LEG10_HUMAN
ID LEG10_HUMAN Reviewed; 142 AA.
AC Q05315; C5HZ13; C5HZ14; Q0VDE3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Galectin-10;
DE Short=Gal-10;
DE AltName: Full=Charcot-Leyden crystal protein;
DE Short=CLC;
DE AltName: Full=Eosinophil lysophospholipase;
DE AltName: Full=Lysolecithin acylhydrolase;
GN Name=CLC; Synonyms=LGALS10, LGALS10A;
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 3-18 AND 93-110, AND
RP VARIANT VAL-28.
RX PubMed=8419478;
RA Ackerman S.J., Corrette S.E., Rosenberg H.F., Bennett J.C.,
RA Mastrianni D.M., Nicholson-Weller A., Weller P.F., Chin D.T., Tenen D.G.;
RT "Molecular cloning and characterization of human eosinophil Charcot-Leyden
RT crystal protein (lysophospholipase). Similarities to IgE binding proteins
RT and the S-type animal lectin superfamily.";
RL J. Immunol. 150:456-468(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-28.
RX PubMed=1577491; DOI=10.1016/0888-7543(92)90237-m;
RA Mastrianni D.M., Eddy R.L., Rosenberg H.F., Corrette S.E., Shows T.B.,
RA Tenen D.G., Ackerman S.J.;
RT "Localization of the human eosinophil Charcot-Leyden crystal protein
RT (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease
RT 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic
RT protein) genes (RNS2 and RNS3) to chromosome 14.";
RL Genomics 13:240-242(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-28.
RX PubMed=9119387; DOI=10.1006/geno.1996.4590;
RA Dyer K.D., Handen J.S., Rosenberg H.F.;
RT "The genomic structure of the human Charcot-Leyden crystal protein gene is
RT analogous to those of the galectin genes.";
RL Genomics 40:217-221(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT VAL-28.
RC TISSUE=Placenta;
RX PubMed=19497882; DOI=10.1073/pnas.0903568106;
RA Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y.,
RA Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J., Kim J.S.,
RA Haidarian S., Uddin M., Bohn H., Benirschke K., Santolaya-Forgas J.,
RA Grossman L.I., Erez O., Hassan S.S., Zavodszky P., Papp Z., Wildman D.E.;
RT "A primate subfamily of galectins expressed at the maternal-fetal interface
RT that promote immune cell death.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-28.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-28.
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 [8]
RP PROTEIN SEQUENCE OF 2-23; 92-99 AND 135-141, ACETYLATION AT SER-2, LACK OF
RP GLYCOSYLATION AT ASN-136, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16457599; DOI=10.1021/pr050341h;
RA Ghafouri B., Irander K., Lindbom J., Tagesson C., Lindahl M.;
RT "Comparative proteomics of nasal fluid in seasonal allergic rhinitis.";
RL J. Proteome Res. 5:330-338(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17502455; DOI=10.1182/blood-2007-01-069229;
RA Kubach J., Lutter P., Bopp T., Stoll S., Becker C., Huter E., Richter C.,
RA Weingarten P., Warger T., Knop J., Muellner S., Wijdenes J., Schild H.,
RA Schmitt E., Jonuleit H.;
RT "Human CD4+CD25+ regulatory T cells: proteome analysis identifies galectin-
RT 10 as a novel marker essential for their anergy and suppressive function.";
RL Blood 110:1550-1558(2007).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=19758173; DOI=10.1111/j.1749-6632.2009.04627.x;
RA De Re V., Simula M.P., Cannizzaro R., Pavan A., De Zorzi M.A., Toffoli G.,
RA Canzonieri V.;
RT "Galectin-10, eosinophils, and celiac disease.";
RL Ann. N. Y. Acad. Sci. 1173:357-364(2009).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=22880030; DOI=10.1371/journal.pone.0042549;
RA Chua J.C., Douglass J.A., Gillman A., O'Hehir R.E., Meeusen E.N.;
RT "Galectin-10, a potential biomarker of eosinophilic airway inflammation.";
RL PLoS ONE 7:E42549-E42549(2012).
RN [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8747464; DOI=10.1016/s0969-2126(01)00275-1;
RA Leonidas D.D., Elbert B.L., Zhou Z., Leffler H., Ackerman S.J.,
RA Acharya K.R.;
RT "Crystal structure of human Charcot-Leyden crystal protein, an eosinophil
RT lysophospholipase, identifies it as a new member of the carbohydrate-
RT binding family of galectins.";
RL Structure 3:1379-1393(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10529229; DOI=10.1021/bi990756e;
RA Swaminathan G.J., Leonidas D.D., Savage M.P., Ackerman S.J., Acharya K.R.;
RT "Selective recognition of mannose by the human eosinophil Charcot-Leyden
RT crystal protein (galectin-10): a crystallographic study at 1.8 A
RT resolution.";
RL Biochemistry 38:13837-13843(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-139, ABSENCE OF
RP LYSOPHOSPHOLIPASE ACTIVITY, AND INTERACTION WITH CEL.
RX PubMed=11834744; DOI=10.1074/jbc.m200221200;
RA Ackerman S.J., Liu L., Kwatia M.A., Savage M.P., Leonidas D.D.,
RA Swaminathan G.J., Acharya K.R.;
RT "Charcot-Leyden crystal protein (galectin-10) is not a dual function
RT galectin with lysophospholipase activity but binds a lysophospholipase
RT inhibitor in a novel structural fashion.";
RL J. Biol. Chem. 277:14859-14868(2002).
CC -!- FUNCTION: Regulates immune responses through the recognition of cell-
CC surface glycans. Essential for the anergy and suppressive function of
CC CD25-positive regulatory T-cells (Treg). {ECO:0000269|PubMed:17502455}.
CC -!- SUBUNIT: Interacts with CEL. {ECO:0000269|PubMed:11834744}.
CC -!- INTERACTION:
CC Q05315; Q05315: CLC; NbExp=4; IntAct=EBI-10485101, EBI-10485101;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17502455}.
CC Cytoplasmic granule {ECO:0000269|PubMed:17502455}. Note=Localized in
CC granules from where it may be secreted or transported to other
CC locations in the cell.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in the bone marrow. Expressed
CC exclusively by eosinophils and basophils. Not detected in monocytes and
CC neutrophils. Expressed in CD25-positive regulatory T-cells (Treg) (at
CC protein level). Found in intestinal tissue from patients with Celiac
CC disease, expression is directly related to the histological grade of
CC mucosal damage and to the number of eosinophils found in the duodenal
CC lesion (at protein level). Found in sputum of patients with
CC eosinophilic inflammatory diseases such as asthma (at protein level).
CC {ECO:0000269|PubMed:17502455, ECO:0000269|PubMed:19497882,
CC ECO:0000269|PubMed:19758173, ECO:0000269|PubMed:22880030}.
CC -!- MISCELLANEOUS: Forms hexagonal bipyramidal crystals, known as Charcot-
CC Leyden crystals, in tissues and secretions from sites of eosinophil-
CC associated inflammation and some myeloid leukemias.
CC -!- CAUTION: Was originally thought to possess lysophospholipase activity
CC but the absence of this activity has been shown by PubMed:11834744.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-10;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_277";
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DR EMBL; L01664; AAA36190.1; -; mRNA.
DR EMBL; L01665; AAC37530.1; -; Genomic_DNA.
DR EMBL; U68398; AAC51157.1; -; Genomic_DNA.
DR EMBL; U68393; AAC51157.1; JOINED; Genomic_DNA.
DR EMBL; U68395; AAC51157.1; JOINED; Genomic_DNA.
DR EMBL; U68396; AAC51157.1; JOINED; Genomic_DNA.
DR EMBL; FJ613334; ACR09636.1; -; mRNA.
DR EMBL; FJ613335; ACR09637.1; -; mRNA.
DR EMBL; AC005393; AAC28912.1; -; Genomic_DNA.
DR EMBL; AC006133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW56914.1; -; Genomic_DNA.
DR EMBL; BC119711; AAI19712.1; -; mRNA.
DR EMBL; BC119712; AAI19713.1; -; mRNA.
DR CCDS; CCDS33025.1; -.
DR PIR; A46523; A46523.
DR RefSeq; NP_001819.2; NM_001828.5.
DR PDB; 1G86; X-ray; 1.80 A; A=1-142.
DR PDB; 1HDK; X-ray; 1.80 A; A=2-142.
DR PDB; 1LCL; X-ray; 1.80 A; A=1-142.
DR PDB; 1QKQ; X-ray; 1.80 A; A=1-142.
DR PDB; 5XRG; X-ray; 1.55 A; A=1-142.
DR PDB; 5XRH; X-ray; 1.55 A; A=1-142.
DR PDB; 5XRI; X-ray; 1.68 A; A=1-142.
DR PDB; 5XRJ; X-ray; 1.90 A; A=1-142.
DR PDB; 5XRK; X-ray; 1.70 A; A=1-142.
DR PDB; 5XRL; X-ray; 2.00 A; A=1-142.
DR PDB; 5XRM; X-ray; 2.00 A; A=1-142.
DR PDB; 5XRN; X-ray; 1.60 A; A=1-142.
DR PDB; 5XRO; X-ray; 1.60 A; A=1-142.
DR PDB; 5XRP; X-ray; 2.00 A; A=1-142.
DR PDB; 5YT4; X-ray; 2.00 A; A=2-139.
DR PDB; 6A1S; X-ray; 1.63 A; A=1-142.
DR PDB; 6A1T; X-ray; 1.97 A; A=1-142.
DR PDB; 6A1U; X-ray; 1.62 A; A=1-142.
DR PDB; 6A1V; X-ray; 1.98 A; A=1-142.
DR PDB; 6A1X; X-ray; 1.99 A; A=1-142.
DR PDB; 6A1Y; X-ray; 1.63 A; A=1-142.
DR PDB; 6GKQ; X-ray; 2.30 A; A=1-142.
DR PDB; 6GKS; X-ray; 1.38 A; A=1-142.
DR PDB; 6GKT; X-ray; 2.10 A; A/B/C/D/E/F=1-142.
DR PDB; 6GKU; X-ray; 1.91 A; A=1-142.
DR PDB; 6GLW; X-ray; 1.90 A; A/B=1-142.
DR PDB; 6GLX; X-ray; 3.40 A; A/B=1-142.
DR PDB; 6L64; X-ray; 2.08 A; A=1-142.
DR PDB; 6L67; X-ray; 1.97 A; A=1-142.
DR PDB; 6L68; X-ray; 1.92 A; A=1-142.
DR PDB; 6L6A; X-ray; 1.81 A; A=1-142.
DR PDB; 6L6B; X-ray; 1.80 A; A=1-142.
DR PDB; 6L6C; X-ray; 1.77 A; A=1-142.
DR PDB; 6L6D; X-ray; 1.93 A; A=1-142.
DR PDB; 6QRN; X-ray; 1.40 A; A=1-142.
DR PDBsum; 1G86; -.
DR PDBsum; 1HDK; -.
DR PDBsum; 1LCL; -.
DR PDBsum; 1QKQ; -.
DR PDBsum; 5XRG; -.
DR PDBsum; 5XRH; -.
DR PDBsum; 5XRI; -.
DR PDBsum; 5XRJ; -.
DR PDBsum; 5XRK; -.
DR PDBsum; 5XRL; -.
DR PDBsum; 5XRM; -.
DR PDBsum; 5XRN; -.
DR PDBsum; 5XRO; -.
DR PDBsum; 5XRP; -.
DR PDBsum; 5YT4; -.
DR PDBsum; 6A1S; -.
DR PDBsum; 6A1T; -.
DR PDBsum; 6A1U; -.
DR PDBsum; 6A1V; -.
DR PDBsum; 6A1X; -.
DR PDBsum; 6A1Y; -.
DR PDBsum; 6GKQ; -.
DR PDBsum; 6GKS; -.
DR PDBsum; 6GKT; -.
DR PDBsum; 6GKU; -.
DR PDBsum; 6GLW; -.
DR PDBsum; 6GLX; -.
DR PDBsum; 6L64; -.
DR PDBsum; 6L67; -.
DR PDBsum; 6L68; -.
DR PDBsum; 6L6A; -.
DR PDBsum; 6L6B; -.
DR PDBsum; 6L6C; -.
DR PDBsum; 6L6D; -.
DR PDBsum; 6QRN; -.
DR AlphaFoldDB; Q05315; -.
DR SASBDB; Q05315; -.
DR SMR; Q05315; -.
DR BioGRID; 107592; 2.
DR STRING; 9606.ENSP00000221804; -.
DR DrugBank; DB02967; N-Ethylmaleimide.
DR DrugBank; DB02983; Para-Mercury-Benzenesulfonic Acid.
DR UniLectin; Q05315; -.
DR iPTMnet; Q05315; -.
DR PhosphoSitePlus; Q05315; -.
DR BioMuta; CLC; -.
DR DMDM; 317373429; -.
DR jPOST; Q05315; -.
DR MassIVE; Q05315; -.
DR PaxDb; Q05315; -.
DR PeptideAtlas; Q05315; -.
DR PRIDE; Q05315; -.
DR ProteomicsDB; 58318; -.
DR TopDownProteomics; Q05315; -.
DR ABCD; Q05315; 3 sequenced antibodies.
DR Antibodypedia; 30409; 289 antibodies from 30 providers.
DR DNASU; 1178; -.
DR Ensembl; ENST00000221804.5; ENSP00000221804.3; ENSG00000105205.7.
DR GeneID; 1178; -.
DR KEGG; hsa:1178; -.
DR MANE-Select; ENST00000221804.5; ENSP00000221804.3; NM_001828.6; NP_001819.2.
DR UCSC; uc002omh.4; human.
DR CTD; 1178; -.
DR DisGeNET; 1178; -.
DR GeneCards; CLC; -.
DR HGNC; HGNC:2014; CLC.
DR HPA; ENSG00000105205; Tissue enriched (bone).
DR MIM; 153310; gene.
DR neXtProt; NX_Q05315; -.
DR OpenTargets; ENSG00000105205; -.
DR PharmGKB; PA26541; -.
DR VEuPathDB; HostDB:ENSG00000105205; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000163192; -.
DR HOGENOM; CLU_037794_4_0_1; -.
DR InParanoid; Q05315; -.
DR OMA; DKYQVMV; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; Q05315; -.
DR TreeFam; TF315551; -.
DR BRENDA; 3.1.1.5; 2681.
DR PathwayCommons; Q05315; -.
DR BioGRID-ORCS; 1178; 12 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; Q05315; -.
DR GeneWiki; CLC_(gene); -.
DR GenomeRNAi; 1178; -.
DR Pharos; Q05315; Tbio.
DR PRO; PR:Q05315; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q05315; protein.
DR Bgee; ENSG00000105205; Expressed in trabecular bone tissue and 114 other tissues.
DR Genevisible; Q05315; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046006; P:regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0002667; P:regulation of T cell anergy; IMP:UniProtKB.
DR GO; GO:0002724; P:regulation of T cell cytokine production; IMP:UniProtKB.
DR GO; GO:0070231; P:T cell apoptotic process; IDA:UniProtKB.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030648; Galectin_10.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF15; PTHR11346:SF15; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Lectin;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16457599"
FT CHAIN 2..142
FT /note="Galectin-10"
FT /id="PRO_0000076960"
FT DOMAIN 6..138
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT SITE 136
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:16457599"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16457599"
FT VARIANT 28
FT /note="A -> V (in dbSNP:rs17608)"
FT /evidence="ECO:0000269|PubMed:15057824,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1577491,
FT ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:8419478,
FT ECO:0000269|PubMed:9119387"
FT /id="VAR_014765"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:6GKS"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:6GKS"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6GKS"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6GKS"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:6GKS"
SQ SEQUENCE 142 AA; 16453 MW; 2744F0C082C6446E CRC64;
MSLLPVPYTE AASLSTGSTV TIKGRPLACF LNEPYLQVDF HTEMKEESDI VFHFQVCFGR
RVVMNSREYG AWKQQVESKN MPFQDGQEFE LSISVLPDKY QVMVNGQSSY TFDHRIKPEA
VKMVQVWRDI SLTKFNVSYL KR
