ID   CLC10_RAT               Reviewed;         306 AA.
AC   P49301;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 131.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2358462; DOI=10.1016/s0021-9258(19)38590-4;
RA   Ii M., Kurata H., Itoh N., Yamashina I., Kawasaki T.;
RT   "Molecular cloning and sequence analysis of cDNA encoding the macrophage
RT   lectin specific for galactose and N-acetylgalactosamine.";
RL   J. Biol. Chem. 265:11295-11298(1990).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 9-28.
RX   PubMed=3421964; DOI=10.1016/s0006-291x(88)80554-0;
RA   Ii M., Kawasaki T., Yamashina I.;
RT   "Structural similarity between the macrophage lectin specific for
RT   galactose/N-acetylgalactosamine and the hepatic asialoglycoprotein binding
RT   protein.";
RL   Biochem. Biophys. Res. Commun. 155:720-725(1988).
CC   -!- FUNCTION: Recognizes terminal galactose and N-acetylgalactosamine
CC       units.
CC   -!- SUBUNIT: Homooligomer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
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DR   EMBL; J05495; AAA41216.1; -; mRNA.
DR   PIR; A42230; A42230.
DR   AlphaFoldDB; P49301; -.
DR   SMR; P49301; -.
DR   STRING; 10116.ENSRNOP00000025308; -.
DR   GlyGen; P49301; 2 sites.
DR   PaxDb; P49301; -.
DR   UCSC; RGD:621158; rat.
DR   RGD; 621158; Clec10a.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; P49301; -.
DR   PhylomeDB; P49301; -.
DR   PRO; PR:P49301; -.
DR   Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
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..306
FT                   /note="C-type lectin domain family 10 member A"
FT                   /id="PRO_0000046658"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          174..300
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        175..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        203..298
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        276..290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   306 AA;  34242 MW;  D68A5DFF0B9E8F13 CRC64;
     MTMAYENFQN LGSEEKNQEA GKAPPQSFLC NILSWTHLLL FSLGLSLLLL VVISVIGSQN
     SQLRRDLETL RTTLDNTTSN TKAELQALAS RGDSLQTGIN SLKVEVDDHG QELQAGRGLS
     QKVASLESTV EKKEQTLRTD LSEITDRVQQ LGKDLKTLTC QLASLKNNGS AVACCPLHWM
     EHEGSCYWFS QSGKPWPEAD KYCQLENSNL VVVNSLAEQN FLQTHMGSVV TWIGLTDQNG
     PWRWVDGTDY EKGFTHWAPK QPDNWYGHGL GGGEDCAHFT SDGRWNDDVC QRPYRWVCEM
     KLAKDS