ID   209L2_MACMU             Reviewed;         256 AA.
AC   Q8MIS5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=CD209 antigen-like protein 2;
DE   AltName: CD_antigen=CD209;
GN   Name=CD209L2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH ICAM3;
RP   HIV-1 AND SIV.
RX   PubMed=12477827; DOI=10.1128/jvi.77.1.217-227.2003;
RA   Bashirova A.A., Wu L., Cheng J., Martin T.D., Martin M.P., Benveniste R.E.,
RA   Lifson J.D., Kewalramani V.N., Hughes A., Carrington M.;
RT   "Novel member of the CD209 (DC-SIGN) gene family in primates.";
RL   J. Virol. 77:217-227(2003).
CC   -!- FUNCTION: Probable pathogen-recognition receptor involved in peripheral
CC       immune surveillance in liver. May mediate the endocytosis of pathogens
CC       which are subsequently degraded in lysosomal compartments. Probably
CC       recognizes in a calcium-dependent manner high mannose N-linked
CC       oligosaccharides in a variety of pathogen antigens. Is a receptor for
CC       ICAM3, probably by binding to mannose-like carbohydrates (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver and axillary lymph
CC       nodes. At very low levels also found in other tissues.
CC       {ECO:0000269|PubMed:12477827}.
CC   -!- MISCELLANEOUS: In vitro, is a weak receptor for HIV-1 and SIV and
CC       poorly transmits HIV-1 to permissive T-cells relative to CD209.
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DR   EMBL; AY074781; AAL71882.1; -; mRNA.
DR   RefSeq; NP_001028123.1; NM_001032951.1.
DR   AlphaFoldDB; Q8MIS5; -.
DR   SMR; Q8MIS5; -.
DR   GeneID; 574373; -.
DR   KEGG; mcc:574373; -.
DR   CTD; 574373; -.
DR   InParanoid; Q8MIS5; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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   Adaptive immunity; Calcium; Disulfide bond; Endocytosis; Immunity;
KW   Innate immunity; Lectin; Mannose-binding; Membrane; Metal-binding;
KW   Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..256
FT                   /note="CD209 antigen-like protein 2"
FT                   /id="PRO_0000046631"
FT   TOPO_DOM        1..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..230
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   MOTIF           14..15
FT                   /note="Endocytosis signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..119
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        136..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        208..221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   256 AA;  28867 MW;  A07C3BA415B9C022 CRC64;
     MSDSKEPRAQ PLGLLEEEEL ITSSMNFFPR DFGFRQTRGY KSLAGCLGHA PLVLPLLFFT
     LFTGLLVAIL VQVSKNPSSQ RLDQSKQDEI SQDLSQLKAA VERLCRPCPW EWTFFQGNCY
     FISNSQRNWH DSITACQEVG AQLVVIKSAE EQNFLQLQSS RSNRFAWMGL SDLNQEDMWQ
     WVDDSPLSTS FKQYWNRGEP NNIGEEDCVE FNGNGWNDDK CSAAKFWICK KSAASCSRDE
     GQLLSSASAS PIAHAA