CLC2D_MOUSE
ID CLC2D_MOUSE Reviewed; 207 AA.
AC Q91V08; Q1AFZ3; Q8VI19; Q8VI20;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=C-type lectin domain family 2 member D;
DE AltName: Full=C-type lectin-related protein B;
DE Short=Clr-b;
DE AltName: Full=Lectin-like transmembrane protein;
DE AltName: Full=Osteoclast inhibitory lectin;
GN Name=Clec2d; Synonyms=Clrb, Ocil;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Natural killer cell;
RX PubMed=11398965; DOI=10.1007/s002510100319;
RA Plougastel B., Dubbelde C., Yokoyama W.M.;
RT "Cloning of Clr, a new family of lectin-like genes localized between mouse
RT Nkrp1a and Cd69.";
RL Immunogenetics 53:209-214(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11278931; DOI=10.1074/jbc.m011554200;
RA Zhou H., Kartsogiannis V., Hu Y.S., Elliott J., Quinn J.M.W.,
RA McKinstry W.J., Gillespie M.T., Ng K.W.;
RT "A novel osteoblast-derived C-type lectin that inhibits osteoclast
RT formation.";
RL J. Biol. Chem. 276:14916-14923(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=12374791; DOI=10.1074/jbc.m209059200;
RA Zhou H., Kartsogiannis V., Quinn J.M.W., Ly C., Gange C., Elliott J.,
RA Ng K.W., Gillespie M.T.;
RT "Osteoclast inhibitory lectin, a family of new osteoclast inhibitors.";
RL J. Biol. Chem. 277:48808-48815(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=14990792; DOI=10.1073/pnas.0308304101;
RA Carlyle J.R., Jamieson A.M., Gasser S., Clingan C.S., Arase H.,
RA Raulet D.H.;
RT "Missing self-recognition of Ocil/Clr-b by inhibitory NKR-P1 natural killer
RT cell receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3527-3532(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-160, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cByJ;
RX PubMed=16751398; DOI=10.4049/jimmunol.176.12.7511;
RA Carlyle J.R., Mesci A., Ljutic B., Belanger S., Tai L.-H., Rousselle E.,
RA Troke A.D., Proteau M.-F., Makrigiannis A.P.;
RT "Molecular and genetic basis for strain-dependent NK1.1 alloreactivity of
RT mouse NK cells.";
RL J. Immunol. 176:7511-7524(2006).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for KLRB1B that protects target cells against
CC natural killer cell-mediated lysis (PubMed:14990792, PubMed:16751398).
CC Inhibits osteoclast formation (PubMed:11278931, PubMed:12374791). Binds
CC high molecular weight sulfated glycosaminoglycans (PubMed:15123656).
CC {ECO:0000269|PubMed:11278931, ECO:0000269|PubMed:12374791,
CC ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:15123656,
CC ECO:0000269|PubMed:16751398}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q9UHP7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14990792,
CC ECO:0000269|PubMed:16751398}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:14990792}.
CC -!- TISSUE SPECIFICITY: Detected in fetal heart, brain, lung, chondrocytes,
CC perichondrium and osteoblasts, and in adult splenocytes, thymocytes,
CC lymph-node cells, osteoblasts, growth plate chondrocytes and skeletal
CC muscle overlying the bone (at protein level). Ubiquitous. Detected in
CC thymus, bone marrow, lung, gut, heart, skeletal muscle, ovary, spleen,
CC ileum, liver and kidney. {ECO:0000269|PubMed:11278931,
CC ECO:0000269|PubMed:11398965, ECO:0000269|PubMed:12374791,
CC ECO:0000269|PubMed:14990792, ECO:0000269|PubMed:16751398}.
CC -!- INDUCTION: Constitutively expressed in bone marrow cells. Down-
CC regulated by treatment with 1,25-dihydroxyvitamin D3. Up-regulated in
CC calvarial osteoblast cells by IL-1alpha, IL11, and 1,25-
CC dihydroxyvitamin D3. {ECO:0000269|PubMed:11278931}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UHP7}.
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DR EMBL; AF350409; AAK70357.1; -; mRNA.
DR EMBL; AF320598; AAL37198.1; -; Genomic_DNA.
DR EMBL; AF320599; AAL37199.1; -; Genomic_DNA.
DR EMBL; AF321553; AAK50881.1; -; mRNA.
DR EMBL; AY137338; AAN15947.1; -; Genomic_DNA.
DR EMBL; AY320031; AAQ16529.1; -; mRNA.
DR EMBL; BC106776; AAI06777.1; -; mRNA.
DR EMBL; DQ143111; ABA43361.1; -; Genomic_DNA.
DR CCDS; CCDS20581.1; -.
DR RefSeq; NP_444339.1; NM_053109.3.
DR PDB; 6E7D; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=73-194.
DR PDBsum; 6E7D; -.
DR AlphaFoldDB; Q91V08; -.
DR SMR; Q91V08; -.
DR STRING; 10090.ENSMUSP00000032260; -.
DR GlyGen; Q91V08; 1 site.
DR iPTMnet; Q91V08; -.
DR PhosphoSitePlus; Q91V08; -.
DR SwissPalm; Q91V08; -.
DR EPD; Q91V08; -.
DR jPOST; Q91V08; -.
DR MaxQB; Q91V08; -.
DR PaxDb; Q91V08; -.
DR PRIDE; Q91V08; -.
DR ProteomicsDB; 283364; -.
DR DNASU; 93694; -.
DR Ensembl; ENSMUST00000032260; ENSMUSP00000032260; ENSMUSG00000030157.
DR GeneID; 93694; -.
DR KEGG; mmu:93694; -.
DR UCSC; uc009efe.2; mouse.
DR CTD; 29121; -.
DR MGI; MGI:2135589; Clec2d.
DR VEuPathDB; HostDB:ENSMUSG00000030157; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155319; -.
DR HOGENOM; CLU_049894_8_1_1; -.
DR InParanoid; Q91V08; -.
DR OMA; RCYSERG; -.
DR OrthoDB; 1289964at2759; -.
DR PhylomeDB; Q91V08; -.
DR TreeFam; TF351467; -.
DR BioGRID-ORCS; 93694; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Clec2d; mouse.
DR PRO; PR:Q91V08; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91V08; protein.
DR Bgee; ENSMUSG00000030157; Expressed in peripheral lymph node and 107 other tissues.
DR ExpressionAtlas; Q91V08; baseline and differential.
DR Genevisible; Q91V08; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISS:MGI.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:MGI.
DR GO; GO:0006968; P:cellular defense response; TAS:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:MGI.
DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:MGI.
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; Cell membrane; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..207
FT /note="C-type lectin domain family 2 member D"
FT /id="PRO_0000315286"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 87..202
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6E7D"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6E7D"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:6E7D"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:6E7D"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6E7D"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6E7D"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:6E7D"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:6E7D"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:6E7D"
SQ SEQUENCE 207 AA; 23647 MW; E4340FCB1E0BD718 CRC64;
MCVTKASLPM LSPTGSPQEV EVGKILQGKR HGTISPESCA KLYCYYGVIM VLTVAVIALS
VALSATKTEQ IPVNKTYAAC PQNWIGVENK CFYFSEYPSN WTFAQAFCMA QEAQLARFDN
QDELNFLMRY KANFDSWIGL HRESSEHPWK WTDNTEYNNT IPIRGEERFA YLNNNGISST
RIYSLRMWIC SKLNSYSLHC QTPFFPS
