ID CLC6A_HUMAN Reviewed; 209 AA.
AC Q6EIG7; A2RUK3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=C-type lectin domain family 6 member A {ECO:0000305};
DE AltName: Full=C-type lectin superfamily member 10;
DE AltName: Full=Dendritic cell-associated C-type lectin 2;
DE Short=DC-associated C-type lectin 2;
DE Short=Dectin-2 {ECO:0000303|PubMed:15175046, ECO:0000303|PubMed:15810886, ECO:0000303|PubMed:28652405};
GN Name=CLEC6A {ECO:0000312|HGNC:HGNC:14556};
GN Synonyms=CLECSF10, DECTIN2 {ECO:0000303|PubMed:15175046,
GN ECO:0000303|PubMed:15810886, ECO:0000303|PubMed:28652405};
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], AND TISSUE SPECIFICITY.
RX PubMed=15368084; DOI=10.1007/s00251-004-0714-x;
RA Flornes L.M., Bryceson Y.T., Spurkland A., Lorentzen J.C., Dissen E.,
RA Fossum S.;
RT "Identification of lectin-like receptors expressed by antigen presenting
RT cells and neutrophils and their mapping to a novel gene complex.";
RL Immunogenetics 56:506-517(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=15175046; DOI=10.1111/j.0022-202x.2004.22602.x;
RA Kanazawa N., Tashiro K., Inaba K., Lutz M.B., Miyachi Y.;
RT "Molecular cloning of human dectin-2.";
RL J. Invest. Dermatol. 122:1522-1524(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP TISSUE SPECIFICITY, INDUCTION, AND ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=15810886; DOI=10.1111/j.0906-6705.2005.00312.x;
RA Gavino A.C., Chung J.S., Sato K., Ariizumi K., Cruz P.D. Jr.;
RT "Identification and expression profiling of a human C-type lectin,
RT structurally homologous to mouse dectin-2.";
RL Exp. Dermatol. 14:281-288(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLEC6A.
RX PubMed=23911656; DOI=10.1016/j.immuni.2013.05.017;
RA Zhu L.L., Zhao X.Q., Jiang C., You Y., Chen X.P., Jiang Y.Y., Jia X.M.,
RA Lin X.;
RT "C-type lectin receptors Dectin-3 and Dectin-2 form a heterodimeric
RT pattern-recognition receptor for host defense against fungal infection.";
RL Immunity 39:324-334(2013).
RN [7] {ECO:0007744|PDB:5VYB}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 64-209 IN COMPLEX WITH
RP HIGH-MANNOSE CARBOHYDRATE AND CALCIUM, DISULFIDE BOND, AND FUNCTION.
RX PubMed=28652405; DOI=10.1074/jbc.m117.799080;
RA Feinberg H., Jegouzo S.A.F., Rex M.J., Drickamer K., Weis W.I.,
RA Taylor M.E.;
RT "Mechanism of pathogen recognition by human dectin-2.";
RL J. Biol. Chem. 292:13402-13414(2017).
CC -!- FUNCTION: Calcium-dependent lectin that acts as a pattern recognition
CC receptor (PRR) of the innate immune system: specifically recognizes and
CC binds alpha-mannans on C.albicans hypheas (PubMed:23911656,
CC PubMed:28652405). Binding of C.albicans alpha-mannans to this receptor
CC complex leads to phosphorylation of the immunoreceptor tyrosine-based
CC activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9
CC and NF-kappa-B, consequently driving maturation of antigen-presenting
CC cells and shaping antigen-specific priming of T-cells toward effector
CC T-helper 1 and T-helper 17 cell subtypes (By similarity). Recognizes
CC also, in a mannose-dependent manner, allergens from house dust mite and
CC fungi, by promoting cysteinyl leukotriene production (By similarity).
CC Recognizes soluble elements from the eggs of Shistosoma mansoni
CC altering adaptive immune responses (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKF4, ECO:0000269|PubMed:23911656,
CC ECO:0000269|PubMed:28652405}.
CC -!- SUBUNIT: Associated with FCER1G (By similarity). Heterodimer with
CC CLEC4D; this heterodimer forms a pattern recognition receptor (PRR)
CC against fungal infection (PubMed:23911656).
CC {ECO:0000250|UniProtKB:Q9JKF4, ECO:0000269|PubMed:23911656}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23911656};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6EIG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6EIG7-2; Sequence=VSP_041514;
CC -!- TISSUE SPECIFICITY: Expressed in lung, spleen, lymph node, leukocytes,
CC bone marrow, tonsils and dendritic cells. Strongly expressed in
CC purified monocytes and weakly in B-cells. In peripheral blood cells,
CC preferentially expressed in plasmacytoids rather than myeloids.
CC {ECO:0000269|PubMed:15175046, ECO:0000269|PubMed:15368084,
CC ECO:0000269|PubMed:15810886}.
CC -!- INDUCTION: Up-regulated by granulocyte-macrophage colony-stimulating
CC factor (GM-CSF), TGF-beta 1, TNF-alpha and down-regulated by IL-4, IL-
CC 10 or UVB in CD14+ monocytes. {ECO:0000269|PubMed:15810886}.
CC -!- DOMAIN: A short stretch of the intracellular domain (AA 8-14) proximal
CC to the transmembrane domain is required for association with Fc
CC receptor gamma chain. {ECO:0000250|UniProtKB:Q9JKF4}.
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DR EMBL; AY365135; AAR13071.1; -; mRNA.
DR EMBL; AY321309; AAQ83725.1; -; mRNA.
DR EMBL; AC092746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132933; AAI32934.1; -; mRNA.
DR EMBL; BC132935; AAI32936.1; -; mRNA.
DR CCDS; CCDS31739.1; -. [Q6EIG7-1]
DR RefSeq; NP_001007034.1; NM_001007033.1. [Q6EIG7-1]
DR RefSeq; NP_001304928.1; NM_001317999.1. [Q6EIG7-2]
DR PDB; 5VYB; X-ray; 2.40 A; A=64-209.
DR PDBsum; 5VYB; -.
DR AlphaFoldDB; Q6EIG7; -.
DR SMR; Q6EIG7; -.
DR STRING; 9606.ENSP00000371505; -.
DR ChEMBL; CHEMBL2176856; -.
DR UniLectin; Q6EIG7; -.
DR GlyCosmos; Q6EIG7; 2 sites, No reported glycans.
DR GlyGen; Q6EIG7; 2 sites.
DR iPTMnet; Q6EIG7; -.
DR PhosphoSitePlus; Q6EIG7; -.
DR BioMuta; CLEC6A; -.
DR DMDM; 59797926; -.
DR MassIVE; Q6EIG7; -.
DR PaxDb; 9606-ENSP00000371505; -.
DR PeptideAtlas; Q6EIG7; -.
DR Antibodypedia; 23055; 497 antibodies from 30 providers.
DR DNASU; 93978; -.
DR Ensembl; ENST00000382073.4; ENSP00000371505.3; ENSG00000205846.4. [Q6EIG7-1]
DR GeneID; 93978; -.
DR KEGG; hsa:93978; -.
DR MANE-Select; ENST00000382073.4; ENSP00000371505.3; NM_001007033.2; NP_001007034.1.
DR UCSC; uc001qum.2; human. [Q6EIG7-1]
DR AGR; HGNC:14556; -.
DR CTD; 93978; -.
DR DisGeNET; 93978; -.
DR GeneCards; CLEC6A; -.
DR HGNC; HGNC:14556; CLEC6A.
DR HPA; ENSG00000205846; Tissue enhanced (lung, lymphoid tissue).
DR MIM; 613579; gene.
DR neXtProt; NX_Q6EIG7; -.
DR OpenTargets; ENSG00000205846; -.
DR PharmGKB; PA26579; -.
DR VEuPathDB; HostDB:ENSG00000205846; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162938; -.
DR HOGENOM; CLU_049894_7_5_1; -.
DR InParanoid; Q6EIG7; -.
DR OMA; EKNVRFW; -.
DR OrthoDB; 2881452at2759; -.
DR PhylomeDB; Q6EIG7; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q6EIG7; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR SignaLink; Q6EIG7; -.
DR BioGRID-ORCS; 93978; 7 hits in 1109 CRISPR screens.
DR ChiTaRS; CLEC6A; human.
DR GenomeRNAi; 93978; -.
DR Pharos; Q6EIG7; Tbio.
DR PRO; PR:Q6EIG7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6EIG7; Protein.
DR Bgee; ENSG00000205846; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 24 other cell types or tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0043274; F:phospholipase binding; ISS:ARUK-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0061760; P:antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR GO; GO:0001879; P:detection of yeast; ISS:ARUK-UCL.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISS:ARUK-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:ARUK-UCL.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0001878; P:response to yeast; ISS:ARUK-UCL.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; ISS:ARUK-UCL.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 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..209
FT /note="C-type lectin domain family 6 member A"
FT /id="PRO_0000046635"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 86..203
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 168..170
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 174
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 182
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 190..191
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 198
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..78
FT /evidence="ECO:0000269|PubMed:28652405,
FT ECO:0007744|PDB:5VYB"
FT DISULFID 79..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB"
FT DISULFID 107..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB"
FT DISULFID 176..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:28652405, ECO:0007744|PDB:5VYB"
FT VAR_SEQ 11..40
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041514"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:5VYB"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:5VYB"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5VYB"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5VYB"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5VYB"
SQ SEQUENCE 209 AA; 23998 MW; 0AF1FE813B7585CF CRC64;
MMQEQQPQST EKRGWLSLRL WSVAGISIAL LSACFIVSCV VTYHFTYGET GKRLSELHSY
HSSLTCFSEG TKVPAWGCCP ASWKSFGSSC YFISSEEKVW SKSEQNCVEM GAHLVVFNTE
AEQNFIVQQL NESFSYFLGL SDPQGNNNWQ WIDKTPYEKN VRFWHLGEPN HSAEQCASIV
FWKPTGWGWN DVICETRRNS ICEMNKIYL
//
