CLC1B_MOUSE
ID CLC1B_MOUSE Reviewed; 229 AA.
AC Q9JL99; A0T1G2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=C-type lectin domain family 1 member B;
DE AltName: Full=C-type lectin-like receptor 2;
DE Short=CLEC-2;
GN Name=Clec1b; Synonyms=Clec2;
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 TISSUE=Spleen;
RX PubMed=10671229;
RX DOI=10.1002/1521-4141(200002)30:2<697::aid-immu697>3.0.co;2-m;
RA Colonna M., Samaridis J., Angman L.;
RT "Molecular characterization of two novel C-type lectin-like receptors, one
RT of which is selectively expressed in human dendritic cells.";
RL Eur. J. Immunol. 30:697-704(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ;
RA Xie J., Wu T., Guo L., Ruan Y., Zhang S., Gu J.;
RT "Identification of alternatively spliced isoforms of mouse Clec-2.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [4]
RP GLYCOSYLATION, PHOSPHORYLATION AT TYR-7, AND TISSUE SPECIFICITY.
RX PubMed=16174766; DOI=10.1182/blood-2005-05-1994;
RA Suzuki-Inoue K., Fuller G.L.J., Garcia A., Eble J.A., Poehlmann S.,
RA Inoue O., Gartner T.K., Hughan S.C., Pearce A.C., Laing G.D.,
RA Theakston R.D.G., Schweighoffer E., Zitzmann N., Morita T.,
RA Tybulewicz V.L.J., Ozaki Y., Watson S.P.;
RT "A novel Syk-dependent mechanism of platelet activation by the C-type
RT lectin receptor CLEC-2.";
RL Blood 107:542-549(2006).
CC -!- FUNCTION: C-type lectin-like receptor that functions as a platelet
CC receptor for the lymphatic endothelial marker, PDPN. After ligand
CC activation, signals via sequential activation of SRC and SYK tyrosine
CC kinases leading to activation of PLCG2. {ECO:0000250|UniProtKB:Q9P126}.
CC -!- SUBUNIT: Homodimer. Interacts (via cytoplasmic domain) with RACK1;
CC promotes CLEC1B ubiquitination and proteasome-mediated degradation.
CC Interacts (dimer) with SYK (via SH2 domains) (By similarity). Interacts
CC with PDPN; the interaction is independent of CLEC1B glycosylation and
CC activates CLEC1B (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9P126}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q9JL99-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9JL99-2; Sequence=VSP_023516;
CC -!- TISSUE SPECIFICITY: Hematopoietic cells, megakaryocytes and platelets.
CC {ECO:0000269|PubMed:10671229, ECO:0000269|PubMed:16174766}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16174766}.
CC -!- PTM: Phosphorylated on tyrosine residue in response to rhodocytin
CC binding. {ECO:0000269|PubMed:16174766}.
CC -!- MISCELLANEOUS: Acts as a receptor for the platelet-aggregating snake
CC venom protein rhodocytin. Rhodocytin binding leads to tyrosine
CC phosphorylation and this promotes the binding of spleen tyrosine kinase
CC (Syk) and initiation of downstream tyrosine phosphorylation events and
CC activation of PLC-gamma-2 (PubMed:16174766).
CC {ECO:0000305|PubMed:16174766}.
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DR EMBL; AF201457; AAF36831.1; -; mRNA.
DR EMBL; EF070191; ABK60036.1; -; mRNA.
DR EMBL; BC064054; AAH64054.1; -; mRNA.
DR CCDS; CCDS20586.1; -. [Q9JL99-1]
DR CCDS; CCDS57452.1; -. [Q9JL99-2]
DR RefSeq; NP_001191168.1; NM_001204239.1. [Q9JL99-2]
DR RefSeq; NP_064369.1; NM_019985.3. [Q9JL99-1]
DR AlphaFoldDB; Q9JL99; -.
DR SMR; Q9JL99; -.
DR STRING; 10090.ENSMUSP00000032262; -.
DR GlyGen; Q9JL99; 4 sites.
DR iPTMnet; Q9JL99; -.
DR PhosphoSitePlus; Q9JL99; -.
DR MaxQB; Q9JL99; -.
DR PaxDb; Q9JL99; -.
DR PRIDE; Q9JL99; -.
DR ProteomicsDB; 283362; -. [Q9JL99-1]
DR ProteomicsDB; 283363; -. [Q9JL99-2]
DR Antibodypedia; 23211; 357 antibodies from 33 providers.
DR DNASU; 56760; -.
DR Ensembl; ENSMUST00000032262; ENSMUSP00000032262; ENSMUSG00000030159. [Q9JL99-1]
DR Ensembl; ENSMUST00000112081; ENSMUSP00000107712; ENSMUSG00000030159. [Q9JL99-2]
DR GeneID; 56760; -.
DR KEGG; mmu:56760; -.
DR UCSC; uc009efo.2; mouse. [Q9JL99-1]
DR UCSC; uc009efp.2; mouse. [Q9JL99-2]
DR CTD; 51266; -.
DR MGI; MGI:1913287; Clec1b.
DR VEuPathDB; HostDB:ENSMUSG00000030159; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162140; -.
DR HOGENOM; CLU_049894_9_0_1; -.
DR InParanoid; Q9JL99; -.
DR OMA; CKNKHYL; -.
DR OrthoDB; 1201127at2759; -.
DR PhylomeDB; Q9JL99; -.
DR TreeFam; TF336674; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-9707616; Heme signaling.
DR BioGRID-ORCS; 56760; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q9JL99; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JL99; protein.
DR Bgee; ENSMUSG00000030159; Expressed in blood and 95 other tissues.
DR ExpressionAtlas; Q9JL99; baseline and differential.
DR Genevisible; Q9JL99; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
DR GO; GO:0030220; P:platelet formation; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
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 Alternative splicing; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..229
FT /note="C-type lectin domain family 1 member B"
FT /id="PRO_0000280044"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 109..217
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:16174766"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 130..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 195..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 23..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023516"
SQ SEQUENCE 229 AA; 26239 MW; 1EC9377F491CA52B CRC64;
MQDEDGYITL NIKPRKQALS SAEPASSWWR VMALVLLISS MGLVVGLVAL GIMSVTQQKY
LLAEKENLSA TLQQLAKKFC QELIRQSEIK TKSTFEHKCS PCATKWRYHG DSCYGFFRRN
LTWEESKQYC TEQNATLVKT ASQSTLDYIA ERITSVRWIG LSRQNSKKDW MWEDSSVLRK
NGINLSGNTE ENMNCAYLHN GKIHPASCKE RHYLICERNA GMTRVDQLL
