LG3BP_HUMAN
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 03-AUG-2022, entry version 194.
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; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 272.
DR IntAct; Q08380; 149.
DR MINT; Q08380; -.
DR STRING; 9606.ENSP00000262776; -.
DR GlyConnect; 1256; 74 N-Linked glycans (6 sites).
DR GlyGen; Q08380; 9 sites, 86 N-linked glycans (6 sites), 2 O-linked glycans (2 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; Q08380; -.
DR PeptideAtlas; Q08380; -.
DR PRIDE; Q08380; -.
DR ProteomicsDB; 58606; -.
DR Antibodypedia; 604; 429 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 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; 1174057at2759; -.
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 1118 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 196 other tissues.
DR ExpressionAtlas; Q08380; baseline and differential.
DR Genevisible; Q08380; HS.
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 Gene3D; 3.10.250.10; -; 1.
DR Gene3D; 3.30.710.10; -; 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 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; SSF56487; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
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
