CLC2D_HUMAN
ID CLC2D_HUMAN Reviewed; 191 AA.
AC Q9UHP7; D6CI39; D6CI40; D6CI41; Q6YID5; Q8WUP7; Q9HD37; Q9HD38;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=C-type lectin domain family 2 member D;
DE AltName: Full=Lectin-like NK cell receptor;
DE AltName: Full=Lectin-like transcript 1;
DE Short=LLT-1;
DE AltName: Full=Osteoclast inhibitory lectin;
GN Name=CLEC2D; Synonyms=CLAX, LLT1, OCIL;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Natural killer cell;
RX PubMed=10541800; DOI=10.1007/s002510050679;
RA Boles K.S., Barten R., Kumaresan P.R., Trowsdale J., Mathew P.A.;
RT "Cloning of a new lectin-like receptor expressed on human NK cells.";
RL Immunogenetics 50:1-7(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION.
RC TISSUE=Fetal liver, and Fetus;
RX PubMed=14753741; DOI=10.1359/jbmr.0301215;
RA Hu Y.S., Zhou H., Myers D., Quinn J.M.W., Atkins G.J., Ly C., Gange C.,
RA Kartsogiannis V., Elliott J., Kostakis P., Zannettino A.C.W., Cromer B.,
RA McKinstry W.J., Findlay D.M., Gillespie M.T., Ng K.W.;
RT "Isolation of a human homolog of osteoclast inhibitory lectin that inhibits
RT the formation and function of osteoclasts.";
RL J. Bone Miner. Res. 19:89-99(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND VARIANTS LYS-19 AND VAL-23.
RC TISSUE=Lymphocyte;
RX PubMed=20843815; DOI=10.1074/jbc.m110.179622;
RA Germain C., Bihl F., Zahn S., Poupon G., Dumaurier M.J., Rampanarivo H.H.,
RA Padkjaer S.B., Spee P., Braud V.M.;
RT "Characterization of alternatively spliced transcript variants of CLEC2D
RT gene.";
RL J. Biol. Chem. 285:36207-36215(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 22-191 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA] OF 27-191 (ISOFORM 4).
RA Yang G., Chen X., Davis P.M., Bowen M.A., Aruffo A.A., Kiener P.A.;
RT "Molecular cloning of a novel CD69 homologue and its variants.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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] (ISOFORM 3), AND VARIANT VAL-23.
RC TISSUE=Testis;
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 FUNCTION.
RX PubMed=15123656; DOI=10.1074/jbc.m312518200;
RA Gange C.T., Quinn J.M.W., Zhou H., Kartsogiannis V., Gillespie M.T.,
RA Ng K.W.;
RT "Characterization of sugar binding by osteoclast inhibitory lectin.";
RL J. Biol. Chem. 279:29043-29049(2004).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=15104121; DOI=10.1016/j.molimm.2003.11.024;
RA Mathew P.A., Chuang S.S., Vaidya S.V., Kumaresan P.R., Boles K.S.,
RA Pham H.T.;
RT "The LLT1 receptor induces IFN-gamma production by human natural killer
RT cells.";
RL Mol. Immunol. 40:1157-1163(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16339513; DOI=10.4049/jimmunol.175.12.7796;
RA Rosen D.B., Bettadapura J., Alsharifi M., Mathew P.A., Warren H.S.,
RA Lanier L.L.;
RT "Lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A
RT receptor.";
RL J. Immunol. 175:7796-7799(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 72-191, SUBUNIT, GLYCOSYLATION AT
RP ASN-95 AND ASN-147, AND DISULFIDE BONDS.
RX PubMed=25760607; DOI=10.1107/s1399004714027928;
RA Skalova T., Blaha J., Harlos K., Duskova J., Koval' T., Stransky J.,
RA Hasek J., Vanek O., Dohnalek J.;
RT "Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied
RT glycosylation and oligomerization states.";
RL Acta Crystallogr. D 71:578-591(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 71-191, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=25826155; DOI=10.1002/eji.201545509;
RA Kita S., Matsubara H., Kasai Y., Tamaoki T., Okabe Y., Fukuhara H.,
RA Kamishikiryo J., Krayukhina E., Uchiyama S., Ose T., Kuroki K., Maenaka K.;
RT "Crystal structure of extracellular domain of human lectin-like transcript
RT 1 (LLT1), the ligand for natural killer receptor-P1A.";
RL Eur. J. Immunol. 45:1605-1613(2015).
CC -!- FUNCTION: Receptor for KLRB1 that protects target cells against natural
CC killer cell-mediated lysis (PubMed:20843815, PubMed:16339513). Inhibits
CC osteoclast formation (PubMed:14753741, PubMed:15123656). Inhibits bone
CC resorption (PubMed:14753741). Modulates the release of interferon-gamma
CC (PubMed:15104121). Binds high molecular weight sulfated
CC glycosaminoglycans (PubMed:15123656). {ECO:0000269|PubMed:14753741,
CC ECO:0000269|PubMed:15104121, ECO:0000269|PubMed:15123656,
CC ECO:0000269|PubMed:16339513, ECO:0000269|PubMed:20843815}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15104121,
CC ECO:0000269|PubMed:20843815, ECO:0000269|PubMed:25760607,
CC ECO:0000269|PubMed:25826155}.
CC -!- INTERACTION:
CC Q9UHP7-1; Q12918: KLRB1; NbExp=2; IntAct=EBI-13640978, EBI-2805465;
CC Q9UHP7-3; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-11749983, EBI-10827839;
CC Q9UHP7-3; P27449: ATP6V0C; NbExp=3; IntAct=EBI-11749983, EBI-721179;
CC Q9UHP7-3; Q9Y2C3: B3GALT5; NbExp=3; IntAct=EBI-11749983, EBI-14141066;
CC Q9UHP7-3; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-11749983, EBI-12244618;
CC Q9UHP7-3; P34810: CD68; NbExp=3; IntAct=EBI-11749983, EBI-2826276;
CC Q9UHP7-3; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-11749983, EBI-12256978;
CC Q9UHP7-3; P57739: CLDN2; NbExp=3; IntAct=EBI-11749983, EBI-751440;
CC Q9UHP7-3; Q6UVW9: CLEC2A; NbExp=3; IntAct=EBI-11749983, EBI-15839595;
CC Q9UHP7-3; A0PK11: CLRN2; NbExp=3; IntAct=EBI-11749983, EBI-12813623;
CC Q9UHP7-3; Q07325: CXCL9; NbExp=3; IntAct=EBI-11749983, EBI-3911467;
CC Q9UHP7-3; Q5J5C9: DEFB121; NbExp=3; IntAct=EBI-11749983, EBI-10244198;
CC Q9UHP7-3; Q5MY95-2: ENTPD8; NbExp=3; IntAct=EBI-11749983, EBI-12909060;
CC Q9UHP7-3; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-11749983, EBI-10976398;
CC Q9UHP7-3; Q92520: FAM3C; NbExp=3; IntAct=EBI-11749983, EBI-2876774;
CC Q9UHP7-3; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-11749983, EBI-12142257;
CC Q9UHP7-3; O15529: GPR42; NbExp=3; IntAct=EBI-11749983, EBI-18076404;
CC Q9UHP7-3; Q01638-2: IL1RL1; NbExp=3; IntAct=EBI-11749983, EBI-12838366;
CC Q9UHP7-3; P26715: KLRC1; NbExp=4; IntAct=EBI-11749983, EBI-9018187;
CC Q9UHP7-3; O95214: LEPROTL1; NbExp=3; IntAct=EBI-11749983, EBI-750776;
CC Q9UHP7-3; Q16617: NKG7; NbExp=3; IntAct=EBI-11749983, EBI-3919611;
CC Q9UHP7-3; Q9Y342: PLLP; NbExp=3; IntAct=EBI-11749983, EBI-3919291;
CC Q9UHP7-3; P26678: PLN; NbExp=3; IntAct=EBI-11749983, EBI-692836;
CC Q9UHP7-3; P60201-2: PLP1; NbExp=3; IntAct=EBI-11749983, EBI-12188331;
CC Q9UHP7-3; Q9NS64: RPRM; NbExp=3; IntAct=EBI-11749983, EBI-1052363;
CC Q9UHP7-3; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11749983, EBI-8652744;
CC Q9UHP7-3; Q9BQS2-2: SYT15; NbExp=3; IntAct=EBI-11749983, EBI-13373352;
CC Q9UHP7-3; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-11749983, EBI-13351685;
CC Q9UHP7-3; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-11749983, EBI-10278423;
CC Q9UHP7-3; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-11749983, EBI-11742770;
CC Q9UHP7-3; O14817: TSPAN4; NbExp=3; IntAct=EBI-11749983, EBI-8652667;
CC Q9UHP7-3; O76024: WFS1; NbExp=3; IntAct=EBI-11749983, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15104121,
CC ECO:0000269|PubMed:20843815, ECO:0000305|PubMed:16339513}; Single-pass
CC type II membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20843815}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20843815}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UHP7-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9UHP7-2; Sequence=VSP_039682;
CC Name=2;
CC IsoId=Q9UHP7-3; Sequence=VSP_039683;
CC Name=4;
CC IsoId=Q9UHP7-5; Sequence=VSP_039678;
CC Name=5;
CC IsoId=Q9UHP7-6; Sequence=VSP_039676;
CC Name=6;
CC IsoId=Q9UHP7-7; Sequence=VSP_039676, VSP_039680, VSP_039681;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood leukocytes,
CC osteoblasts, lymph node, thymus and spleen. Isoform 1, isoform 2 and
CC isoform 4 are expressed in T- and B-lymphocytes, and at lower levels in
CC NK cells. They are also expressed in B-cell lines and LPS-matured
CC monocyte-derived dendritic cells. {ECO:0000269|PubMed:10541800,
CC ECO:0000269|PubMed:20843815}.
CC -!- INDUCTION: Up-regulated by IL1A/interleukin-1 alpha and prostaglandin
CC E2 in cultured osteogenic sarcoma cells. {ECO:0000269|PubMed:14753741}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15104121,
CC ECO:0000269|PubMed:20843815, ECO:0000269|PubMed:25760607}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=LLT1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_242";
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DR EMBL; AF133299; AAF22159.1; -; mRNA.
DR EMBL; AY144606; AAN59996.1; -; Genomic_DNA.
DR EMBL; FN813349; CBL81070.1; -; mRNA.
DR EMBL; FN813350; CBL81071.1; -; mRNA.
DR EMBL; FN813351; CBL81072.1; -; mRNA.
DR EMBL; AF285087; AAG00514.1; -; mRNA.
DR EMBL; AF285088; AAG00515.1; -; mRNA.
DR EMBL; AF285089; AAG00516.1; -; mRNA.
DR EMBL; AC007068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96114.1; -; Genomic_DNA.
DR EMBL; BC019883; AAH19883.1; -; mRNA.
DR CCDS; CCDS31741.1; -. [Q9UHP7-3]
DR CCDS; CCDS55800.1; -. [Q9UHP7-5]
DR CCDS; CCDS55801.1; -. [Q9UHP7-6]
DR CCDS; CCDS55802.1; -. [Q9UHP7-7]
DR CCDS; CCDS8602.1; -. [Q9UHP7-1]
DR RefSeq; NP_001004419.1; NM_001004419.4. [Q9UHP7-3]
DR RefSeq; NP_001184246.1; NM_001197317.2. [Q9UHP7-6]
DR RefSeq; NP_001184247.1; NM_001197318.2. [Q9UHP7-5]
DR RefSeq; NP_001184248.1; NM_001197319.2. [Q9UHP7-7]
DR RefSeq; NP_037401.1; NM_013269.5. [Q9UHP7-1]
DR PDB; 4QKG; X-ray; 1.95 A; A=72-191.
DR PDB; 4QKH; X-ray; 1.80 A; A/B=72-191.
DR PDB; 4QKI; X-ray; 1.80 A; A/B=72-191.
DR PDB; 4QKJ; X-ray; 2.75 A; A=72-191.
DR PDB; 4WCO; X-ray; 2.46 A; A/B/C=71-191.
DR PDB; 5MGT; X-ray; 1.90 A; A/B=72-191.
DR PDBsum; 4QKG; -.
DR PDBsum; 4QKH; -.
DR PDBsum; 4QKI; -.
DR PDBsum; 4QKJ; -.
DR PDBsum; 4WCO; -.
DR PDBsum; 5MGT; -.
DR AlphaFoldDB; Q9UHP7; -.
DR SMR; Q9UHP7; -.
DR BioGRID; 118886; 223.
DR IntAct; Q9UHP7; 106.
DR STRING; 9606.ENSP00000261340; -.
DR GlyGen; Q9UHP7; 2 sites.
DR iPTMnet; Q9UHP7; -.
DR PhosphoSitePlus; Q9UHP7; -.
DR BioMuta; CLEC2D; -.
DR DMDM; 74753331; -.
DR MassIVE; Q9UHP7; -.
DR PeptideAtlas; Q9UHP7; -.
DR PRIDE; Q9UHP7; -.
DR ProteomicsDB; 84389; -. [Q9UHP7-1]
DR ProteomicsDB; 84390; -. [Q9UHP7-2]
DR ProteomicsDB; 84391; -. [Q9UHP7-3]
DR ProteomicsDB; 84393; -. [Q9UHP7-6]
DR Antibodypedia; 2229; 279 antibodies from 31 providers.
DR DNASU; 29121; -.
DR Ensembl; ENST00000261339.10; ENSP00000261339.6; ENSG00000069493.15. [Q9UHP7-6]
DR Ensembl; ENST00000261340.11; ENSP00000261340.7; ENSG00000069493.15. [Q9UHP7-3]
DR Ensembl; ENST00000290855.11; ENSP00000290855.6; ENSG00000069493.15. [Q9UHP7-1]
DR Ensembl; ENST00000479877.5; ENSP00000441653.1; ENSG00000069493.15. [Q9UHP7-2]
DR Ensembl; ENST00000543300.5; ENSP00000443065.1; ENSG00000069493.15. [Q9UHP7-5]
DR Ensembl; ENST00000545918.5; ENSP00000444818.1; ENSG00000069493.15. [Q9UHP7-7]
DR GeneID; 29121; -.
DR KEGG; hsa:29121; -.
DR MANE-Select; ENST00000290855.11; ENSP00000290855.6; NM_013269.6; NP_037401.1.
DR UCSC; uc001qwf.4; human. [Q9UHP7-1]
DR CTD; 29121; -.
DR DisGeNET; 29121; -.
DR GeneCards; CLEC2D; -.
DR HGNC; HGNC:14351; CLEC2D.
DR HPA; ENSG00000069493; Tissue enhanced (lymphoid).
DR MIM; 605659; gene.
DR neXtProt; NX_Q9UHP7; -.
DR OpenTargets; ENSG00000069493; -.
DR PharmGKB; PA142672100; -.
DR VEuPathDB; HostDB:ENSG00000069493; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155319; -.
DR HOGENOM; CLU_049894_8_4_1; -.
DR InParanoid; Q9UHP7; -.
DR OMA; PAINANC; -.
DR OrthoDB; 1289964at2759; -.
DR PhylomeDB; Q9UHP7; -.
DR TreeFam; TF351467; -.
DR PathwayCommons; Q9UHP7; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q9UHP7; -.
DR BioGRID-ORCS; 29121; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; CLEC2D; human.
DR GeneWiki; CLEC2D; -.
DR GenomeRNAi; 29121; -.
DR Pharos; Q9UHP7; Tbio.
DR PRO; PR:Q9UHP7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UHP7; protein.
DR Bgee; ENSG00000069493; Expressed in granulocyte and 115 other tissues.
DR ExpressionAtlas; Q9UHP7; baseline and differential.
DR Genevisible; Q9UHP7; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR CDD; cd03593; CLECT_NK_receptors_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; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..191
FT /note="C-type lectin domain family 2 member D"
FT /id="PRO_0000315285"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 82..185
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25760607,
FT ECO:0007744|PDB:4QKG, ECO:0007744|PDB:4QKH,
FT ECO:0007744|PDB:4QKJ"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25826155,
FT ECO:0007744|PDB:4QKH"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0007744|PDB:4QKG, ECO:0007744|PDB:4QKH,
FT ECO:0007744|PDB:4QKI, ECO:0007744|PDB:4QKJ,
FT ECO:0007744|PDB:4WCO"
FT DISULFID 103..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0007744|PDB:4QKG, ECO:0007744|PDB:4QKH,
FT ECO:0007744|PDB:4QKI, ECO:0007744|PDB:4QKJ,
FT ECO:0007744|PDB:4WCO"
FT VAR_SEQ 21..57
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:20843815"
FT /id="VSP_039676"
FT VAR_SEQ 120..191
FT /note="NFLLRYKGPSDHWIGLSREQGQPWKWINGTEWTRQFPILGAGECAYLNDKGA
FT SSARHYTERKWICSKSDIHV -> VSYPGSRRVCLFE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20843815, ECO:0000303|Ref.4"
FT /id="VSP_039678"
FT VAR_SEQ 120..132
FT /note="NFLLRYKGPSDHW -> VSYPGSRRVCLFE (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:20843815"
FT /id="VSP_039680"
FT VAR_SEQ 133..191
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:20843815"
FT /id="VSP_039681"
FT VAR_SEQ 155..191
FT /note="FPILGAGECAYLNDKGASSARHYTERKWICSKSDIHV -> LVMKEDGANLY
FT VAKVSQVPRMNPRPVMVSYPGSRRVCLFE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_039683"
FT VAR_SEQ 155..191
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039682"
FT VARIANT 19
FT /note="N -> K (in dbSNP:rs16914640)"
FT /evidence="ECO:0000269|PubMed:20843815"
FT /id="VAR_038172"
FT VARIANT 23
FT /note="L -> V (in dbSNP:rs3764022)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:20843815"
FT /id="VAR_038173"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4QKH"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4QKH"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:4QKH"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:4QKH"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4QKH"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:4QKI"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:4WCO"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4QKH"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:4QKH"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:4QKH"
SQ SEQUENCE 191 AA; 21849 MW; E71F3E21DC361F10 CRC64;
MHDSNNVEKD ITPSELPANP GCLHSKEHSI KATLIWRLFF LIMFLTIIVC GMVAALSAIR
ANCHQEPSVC LQAACPESWI GFQRKCFYFS DDTKNWTSSQ RFCDSQDADL AQVESFQELN
FLLRYKGPSD HWIGLSREQG QPWKWINGTE WTRQFPILGA GECAYLNDKG ASSARHYTER
KWICSKSDIH V
