CLC4C_HUMAN
ID CLC4C_HUMAN Reviewed; 213 AA.
AC Q8WTT0; D3DUU3; Q3T1C3; Q6UXS8; Q8WXX8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=C-type lectin domain family 4 member C;
DE AltName: Full=Blood dendritic cell antigen 2;
DE Short=BDCA-2;
DE AltName: Full=C-type lectin superfamily member 7;
DE AltName: Full=Dendritic lectin;
DE AltName: CD_antigen=CD303;
GN Name=CLEC4C; Synonyms=BDCA2, CLECSF11, CLECSF7, DLEC, HECL;
GN ORFNames=UNQ9361/PRO34150;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=11536172;
RX DOI=10.1002/1521-4141(200109)31:9<2733::aid-immu2733>3.0.co;2-x;
RA Arce I., Roda-Navarro P., Montoya M.C., Hernanz-Falcon P., Puig-Kroger A.,
RA Fernandez-Ruiz E.;
RT "Molecular and genomic characterization of human DLEC, a novel member of
RT the C-type lectin receptor gene family preferentially expressed on
RT monocyte-derived dendritic cells.";
RL Eur. J. Immunol. 31:2733-2740(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11748283; DOI=10.1084/jem.194.12.1823;
RA Dzionek A., Sohma Y., Nagafune J., Cella M., Colonna M., Facchetti F.,
RA Gunther G., Johnston I., Lanzavecchia A., Nagasaka T., Okada T., Vermi W.,
RA Winkels G., Yamamoto T., Zysk M., Yamaguchi Y., Schmitz J.;
RT "BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type
RT lectin, mediates antigen capture and is a potent inhibitor of interferon
RT alpha/beta induction.";
RL J. Exp. Med. 194:1823-1834(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=11031109; DOI=10.1006/geno.2000.6316;
RA Fernandes M.J., Iscove N.N., Gingras G., Calabretta B.;
RT "Identification and characterization of the gene for a novel C-type lectin
RT (CLECSF7) that maps near the natural killer gene complex on human
RT chromosome 12.";
RL Genomics 69:263-270(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21880719; DOI=10.1074/jbc.c111.290494;
RA Riboldi E., Daniele R., Parola C., Inforzato A., Arnold P.L., Bosisio D.,
RA Fremont D.H., Bastone A., Colonna M., Sozzani S.;
RT "Human C-type lectin domain family 4, member C (CLEC4C/BDCA-2/CD303) is a
RT receptor for asialo-galactosyl-oligosaccharides.";
RL J. Biol. Chem. 286:35329-35333(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 83-210, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=24425442; DOI=10.1002/prot.24504;
RA Nagae M., Ikeda A., Kitago Y., Matsumoto N., Yamamoto K., Yamaguchi Y.;
RT "Crystal structures of carbohydrate recognition domain of blood dendritic
RT cell antigen-2 (BDCA2) reveal a common domain-swapped dimer.";
RL Proteins 82:1512-1518(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 67-213 IN COMPLEX WITH
RP MONOSACCHARIDE; TRISACCHARIDE AND CALCIUM, SUBUNIT, DISULFIDE BONDS, AND
RP MUTAGENESIS OF ASN-184.
RX PubMed=25995448; DOI=10.1074/jbc.m115.660613;
RA Jegouzo S.A., Feinberg H., Dungarwalla T., Drickamer K., Weis W.I.,
RA Taylor M.E.;
RT "A novel mechanism for binding of galactose-terminated glycans by the C-
RT type carbohydrate recognition domain in blood dendritic cell antigen 2.";
RL J. Biol. Chem. 290:16759-16771(2015).
CC -!- FUNCTION: Lectin-type cell surface receptor which may play a role in
CC antigen capturing by dendritic cells (PubMed:11748283, PubMed:21880719,
CC PubMed:25995448). Specifically recognizes non-sialylated galactose-
CC terminated biantennary glycans containing the trisaccharide epitope
CC Gal(beta1-3/4)GlcNAc(beta1-2)Man (PubMed:21880719, PubMed:25995448).
CC Binds to serum IgG (PubMed:25995448). Efficiently targets ligand into
CC antigen-processing and peptide-loading compartments for presentation to
CC T-cells (PubMed:11748283). May mediate potent inhibition of induction
CC of IFN-alpha/beta expression in plasmacytoid dendritic cells
CC (PubMed:11748283, PubMed:21880719). May act as a signaling receptor
CC that activates protein-tyrosine kinases and mobilizes intracellular
CC calcium (PubMed:11748283). {ECO:0000269|PubMed:11748283,
CC ECO:0000269|PubMed:21880719, ECO:0000269|PubMed:25995448}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24425442,
CC ECO:0000269|PubMed:25995448}.
CC -!- INTERACTION:
CC Q8WTT0; Q8N7P3: CLDN22; NbExp=3; IntAct=EBI-12913226, EBI-17766761;
CC Q8WTT0; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-12913226, EBI-12007212;
CC Q8WTT0; P21145: MAL; NbExp=4; IntAct=EBI-12913226, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11748283,
CC ECO:0000269|PubMed:21880719}; Single-pass type II membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WTT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WTT0-2; Sequence=VSP_012845;
CC -!- TISSUE SPECIFICITY: Expressed in plasmacytoid dendritic cells (PDCs).
CC Constitutively expressed in immature monocyte-derived dendritic cells
CC (iMDDC) and is significantly down-regulated upon maturation with LPS
CC but not with TNF-alpha. {ECO:0000269|PubMed:11031109,
CC ECO:0000269|PubMed:11536172, ECO:0000269|PubMed:11748283}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=BDCA-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00133";
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DR EMBL; AF325459; AAL37358.1; -; mRNA.
DR EMBL; AF325460; AAL37359.1; -; mRNA.
DR EMBL; AF293615; AAL37036.1; -; mRNA.
DR EMBL; AY358223; AAQ88590.1; -; mRNA.
DR EMBL; CH471116; EAW88655.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88656.1; -; Genomic_DNA.
DR EMBL; BC074967; AAH74967.1; -; mRNA.
DR EMBL; BC074968; AAH74968.1; -; mRNA.
DR EMBL; BC102015; AAI02016.1; -; mRNA.
DR EMBL; BC102016; AAI02017.1; -; mRNA.
DR EMBL; BC102017; AAI02018.1; -; mRNA.
DR EMBL; BC114338; AAI14339.1; -; mRNA.
DR CCDS; CCDS8583.1; -. [Q8WTT0-1]
DR CCDS; CCDS8584.1; -. [Q8WTT0-2]
DR RefSeq; NP_569708.1; NM_130441.2. [Q8WTT0-1]
DR RefSeq; NP_987099.1; NM_203503.1. [Q8WTT0-2]
DR PDB; 3WBP; X-ray; 1.80 A; A/B=83-210.
DR PDB; 3WBQ; X-ray; 2.30 A; A/B=83-210.
DR PDB; 3WBR; X-ray; 2.20 A; A/B/C/D/E/F/G/H=83-210.
DR PDB; 4ZES; X-ray; 1.65 A; A/B=67-213.
DR PDB; 4ZET; X-ray; 2.90 A; A/B=67-213.
DR PDBsum; 3WBP; -.
DR PDBsum; 3WBQ; -.
DR PDBsum; 3WBR; -.
DR PDBsum; 4ZES; -.
DR PDBsum; 4ZET; -.
DR AlphaFoldDB; Q8WTT0; -.
DR SMR; Q8WTT0; -.
DR BioGRID; 128012; 27.
DR DIP; DIP-29513N; -.
DR IntAct; Q8WTT0; 4.
DR STRING; 9606.ENSP00000440428; -.
DR BindingDB; Q8WTT0; -.
DR ChEMBL; CHEMBL2176855; -.
DR MEROPS; I63.002; -.
DR UniLectin; Q8WTT0; -.
DR GlyGen; Q8WTT0; 3 sites.
DR BioMuta; CLEC4C; -.
DR DMDM; 59797957; -.
DR MassIVE; Q8WTT0; -.
DR PaxDb; Q8WTT0; -.
DR PeptideAtlas; Q8WTT0; -.
DR PRIDE; Q8WTT0; -.
DR ProteomicsDB; 74596; -. [Q8WTT0-1]
DR ProteomicsDB; 74597; -. [Q8WTT0-2]
DR ABCD; Q8WTT0; 50 sequenced antibodies.
DR Antibodypedia; 22963; 207 antibodies from 30 providers.
DR DNASU; 170482; -.
DR Ensembl; ENST00000354629.9; ENSP00000346648.5; ENSG00000198178.11. [Q8WTT0-2]
DR Ensembl; ENST00000360345.8; ENSP00000353500.3; ENSG00000198178.11. [Q8WTT0-1]
DR Ensembl; ENST00000540085.5; ENSP00000445338.1; ENSG00000198178.11. [Q8WTT0-2]
DR Ensembl; ENST00000542353.5; ENSP00000440428.1; ENSG00000198178.11. [Q8WTT0-1]
DR GeneID; 170482; -.
DR KEGG; hsa:170482; -.
DR MANE-Select; ENST00000360345.8; ENSP00000353500.3; NM_001371390.1; NP_001358319.1.
DR UCSC; uc001qtg.2; human. [Q8WTT0-1]
DR CTD; 170482; -.
DR DisGeNET; 170482; -.
DR GeneCards; CLEC4C; -.
DR HGNC; HGNC:13258; CLEC4C.
DR HPA; ENSG00000198178; Tissue enhanced (lymphoid).
DR MIM; 606677; gene.
DR neXtProt; NX_Q8WTT0; -.
DR OpenTargets; ENSG00000198178; -.
DR PharmGKB; PA26585; -.
DR VEuPathDB; HostDB:ENSG00000198178; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162867; -.
DR InParanoid; Q8WTT0; -.
DR OMA; PDERCAI; -.
DR OrthoDB; 1446150at2759; -.
DR PhylomeDB; Q8WTT0; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q8WTT0; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q8WTT0; -.
DR BioGRID-ORCS; 170482; 6 hits in 1055 CRISPR screens.
DR ChiTaRS; CLEC4C; human.
DR GenomeRNAi; 170482; -.
DR Pharos; Q8WTT0; Tbio.
DR PRO; PR:Q8WTT0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WTT0; protein.
DR Bgee; ENSG00000198178; Expressed in secondary oocyte and 50 other tissues.
DR ExpressionAtlas; Q8WTT0; baseline and differential.
DR Genevisible; Q8WTT0; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0061760; P:antifungal innate immune response; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Calcium;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity; Innate immunity;
KW Lectin; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="C-type lectin domain family 4 member C"
FT /id="PRO_0000046615"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 90..207
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 139
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT BINDING 178
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT BINDING 184..186
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT BINDING 194..195
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT BINDING 194
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT BINDING 202
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZET"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..82
FT /evidence="ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:4ZES, ECO:0007744|PDB:4ZET"
FT DISULFID 83..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:24425442, ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:3WBP, ECO:0007744|PDB:3WBQ,
FT ECO:0007744|PDB:3WBR, ECO:0007744|PDB:4ZES,
FT ECO:0007744|PDB:4ZET"
FT DISULFID 111..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:24425442, ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:3WBP, ECO:0007744|PDB:3WBQ,
FT ECO:0007744|PDB:3WBR, ECO:0007744|PDB:4ZES,
FT ECO:0007744|PDB:4ZET"
FT DISULFID 180..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:24425442, ECO:0000269|PubMed:25995448,
FT ECO:0007744|PDB:3WBP, ECO:0007744|PDB:3WBQ,
FT ECO:0007744|PDB:3WBR, ECO:0007744|PDB:4ZES,
FT ECO:0007744|PDB:4ZET"
FT VAR_SEQ 11..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11536172"
FT /id="VSP_012845"
FT MUTAGEN 139
FT /note="S->A: Significantly impairs carbohydrate binding for
FT the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man."
FT /evidence="ECO:0000269|PubMed:25995448"
FT MUTAGEN 184
FT /note="N->A: Abolishes carbohydrate binding for the
FT trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man."
FT /evidence="ECO:0000269|PubMed:25995448"
FT MUTAGEN 186
FT /note="R->A: Significantly impairs carbohydrate binding for
FT the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man."
FT /evidence="ECO:0000269|PubMed:25995448"
FT MUTAGEN 200
FT /note="V->A: Significantly impairs carbohydrate binding for
FT the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man."
FT /evidence="ECO:0000269|PubMed:25995448"
FT MUTAGEN 202
FT /note="Q->A: Significantly impairs carbohydrate binding for
FT the trisaccharide Gal(beta1-3/4)GlcNAc(beta1-2)Man."
FT /evidence="ECO:0000269|PubMed:25995448"
FT CONFLICT 66
FT /note="P -> S (in Ref. 3; AAQ88590)"
FT /evidence="ECO:0000305"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:4ZES"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4ZES"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:4ZES"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3WBQ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:4ZES"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:4ZES"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4ZES"
SQ SEQUENCE 213 AA; 25038 MW; 5DC82C95BE2378C1 CRC64;
MVPEEEPQDR EKGLWWFQLK VWSMAVVSIL LLSVCFTVSS VVPHNFMYSK TVKRLSKLRE
YQQYHPSLTC VMEGKDIEDW SCCPTPWTSF QSSCYFISTG MQSWTKSQKN CSVMGADLVV
INTREEQDFI IQNLKRNSSY FLGLSDPGGR RHWQWVDQTP YNENVTFWHS GEPNNLDERC
AIINFRSSEE WGWNDIHCHV PQKSICKMKK IYI
