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 27-MAR-2024, entry version 203. 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"; 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; 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; 9606-ENSP00000221804; -. DR PeptideAtlas; Q05315; -. DR ProteomicsDB; 58318; -. DR TopDownProteomics; Q05315; -. DR ABCD; Q05315; 3 sequenced antibodies. DR Antibodypedia; 30409; 319 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 AGR; HGNC:2014; -. 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; 2874391at2759; -. DR PhylomeDB; Q05315; -. DR TreeFam; TF315551; -. DR BRENDA; 3.1.1.5; 2681. DR PathwayCommons; Q05315; -. DR BioGRID-ORCS; 1178; 13 hits in 1150 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 115 other cell types or tissues. 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 Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR044156; Galectin-like. DR InterPro; IPR001079; Galectin_CRD. DR PANTHER; PTHR11346; GALECTIN; 1. DR PANTHER; PTHR11346:SF15; GALECTIN-10-RELATED; 1. DR Pfam; PF00337; Gal-bind_lectin; 1. DR SMART; SM00908; Gal-bind_lectin; 1. DR SMART; SM00276; GLECT; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS51304; GALECTIN; 1. DR Genevisible; Q05315; HS. 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 //