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C-type lectin domain family 10 member A (MMGL) (Macrophage asialoglycoprotein-binding protein 1) (M-ASGP-BP-1) (Macrophage galactose/N-acetylgalactosamine-specific lectin)

 CLC10_MOUSE             Reviewed;         304 AA.
P49300; Q549F6; Q91YT3;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
05-DEC-2018, entry version 133.
RecName: Full=C-type lectin domain family 10 member A;
AltName: Full=MMGL;
AltName: Full=Macrophage asialoglycoprotein-binding protein 1;
Short=M-ASGP-BP-1;
AltName: Full=Macrophage galactose/N-acetylgalactosamine-specific lectin;
Name=Clec10a; Synonyms=Mgl, Mgl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeN;
PubMed=1587794;
Sato M., Kawakamyi K., Osawa T., Toyoshima S.;
"Molecular cloning and expression of cDNA encoding a galactose/N-
acetylgalactosamine-specific lectin on mouse tumoricidal
macrophages.";
J. Biochem. 111:331-336(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=10541808; DOI=10.1007/s002510050687;
Tsuiji M., Fujimori M., Seldin M.F., Taketo M.M., Irimura T.;
"Genomic structure and chromosomal location of the mouse macrophage C-
type lectin gene.";
Immunogenetics 50:67-70(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 102-120 AND 137-151.
STRAIN=C3H/HeN;
PubMed=3241002; DOI=10.1093/oxfordjournals.jbchem.a122518;
Oda S., Sato M., Toyoshima S., Osawa T.;
"Purification and characterization of a lectin-like molecule specific
for galactose/N-acetyl-galactosamine from tumoricidal macrophages.";
J. Biochem. 104:600-605(1988).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12016228; DOI=10.1074/jbc.M203774200;
Tsuiji M., Fujimori M., Ohashi Y., Higashi N., Onami T.M.,
Hedrick S.M., Irimura T.;
"Molecular cloning and characterization of a novel mouse macrophage C-
type lectin, mMGL2, which has a distinct carbohydrate specificity from
mMGL1.";
J. Biol. Chem. 277:28892-28901(2002).
[8]
INTERACTION WITH SIGLEC1, AND TISSUE SPECIFICITY.
PubMed=15364954; DOI=10.1074/jbc.M409300200;
Kumamoto Y., Higashi N., Denda-Nagai K., Tsuiji M., Sato K.,
Crocker P.R., Irimura T.;
"Identification of sialoadhesin as a dominant lymph node counter-
receptor for mouse macrophage galactose-type C-type lectin 1.";
J. Biol. Chem. 279:49274-49280(2004).
[9]
FUNCTION.
PubMed=19995956; DOI=10.1084/jem.20091333;
Westcott D.J., Delproposto J.B., Geletka L.M., Wang T., Singer K.,
Saltiel A.R., Lumeng C.N.;
"MGL1 promotes adipose tissue inflammation and insulin resistance by
regulating 7/4hi monocytes in obesity.";
J. Exp. Med. 206:3143-3156(2009).
-!- FUNCTION: Recognizes terminal galactose and N-acetylgalactosamine
units. May participate in the interaction between tumoricidal
macrophages and tumor cells. Plays a role in the recruitment of
inflammatory monocytes to adipose tissue in diet-induced obesity.
{ECO:0000269|PubMed:19995956}.
-!- SUBUNIT: Homooligomer. Interacts with SIGLEC1, which may act as a
counter-receptor for CLEC10A in lymph node.
{ECO:0000269|PubMed:15364954}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
protein.
-!- TISSUE SPECIFICITY: Detected in lymph node in the subcapsular
sinus, interfollicular regions, T and B-cell boundary and in the
areas surrounding high endothelial venules (at protein level).
Expressed on the surface of activated macrophages. Expressed in
heart, lung, testis, skeletal muscle, spleen, brain, kidney and
thymus. Expressed in P388, RAW 264.7 and M1 cell lines.
{ECO:0000269|PubMed:12016228, ECO:0000269|PubMed:15364954}.
-!- DEVELOPMENTAL STAGE: Detected in E7, E11, E15 and E17 embryo.
{ECO:0000269|PubMed:12016228}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=MGL1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_158";
-----------------------------------------------------------------------
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EMBL; S36676; AAB22171.1; -; mRNA.
EMBL; AF132744; AAD31028.1; -; Genomic_DNA.
EMBL; CH466596; EDL12536.1; -; Genomic_DNA.
EMBL; AL669869; CAI35217.1; -; Genomic_DNA.
EMBL; CR933731; CAM28085.1; -; Genomic_DNA.
EMBL; BC014811; AAH14811.1; -; mRNA.
CCDS; CCDS24936.1; -.
PIR; JX0209; JX0209.
RefSeq; NP_034926.1; NM_010796.3.
UniGene; Mm.252405; -.
ProteinModelPortal; P49300; -.
SMR; P49300; -.
IntAct; P49300; 1.
MINT; P49300; -.
STRING; 10090.ENSMUSP00000000327; -.
iPTMnet; P49300; -.
PhosphoSitePlus; P49300; -.
PaxDb; P49300; -.
PRIDE; P49300; -.
Ensembl; ENSMUST00000102571; ENSMUSP00000099631; ENSMUSG00000000318.
GeneID; 17312; -.
KEGG; mmu:17312; -.
UCSC; uc007jtx.2; mouse.
CTD; 10462; -.
MGI; MGI:96975; Clec10a.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
GeneTree; ENSGT00940000162036; -.
HOGENOM; HOG000034093; -.
HOVERGEN; HBG000270; -.
InParanoid; P49300; -.
KO; K06721; -.
PhylomeDB; P49300; -.
PRO; PR:P49300; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000318; Expressed in 113 organ(s), highest expression level in zone of skin.
ExpressionAtlas; P49300; baseline and differential.
Genevisible; P49300; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; IMP:MGI.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Lectin; Membrane; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 304 C-type lectin domain family 10 member A.
/FTId=PRO_0000046657.
TOPO_DOM 1 35 Cytoplasmic. {ECO:0000255}.
TRANSMEM 36 56 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 57 304 Extracellular. {ECO:0000255}.
DOMAIN 172 298 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 173 184 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 201 296 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 274 288 {ECO:0000255|PROSITE-ProRule:PRU00040}.
CONFLICT 71 71 T -> I (in Ref. 5; AAH14811).
{ECO:0000305}.
CONFLICT 128 128 V -> L (in Ref. 5; AAH14811).
{ECO:0000305}.
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


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