CLC2I_MOUSE
ID CLC2I_MOUSE Reviewed; 217 AA.
AC Q9WVF9; Q1AFZ2; Q7TSP6; Q7TSP7; Q8BFR3; Q924B1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=C-type lectin domain family 2 member I;
DE AltName: Full=C-type lectin-related protein DCL1;
DE AltName: Full=C-type lectin-related protein G;
DE Short=Clr-g;
DE AltName: Full=Lymphoid-derived C-type lectin-1;
DE Short=LCL-1;
DE AltName: Full=Osteoclast inhibitory lectin-related protein 2;
DE Short=Ocil-related protein 2;
GN Name=Clec2i; Synonyms=Clrg, Dcl1, Ocilrp2;
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 [MRNA] (ISOFORM 1), 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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv, and C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=15963483; DOI=10.1016/j.cellimm.2005.04.021;
RA Tian W., Nunez R., Cheng S., Ding Y., Tumang J., Lyddane C., Roman C.,
RA Liou H.-C.;
RT "C-type lectin OCILRP2/Clr-g and its ligand NKRP1f costimulate T cell
RT proliferation and IL-2 production.";
RL Cell. Immunol. 234:39-53(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Dendritic cell;
RA Gorski K.S., Huang X., Pardoll D.M., Tsuchiya H.;
RT "A novel c-type lectin (DCL1) expressed in bone marrow derived dendritic
RT cells.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-171.
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).
CC -!- FUNCTION: Inhibits osteoclast formation. Receptor for KLRB1F. Enhances
CC T-cell activation. Plays a role in splenocyte activation, T-cell
CC responses and IL-2 production. {ECO:0000269|PubMed:12374791,
CC ECO:0000269|PubMed:15963483}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9WVF9-1; Sequence=Displayed;
CC Name=2; Synonyms=Lymphoid-derived C-type lectin-1b, LCL-1b;
CC IsoId=Q9WVF9-2; Sequence=VSP_030532;
CC Name=3; Synonyms=Lymphoid-derived C-type lectin-1a, LCL-1a;
CC IsoId=Q9WVF9-3; Sequence=VSP_030531, VSP_030532;
CC Name=4; Synonyms=Lymphoid-derived C-type lectin-1c, LCL-1c;
CC IsoId=Q9WVF9-4; Sequence=VSP_030530;
CC -!- TISSUE SPECIFICITY: Detected in osteoblasts, growth plate chondrocytes
CC and skeletal muscle overlying the bone (at protein level). Detected in
CC spleen, B-cells, dendritic cells, thymus, and in IL2-activated natural
CC killer cells. {ECO:0000269|PubMed:11398965,
CC ECO:0000269|PubMed:12374791, ECO:0000269|PubMed:15963483}.
CC -!- INDUCTION: Up-regulated in CD4(+) T-cells upon stimulation with CD3-
CC ligands. Up-regulated in cultured calvarial osteoblasts by 1,25-
CC dihydroxyvitamin D3. Constitutively expressed in cultured bone marrow
CC cells during osteoclast formation. {ECO:0000269|PubMed:12374791,
CC ECO:0000269|PubMed:15963483}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK70359.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF350411; AAK70359.1; ALT_INIT; mRNA.
DR EMBL; AY137343; AAN15951.1; -; Genomic_DNA.
DR EMBL; AY137343; AAN15952.1; -; Genomic_DNA.
DR EMBL; AY137344; AAN15953.1; -; mRNA.
DR EMBL; AY137345; AAN15954.1; -; mRNA.
DR EMBL; AY256574; AAP32744.1; -; mRNA.
DR EMBL; AY256575; AAP32745.1; -; mRNA.
DR EMBL; AY256576; AAP32746.1; -; mRNA.
DR EMBL; AF121352; AAD22055.1; -; mRNA.
DR EMBL; DQ143112; ABA43362.1; -; Genomic_DNA.
DR CCDS; CCDS51920.1; -. [Q9WVF9-1]
DR CCDS; CCDS71844.1; -. [Q9WVF9-2]
DR CCDS; CCDS85166.1; -. [Q9WVF9-4]
DR RefSeq; NP_001276635.1; NM_001289706.1.
DR RefSeq; NP_001276636.1; NM_001289707.1. [Q9WVF9-2]
DR RefSeq; NP_001276637.1; NM_001289708.1. [Q9WVF9-4]
DR RefSeq; NP_064653.1; NM_020257.2. [Q9WVF9-1]
DR PDB; 3RS1; X-ray; 1.94 A; A/B=85-206.
DR PDBsum; 3RS1; -.
DR AlphaFoldDB; Q9WVF9; -.
DR SMR; Q9WVF9; -.
DR BioGRID; 220229; 1.
DR STRING; 10090.ENSMUSP00000123804; -.
DR GlyGen; Q9WVF9; 1 site.
DR iPTMnet; Q9WVF9; -.
DR PhosphoSitePlus; Q9WVF9; -.
DR PaxDb; Q9WVF9; -.
DR PRIDE; Q9WVF9; -.
DR ProteomicsDB; 283277; -. [Q9WVF9-1]
DR ProteomicsDB; 283278; -. [Q9WVF9-2]
DR ProteomicsDB; 283279; -. [Q9WVF9-3]
DR ProteomicsDB; 283280; -. [Q9WVF9-4]
DR DNASU; 93675; -.
DR Ensembl; ENSMUST00000032519; ENSMUSP00000032519; ENSMUSG00000030365. [Q9WVF9-1]
DR Ensembl; ENSMUST00000159866; ENSMUSP00000123804; ENSMUSG00000030365. [Q9WVF9-2]
DR Ensembl; ENSMUST00000160867; ENSMUSP00000145115; ENSMUSG00000030365. [Q9WVF9-4]
DR GeneID; 93675; -.
DR KEGG; mmu:93675; -.
DR UCSC; uc009eeu.2; mouse. [Q9WVF9-1]
DR CTD; 93675; -.
DR MGI; MGI:2136650; Clec2i.
DR VEuPathDB; HostDB:ENSMUSG00000030365; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155319; -.
DR HOGENOM; CLU_049894_8_1_1; -.
DR InParanoid; Q9WVF9; -.
DR OMA; NISSCCA; -.
DR OrthoDB; 1140637at2759; -.
DR TreeFam; TF351467; -.
DR BioGRID-ORCS; 93675; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Clec2i; mouse.
DR PRO; PR:Q9WVF9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9WVF9; protein.
DR Bgee; ENSMUSG00000030365; Expressed in thymus and 36 other tissues.
DR ExpressionAtlas; Q9WVF9; baseline and differential.
DR Genevisible; Q9WVF9; MM.
DR GO; GO:0009986; C:cell surface; IDA: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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001765; P:membrane raft assembly; NAS:BHF-UCL.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; NAS:BHF-UCL.
DR GO; GO:2000522; P:positive regulation of immunological synapse formation; NAS:BHF-UCL.
DR GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0032663; P:regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP: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; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="C-type lectin domain family 2 member I"
FT /id="PRO_0000315291"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 99..203
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 120..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15963483"
FT /id="VSP_030530"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15963483"
FT /id="VSP_030531"
FT VAR_SEQ 35
FT /note="G -> GVQCC (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12374791,
FT ECO:0000303|PubMed:15963483"
FT /id="VSP_030532"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3RS1"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:3RS1"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:3RS1"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3RS1"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3RS1"
SQ SEQUENCE 217 AA; 24671 MW; 28D497A39F05DCD8 CRC64;
MPDCLETGEK LFVHNMNAQC VQKPEEGNGP LGTGGKIVQG KCFRIISTVS PVKLYCCYGV
IMVLTVAVIA LSVALSTKKT EQIIINKTYA ACSKNWTGVG NKCFYFSGYP RNWTFAQAFC
MAQEAQLARF DNEEELIFLK RFKGDFDCWI GLHRESSEHP WKWTNNTEYN NMNPILGVGR
YAYLSSDRIS SSRSYINRMW ICSKLNNYNL HCQTPPV
