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Database: UniProt
Entry: CLC1B_MOUSE
LinkDB: CLC1B_MOUSE
Original site: 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   24-JAN-2024, entry version 148.
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   GlyCosmos; Q9JL99; 4 sites, No reported glycans.
DR   GlyGen; Q9JL99; 4 sites.
DR   iPTMnet; Q9JL99; -.
DR   PhosphoSitePlus; Q9JL99; -.
DR   MaxQB; Q9JL99; -.
DR   PaxDb; 10090-ENSMUSP00000032262; -.
DR   ProteomicsDB; 283362; -. [Q9JL99-1]
DR   ProteomicsDB; 283363; -. [Q9JL99-2]
DR   Antibodypedia; 23211; 399 antibodies from 33 providers.
DR   DNASU; 56760; -.
DR   Ensembl; ENSMUST00000032262.14; ENSMUSP00000032262.8; ENSMUSG00000030159.16. [Q9JL99-1]
DR   Ensembl; ENSMUST00000112081.9; ENSMUSP00000107712.3; ENSMUSG00000030159.16. [Q9JL99-2]
DR   GeneID; 56760; -.
DR   KEGG; mmu:56760; -.
DR   UCSC; uc009efo.2; mouse. [Q9JL99-1]
DR   UCSC; uc009efp.2; mouse. [Q9JL99-2]
DR   AGR; MGI:1913287; -.
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; 5399275at2759; -.
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 75 CRISPR screens.
DR   PRO; PR:Q9JL99; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9JL99; Protein.
DR   Bgee; ENSMUSG00000030159; Expressed in blood and 96 other cell types or tissues.
DR   ExpressionAtlas; Q9JL99; baseline and differential.
DR   Genevisible; Q9JL99; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005886; C: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; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR46490:SF2; C-TYPE LECTIN DOMAIN FAMILY 1 MEMBER B; 1.
DR   PANTHER; PTHR46490; C-TYPE LECTIN DOMAIN FAMILY 12 MEMBER A-RELATED; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 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
//
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