CLC4A_HUMAN
ID CLC4A_HUMAN Reviewed; 237 AA.
AC Q9UMR7; Q17R69; Q8WXW9; Q9H2Z9; Q9NS33; Q9UI34;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=C-type lectin domain family 4 member A {ECO:0000305};
DE AltName: Full=C-type lectin DDB27;
DE AltName: Full=C-type lectin superfamily member 6;
DE AltName: Full=Dendritic cell immunoreceptor;
DE AltName: Full=Lectin-like immunoreceptor;
DE AltName: CD_antigen=CD367;
GN Name=CLEC4A {ECO:0000312|HGNC:HGNC:13257};
GN Synonyms=CLECSF6 {ECO:0000303|PubMed:27015765},
GN DCIR {ECO:0000303|PubMed:27015765}, LLIR; ORFNames=HDCGC13P;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10438934;
RA Bates E.E.M., Fournier N., Garcia E., Valladeau J., Durand I., Pin J.-J.,
RA Zurawski S.M., Patel S., Abrams J.S., Lebecque S., Garrone P., Saeland S.;
RT "APCs express DCIR, a novel C-type lectin surface receptor containing an
RT immunoreceptor tyrosine-based inhibitory motif.";
RL J. Immunol. 163:1973-1983(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), INTERACTION WITH PTPN6,
RP TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND VARIANT LEU-36.
RX PubMed=11178971; DOI=10.1006/bbrc.2001.4322;
RA Huang X., Yuan Z., Chen G., Zhang M., Zhang W., Yu Y., Cao X.;
RT "Cloning and characterization of a novel ITIM containing lectin-like
RT immunoreceptor LLIR and its two transmembrane region deletion variants.";
RL Biochem. Biophys. Res. Commun. 281:131-140(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP INDUCTION, AND VARIANT LEU-36.
RX PubMed=11994513;
RA Richard M., Veilleux P., Rouleau M., Paquin R., Beaulieu A.D.;
RT "The expression pattern of the ITIM-bearing lectin CLECSF6 in neutrophils
RT suggests a key role in the control of inflammation.";
RL J. Leukoc. Biol. 71:871-880(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-36.
RC TISSUE=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 [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY TRL9, AND SUBCELLULAR LOCATION.
RX PubMed=18258799; DOI=10.1182/blood-2007-03-081398;
RA Meyer-Wentrup F., Benitez-Ribas D., Tacken P.J., Punt C.J., Figdor C.G.,
RA de Vries I.J., Adema G.J.;
RT "Targeting DCIR on human plasmacytoid dendritic cells results in antigen
RT presentation and inhibits IFN-alpha production.";
RL Blood 111:4245-4253(2008).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20530286; DOI=10.1182/blood-2010-01-264960;
RA Klechevsky E., Flamar A.L., Cao Y., Blanck J.P., Liu M., O'Bar A.,
RA Agouna-Deciat O., Klucar P., Thompson-Snipes L., Zurawski S., Reiter Y.,
RA Palucka A.K., Zurawski G., Banchereau J.;
RT "Cross-priming CD8+ T cells by targeting antigens to human dendritic cells
RT through DCIR.";
RL Blood 116:1685-1697(2010).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND MUTAGENESIS OF THR-6 AND TYR-7.
RX PubMed=21536857; DOI=10.1182/blood-2011-01-331363;
RA Lambert A.A., Barabe F., Gilbert C., Tremblay M.J.;
RT "DCIR-mediated enhancement of HIV-1 infection requires the ITIM-associated
RT signal transduction pathway.";
RL Blood 117:6589-6599(2011).
RN [9] {ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 106-237 IN COMPLEX WITH CALCIUM;
RP MANNOSE AND N-ACETYL-D-GLUCOSAMINE, AND DISULFIDE BOND.
RX PubMed=27015765; DOI=10.1002/1873-3468.12162;
RA Nagae M., Ikeda A., Hanashima S., Kojima T., Matsumoto N., Yamamoto K.,
RA Yamaguchi Y.;
RT "Crystal structure of human dendritic cell inhibitory receptor C-type
RT lectin domain reveals the binding mode with N-glycan.";
RL FEBS Lett. 590:1280-1288(2016).
CC -!- FUNCTION: C-type lectin receptor that binds carbohydrates mannose and
CC fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a
CC Ca(2+)-dependent manner (PubMed:27015765). Involved in regulating
CC immune reactivity (PubMed:18258799, PubMed:10438934). Once triggered by
CC antigen, it is internalized by clathrin-dependent endocytosis and
CC delivers its antigenic cargo into the antigen presentation pathway
CC resulting in cross-priming of CD8(+) T cells. This cross-presentation
CC and cross-priming are enhanced by TLR7 and TLR8 agonists with increased
CC expansion of the CD8(+) T cells, high production of IFNG and TNF with
CC reduced levels of IL4, IL5 and IL13 (PubMed:18258799, PubMed:20530286).
CC In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF
CC production (PubMed:18258799). May be involved via its ITIM motif
CC (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of
CC B-cell-receptor-mediated calcium mobilization and protein tyrosine
CC phosphorylation (PubMed:10438934). {ECO:0000269|PubMed:10438934,
CC ECO:0000269|PubMed:18258799, ECO:0000269|PubMed:20530286,
CC ECO:0000269|PubMed:27015765}.
CC -!- FUNCTION: (Microbial infection) Involved in the interaction between
CC HIV-1 virus and dendritic cells. Enhances HIV-1 binding/entry and virus
CC infection. Requires ITIM motif-associated signal transduction pathway
CC involving phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP
CC kinases. {ECO:0000269|PubMed:21536857}.
CC -!- SUBUNIT: May interact with PTPN6 via its ITIM motif.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18258799};
CC Single-pass type II membrane protein {ECO:0000305}; Extracellular side
CC {ECO:0000269|PubMed:18258799}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UMR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMR7-2; Sequence=VSP_012844;
CC Name=3; Synonyms=llirV1;
CC IsoId=Q9UMR7-3; Sequence=VSP_041348;
CC Name=4; Synonyms=llirV2;
CC IsoId=Q9UMR7-4; Sequence=VSP_012842;
CC -!- TISSUE SPECIFICITY: Expressed preferentially in hematopoietic tissues.
CC Expressed in all circulating Ag-presenting cells such as dendritic
CC cells, myeloid cells, monocytes, macrophages, B-cells and epidermal
CC Langerhans cells (at protein level). Expressed in peripheral blood
CC leukocytes, neutrophils, moderate quantities in spleen, lymph node, and
CC bone marrow, and at very low levels in thymus.
CC {ECO:0000269|PubMed:10438934, ECO:0000269|PubMed:11178971,
CC ECO:0000269|PubMed:11994513, ECO:0000269|PubMed:18258799,
CC ECO:0000269|PubMed:20530286}.
CC -!- INDUCTION: TNF alpha, IL-1 alpha, and LPS, down-regulated expression at
CC the surface of neutrophils (at protein level) (PubMed:11994513).
CC Expression is decreased in dendritic cells by signals inducing their
CC maturation (e.g. CD40 ligand, TLR9 ligands, LPS, and TNF alpha)
CC (PubMed:10438934, PubMed:18258799). Isoform 2: mRNA expression is up-
CC regulated by agonists of neutrophils CSF2/GM-CSF, IL3/interleukin-3,
CC IL4/interleukin-4 and IL13/interleukin-13 (PubMed:11994513).
CC {ECO:0000269|PubMed:10438934, ECO:0000269|PubMed:11994513,
CC ECO:0000269|PubMed:18258799}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases
CC (PubMed:20530286). Involved in the interaction between HIV-1 virus and
CC dendritic cells. Enhances HIV-1 binding/entry and virus infection.
CC Requires ITIM motif-associated signal transduction pathway involving
CC phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP kinases
CC (PubMed:20530286). ITIM motif-associated signal transduction pathway
CC involving phosphatases PTPN6 and PTPN11, SYK, Src kinases and MAP
CC kinases is required for HIV-1 binding/entry and virus infection
CC (PubMed:20530286). {ECO:0000269|PubMed:20530286}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL56016.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=DCIR;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00137";
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DR EMBL; AJ133532; CAB54001.1; -; mRNA.
DR EMBL; AF067800; AAF75560.1; -; mRNA.
DR EMBL; AF328684; AAL56016.1; ALT_FRAME; mRNA.
DR EMBL; AF109146; AAF14348.1; -; mRNA.
DR EMBL; AF200738; AAG35593.1; -; mRNA.
DR EMBL; AC006511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074822; AAH74822.1; -; mRNA.
DR EMBL; BC074874; AAH74874.1; -; mRNA.
DR EMBL; BC117439; AAI17440.1; -; mRNA.
DR EMBL; BC117441; AAI17442.1; -; mRNA.
DR CCDS; CCDS41745.1; -. [Q9UMR7-3]
DR CCDS; CCDS8590.1; -. [Q9UMR7-1]
DR CCDS; CCDS8591.1; -. [Q9UMR7-4]
DR CCDS; CCDS8592.1; -. [Q9UMR7-2]
DR PIR; JC7608; JC7608.
DR RefSeq; NP_057268.1; NM_016184.3. [Q9UMR7-1]
DR RefSeq; NP_919429.2; NM_194447.2. [Q9UMR7-3]
DR RefSeq; NP_919430.1; NM_194448.2. [Q9UMR7-4]
DR RefSeq; NP_919432.1; NM_194450.2. [Q9UMR7-2]
DR PDB; 5B1W; X-ray; 3.05 A; A/B/C/D=106-237.
DR PDB; 5B1X; X-ray; 2.90 A; A/B/C/D=106-237.
DR PDBsum; 5B1W; -.
DR PDBsum; 5B1X; -.
DR AlphaFoldDB; Q9UMR7; -.
DR SMR; Q9UMR7; -.
DR BioGRID; 119158; 114.
DR STRING; 9606.ENSP00000229332; -.
DR UniLectin; Q9UMR7; -.
DR GlyGen; Q9UMR7; 1 site.
DR iPTMnet; Q9UMR7; -.
DR PhosphoSitePlus; Q9UMR7; -.
DR BioMuta; CLEC4A; -.
DR DMDM; 59797977; -.
DR jPOST; Q9UMR7; -.
DR MassIVE; Q9UMR7; -.
DR PaxDb; Q9UMR7; -.
DR PeptideAtlas; Q9UMR7; -.
DR PRIDE; Q9UMR7; -.
DR ProteomicsDB; 85200; -. [Q9UMR7-1]
DR ProteomicsDB; 85201; -. [Q9UMR7-2]
DR ProteomicsDB; 85202; -. [Q9UMR7-3]
DR ProteomicsDB; 85203; -. [Q9UMR7-4]
DR ABCD; Q9UMR7; 1 sequenced antibody.
DR Antibodypedia; 1471; 330 antibodies from 25 providers.
DR DNASU; 50856; -.
DR Ensembl; ENST00000229332.12; ENSP00000229332.5; ENSG00000111729.15. [Q9UMR7-1]
DR Ensembl; ENST00000345999.9; ENSP00000344646.3; ENSG00000111729.15. [Q9UMR7-4]
DR Ensembl; ENST00000352620.9; ENSP00000247243.5; ENSG00000111729.15. [Q9UMR7-2]
DR Ensembl; ENST00000360500.5; ENSP00000353690.3; ENSG00000111729.15. [Q9UMR7-3]
DR GeneID; 50856; -.
DR KEGG; hsa:50856; -.
DR MANE-Select; ENST00000229332.12; ENSP00000229332.5; NM_016184.4; NP_057268.1.
DR UCSC; uc001qtz.1; human. [Q9UMR7-1]
DR CTD; 50856; -.
DR DisGeNET; 50856; -.
DR GeneCards; CLEC4A; -.
DR HGNC; HGNC:13257; CLEC4A.
DR HPA; ENSG00000111729; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605306; gene.
DR neXtProt; NX_Q9UMR7; -.
DR OpenTargets; ENSG00000111729; -.
DR PharmGKB; PA26584; -.
DR VEuPathDB; HostDB:ENSG00000111729; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000158835; -.
DR HOGENOM; CLU_049894_10_2_1; -.
DR InParanoid; Q9UMR7; -.
DR OMA; ASATFWH; -.
DR OrthoDB; 1378771at2759; -.
DR PhylomeDB; Q9UMR7; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q9UMR7; -.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR SignaLink; Q9UMR7; -.
DR BioGRID-ORCS; 50856; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; CLEC4A; human.
DR GeneWiki; CLEC4A; -.
DR GenomeRNAi; 50856; -.
DR Pharos; Q9UMR7; Tbio.
DR PRO; PR:Q9UMR7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UMR7; protein.
DR Bgee; ENSG00000111729; Expressed in monocyte and 98 other tissues.
DR ExpressionAtlas; Q9UMR7; baseline and differential.
DR Genevisible; Q9UMR7; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
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:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:UniProtKB.
DR GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0002470; P:plasmacytoid dendritic cell antigen processing and presentation; IDA:UniProtKB.
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; Host-virus interaction;
KW Immunity; Innate immunity; Lectin; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..237
FT /note="C-type lectin domain family 4 member A"
FT /id="PRO_0000046612"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 113..231
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT /evidence="ECO:0000269|PubMed:20530286"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 195..197
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1X"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 201
FT /ligand="alpha-D-mannopyranose"
FT /ligand_id="ChEBI:CHEBI:28729"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1X"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 207..209
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1X"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27015765,
FT ECO:0007744|PDB:5B1W, ECO:0007744|PDB:5B1X"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:27015765, ECO:0007744|PDB:5B1W,
FT ECO:0007744|PDB:5B1X"
FT DISULFID 134..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:27015765, ECO:0007744|PDB:5B1W,
FT ECO:0007744|PDB:5B1X"
FT DISULFID 203..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:27015765, ECO:0007744|PDB:5B1W,
FT ECO:0007744|PDB:5B1X"
FT VAR_SEQ 28..99
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11178971"
FT /id="VSP_012842"
FT VAR_SEQ 28..67
FT /note="ASKERTAPHKSNTGFPKLLCASLLIFFLLLAISFFIAFVI -> V (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11178971"
FT /id="VSP_041348"
FT VAR_SEQ 67..100
FT /note="IFFQKYSQLLEKKTTKELVHTTLECVKKNMPVEE -> K (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11994513"
FT /id="VSP_012844"
FT VARIANT 36
FT /note="H -> L (in dbSNP:rs2024301)"
FT /evidence="ECO:0000269|PubMed:11178971,
FT ECO:0000269|PubMed:11994513, ECO:0000269|PubMed:15489334"
FT /id="VAR_021260"
FT MUTAGEN 6
FT /note="T->F: Decreases HIV-1 binding/entry in cells as well
FT as virus replication."
FT /evidence="ECO:0000269|PubMed:21536857"
FT MUTAGEN 7
FT /note="Y->F: Decreases HIV-1 binding/entry in cells as well
FT as virus replication."
FT /evidence="ECO:0000269|PubMed:21536857"
FT CONFLICT 130
FT /note="S -> C (in Ref. 4; AAF75560)"
FT /evidence="ECO:0000305"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:5B1X"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:5B1X"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5B1X"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:5B1X"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:5B1X"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:5B1X"
SQ SEQUENCE 237 AA; 27512 MW; 1D07003E4C9CF96E CRC64;
MTSEITYAEV RFKNEFKSSG INTASSAASK ERTAPHKSNT GFPKLLCASL LIFFLLLAIS
FFIAFVIFFQ KYSQLLEKKT TKELVHTTLE CVKKNMPVEE TAWSCCPKNW KSFSSNCYFI
STESASWQDS EKDCARMEAH LLVINTQEEQ DFIFQNLQEE SAYFVGLSDP EGQRHWQWVD
QTPYNESSTF WHPREPSDPN ERCVVLNFRK SPKRWGWNDV NCLGPQRSVC EMMKIHL
