CLC10_MOUSE
ID CLC10_MOUSE Reviewed; 304 AA.
AC P49300; Q549F6; Q91YT3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=C-type lectin domain family 10 member A;
DE AltName: Full=MMGL;
DE AltName: Full=Macrophage asialoglycoprotein-binding protein 1;
DE Short=M-ASGP-BP-1;
DE AltName: Full=Macrophage galactose/N-acetylgalactosamine-specific lectin;
GN Name=Clec10a; Synonyms=Mgl, Mgl1;
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].
RC STRAIN=C3H/HeN;
RX PubMed=1587794; DOI=10.1093/oxfordjournals.jbchem.a123758;
RA Sato M., Kawakamyi K., Osawa T., Toyoshima S.;
RT "Molecular cloning and expression of cDNA encoding a galactose/N-
RT acetylgalactosamine-specific lectin on mouse tumoricidal macrophages.";
RL J. Biochem. 111:331-336(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10541808; DOI=10.1007/s002510050687;
RA Tsuiji M., Fujimori M., Seldin M.F., Taketo M.M., Irimura T.;
RT "Genomic structure and chromosomal location of the mouse macrophage C-type
RT lectin gene.";
RL Immunogenetics 50:67-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RG The mouse genome sequencing consortium;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 102-120 AND 137-151.
RC STRAIN=C3H/HeN;
RX PubMed=3241002; DOI=10.1093/oxfordjournals.jbchem.a122518;
RA Oda S., Sato M., Toyoshima S., Osawa T.;
RT "Purification and characterization of a lectin-like molecule specific for
RT galactose/N-acetyl-galactosamine from tumoricidal macrophages.";
RL J. Biochem. 104:600-605(1988).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12016228; DOI=10.1074/jbc.m203774200;
RA Tsuiji M., Fujimori M., Ohashi Y., Higashi N., Onami T.M., Hedrick S.M.,
RA Irimura T.;
RT "Molecular cloning and characterization of a novel mouse macrophage C-type
RT lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1.";
RL J. Biol. Chem. 277:28892-28901(2002).
RN [8]
RP INTERACTION WITH SIGLEC1, AND TISSUE SPECIFICITY.
RX PubMed=15364954; DOI=10.1074/jbc.m409300200;
RA Kumamoto Y., Higashi N., Denda-Nagai K., Tsuiji M., Sato K., Crocker P.R.,
RA Irimura T.;
RT "Identification of sialoadhesin as a dominant lymph node counter-receptor
RT for mouse macrophage galactose-type C-type lectin 1.";
RL J. Biol. Chem. 279:49274-49280(2004).
RN [9]
RP FUNCTION.
RX PubMed=19995956; DOI=10.1084/jem.20091333;
RA Westcott D.J., Delproposto J.B., Geletka L.M., Wang T., Singer K.,
RA Saltiel A.R., Lumeng C.N.;
RT "MGL1 promotes adipose tissue inflammation and insulin resistance by
RT regulating 7/4hi monocytes in obesity.";
RL J. Exp. Med. 206:3143-3156(2009).
CC -!- FUNCTION: Recognizes terminal galactose and N-acetylgalactosamine
CC units. May participate in the interaction between tumoricidal
CC macrophages and tumor cells. Plays a role in the recruitment of
CC inflammatory monocytes to adipose tissue in diet-induced obesity.
CC {ECO:0000269|PubMed:19995956}.
CC -!- SUBUNIT: Homooligomer. Interacts with SIGLEC1, which may act as a
CC counter-receptor for CLEC10A in lymph node.
CC {ECO:0000269|PubMed:15364954}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in lymph node in the subcapsular sinus,
CC interfollicular regions, T and B-cell boundary and in the areas
CC surrounding high endothelial venules (at protein level). Expressed on
CC the surface of activated macrophages. Expressed in heart, lung, testis,
CC skeletal muscle, spleen, brain, kidney and thymus. Expressed in P388,
CC RAW 264.7 and M1 cell lines. {ECO:0000269|PubMed:12016228,
CC ECO:0000269|PubMed:15364954}.
CC -!- DEVELOPMENTAL STAGE: Detected in 7 dpc, 11 dpc, 15 dpc and 17 dpc
CC embryo. {ECO:0000269|PubMed:12016228}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=MGL1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_158";
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DR EMBL; S36676; AAB22171.1; -; mRNA.
DR EMBL; AF132744; AAD31028.1; -; Genomic_DNA.
DR EMBL; CH466596; EDL12536.1; -; Genomic_DNA.
DR EMBL; AL669869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014811; AAH14811.1; -; mRNA.
DR CCDS; CCDS24936.1; -.
DR PIR; JX0209; JX0209.
DR RefSeq; NP_034926.1; NM_010796.3.
DR AlphaFoldDB; P49300; -.
DR SMR; P49300; -.
DR STRING; 10090.ENSMUSP00000000327; -.
DR GlyGen; P49300; 2 sites.
DR iPTMnet; P49300; -.
DR PhosphoSitePlus; P49300; -.
DR PaxDb; P49300; -.
DR PRIDE; P49300; -.
DR ProteomicsDB; 283275; -.
DR DNASU; 17312; -.
DR Ensembl; ENSMUST00000102571; ENSMUSP00000099631; ENSMUSG00000000318.
DR GeneID; 17312; -.
DR KEGG; mmu:17312; -.
DR UCSC; uc007jtx.2; mouse.
DR CTD; 10462; -.
DR MGI; MGI:96975; Clec10a.
DR VEuPathDB; HostDB:ENSMUSG00000000318; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162036; -.
DR HOGENOM; CLU_049894_2_0_1; -.
DR InParanoid; P49300; -.
DR PhylomeDB; P49300; -.
DR BioGRID-ORCS; 17312; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Clec10a; mouse.
DR PRO; PR:P49300; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P49300; protein.
DR Bgee; ENSMUSG00000000318; Expressed in stroma of bone marrow and 112 other tissues.
DR ExpressionAtlas; P49300; baseline and differential.
DR Genevisible; P49300; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; IMP:MGI.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..304
FT /note="C-type lectin domain family 10 member A"
FT /id="PRO_0000046657"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 172..298
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 201..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 274..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 71
FT /note="T -> I (in Ref. 5; AAH14811)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="V -> L (in Ref. 5; AAH14811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34596 MW; 3F79CD12C34F5BCC CRC64;
MIYENLQNSR IEEKTQEPGK APSQSFLWRI LSWTHLLLFS LGLSLLLLVV VSVIGSQNSQ
LRRDLGTLRA TLDNTTSKIK AEFQSLDSRA DSFEKGISSL KVDVEDHRQE LQAGRDLSQK
VTSLESTVEK REQALKTDLS DLTDHVQQLR KDLKALTCQL ANLKNNGSEV ACCPLHWTEH
EGSCYWFSES EKSWPEADKY CRLENSHLVV VNSLEEQNFL QNRLANVVSW IGLTDQNGPW
RWVDGTDFEK GFKNWAPLQP DNWFGHGLGG GEDCAHITTG GPWNDDVCQR TFRWICEMKL
AKES
