
FT                   ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9501082"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401,
FT                   ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490"
FT   DISULFID        49..113
FT                   /evidence="ECO:0000269|PubMed:9501082,
FT                   ECO:0007744|PDB:1BY2"
FT   DISULFID        62..123
FT                   /evidence="ECO:0000269|PubMed:9501082,
FT                   ECO:0007744|PDB:1BY2"
FT   DISULFID        93..103
FT                   /evidence="ECO:0000269|PubMed:9501082,
FT                   ECO:0007744|PDB:1BY2"
FT   CONFLICT        19
FT                   /note="V -> S (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="R -> C (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="R -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="L -> M (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30..31
FT                   /note="GA -> ED (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="R -> H (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="R -> L (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   HELIX           55..64
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   TURN            76..79
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:1BY2"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           139..149
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   STRAND          155..161
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   STRAND          164..171
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   STRAND          191..196
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           199..204
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           205..214
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   STRAND          215..219
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           224..234
FT                   /evidence="ECO:0007829|PDB:6GFB"
FT   HELIX           237..246
FT                   /evidence="ECO:0007829|PDB:6GFB"
SQ   SEQUENCE   585 AA;  65331 MW;  C488C2E99D77435B CRC64;
     MTPPRLFWVW LLVAGTQGVN DGDMRLADGG ATNQGRVEIF YRGQWGTVCD NLWDLTDASV
     VCRALGFENA TQALGRAAFG QGSGPIMLDE VQCTGTEASL ADCKSLGWLK SNCRHERDAG
     VVCTNETRST HTLDLSRELS EALGQIFDSQ RGCDLSISVN VQGEDALGFC GHTVILTANL
     EAQALWKEPG SNVTMSVDAE CVPMVRDLLR YFYSRRIDIT LSSVKCFHKL ASAYGARQLQ
     GYCASLFAIL LPQDPSFQMP LDLYAYAVAT GDALLEKLCL QFLAWNFEAL TQAEAWPSVP
     TDLLQLLLPR SDLAVPSELA LLKAVDTWSW GERASHEEVE GLVEKIRFPM MLPEELFELQ
     FNLSLYWSHE ALFQKKTLQA LEFHTVPFQL LARYKGLNLT EDTYKPRIYT SPTWSAFVTD
     SSWSARKSQL VYQSRRGPLV KYSSDYFQAP SDYRYYPYQS FQTPQHPSFL FQDKRVSWSL
     VYLPTIQSCW NYGFSCSSDE LPVLGLTKSG GSDRTIAYEN KALMLCEGLF VADVTDFEGW
     KAAIPSALDT NSSKSTSSFP CPAGHFNGFR TVIRPFYLTN SSGVD
//