CLC4M_HYLLA
ID CLC4M_HYLLA Reviewed; 399 AA.
AC Q8HY12;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=C-type lectin domain family 4 member M;
DE AltName: Full=CD209 antigen-like protein 1;
DE AltName: CD_antigen=CD299;
GN Name=CLEC4M; Synonyms=CD209L1;
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate B23;
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The tandem repeat domain, also called neck domain, mediates
CC oligomerization. {ECO:0000250}.
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DR EMBL; AY078813; AAL89528.1; -; Genomic_DNA.
DR EMBL; AY078807; AAL89528.1; JOINED; Genomic_DNA.
DR EMBL; AY078808; AAL89528.1; JOINED; Genomic_DNA.
DR EMBL; AY078809; AAL89528.1; JOINED; Genomic_DNA.
DR EMBL; AY078810; AAL89528.1; JOINED; Genomic_DNA.
DR EMBL; AY078811; AAL89528.1; JOINED; Genomic_DNA.
DR EMBL; AY078812; AAL89528.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8HY12; -.
DR SMR; Q8HY12; -.
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 3: Inferred from homology;
KW Adaptive immunity; Calcium; Disulfide bond; Endocytosis; Glycoprotein;
KW Immunity; Innate immunity; Lectin; Mannose-binding; Membrane;
KW Metal-binding; Receptor; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..399
FT /note="C-type lectin domain family 4 member M"
FT /id="PRO_0000046628"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 108..130
FT /note="1"
FT REPEAT 131..153
FT /note="2"
FT REPEAT 154..176
FT /note="3"
FT REPEAT 177..199
FT /note="4"
FT REPEAT 200..222
FT /note="5"
FT REPEAT 223..245
FT /note="6"
FT REPEAT 246..268
FT /note="7"
FT DOMAIN 274..390
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 108..269
FT /note="7 X approximate tandem repeats"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 265..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 268..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 296..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 368..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 399 AA; 45404 MW; DEC669244205B27A CRC64;
MSDSKEQRVQ PLGLLEEDPT TSGIRLFPRD FQFQQTHGHK SSTGCLGHGP LVLQLLSFTL
LAGVLVAILV QVYKVPSSLS QEQSEQDVIY QNLTQLKAAV GELSEKSKLQ EIYQELIQLK
AAVGELPEKS TLQEIYQELT RLKAAVGELP EKSRLQEIYQ ELTRLKAAVG ELPEKSKQQE
IYQELTRLKA AVGELPEKSK QQEIYQELTR LKAAVGELPE KSKQQEIYQE LTRLKAAVGE
LPDQSKQQQI YQELTDLKTA FERLCCRCPK DWTFFQGNCY FISNSQRNWH DSVTACREVG
AQLVVIKSAE EQNFLQLQSS RSNRFAWMGL SDLNQEGTWQ WVDGSPLSSS FQRYWNSGEP
NNSGDEDCAE FSGSGWNDNR CNVDNYWICK KPTACFRDE
