CLC4M_PANTR
ID CLC4M_PANTR Reviewed; 445 AA.
AC Q8HYC0; Q8HY05;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Isolate B1437, and Isolate CH1602; TISSUE=Liver;
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; AY078856; AAL89536.1; -; mRNA.
DR EMBL; AY078863; AAL89535.1; -; Genomic_DNA.
DR EMBL; AY078857; AAL89535.1; JOINED; Genomic_DNA.
DR EMBL; AY078858; AAL89535.1; JOINED; Genomic_DNA.
DR EMBL; AY078859; AAL89535.1; JOINED; Genomic_DNA.
DR EMBL; AY078860; AAL89535.1; JOINED; Genomic_DNA.
DR EMBL; AY078861; AAL89535.1; JOINED; Genomic_DNA.
DR EMBL; AY078862; AAL89535.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001065255.1; NM_001071787.1.
DR AlphaFoldDB; Q8HYC0; -.
DR SMR; Q8HYC0; -.
DR STRING; 9598.ENSPTRP00000054847; -.
DR PaxDb; Q8HYC0; -.
DR Ensembl; ENSPTRT00000062284; ENSPTRP00000054840; ENSPTRG00000010404.
DR GeneID; 455661; -.
DR KEGG; ptr:455661; -.
DR CTD; 10332; -.
DR VGNC; VGNC:6620; CLEC4M.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000167383; -.
DR HOGENOM; CLU_049894_7_3_1; -.
DR InParanoid; Q8HYC0; -.
DR OrthoDB; 1509611at2759; -.
DR TreeFam; TF333341; -.
DR Proteomes; UP000002277; Chromosome 19.
DR Bgee; ENSPTRG00000010404; Expressed in lymph node and 7 other tissues.
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:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; IEA:Ensembl.
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 GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Adaptive immunity; Calcium; Disulfide bond; Endocytosis; Glycoprotein;
KW Immunity; Innate immunity; Lectin; Mannose-binding; Membrane;
KW Metal-binding; Receptor; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..445
FT /note="C-type lectin domain family 4 member M"
FT /id="PRO_0000046630"
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..445
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 108..130
FT /note="1"
FT REPEAT 131..151
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 REPEAT 269..291
FT /note="8"
FT REPEAT 292..314
FT /note="9"
FT DOMAIN 320..436
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 108..315
FT /note="9 X approximate tandem repeats"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 424
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 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 311..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 314..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 342..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 414..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 445 AA; 50544 MW; 4B77D8968E9CA1FF CRC64;
MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGP LVLQLLSFTL
LAGVLVAILV QVSKVPSSLS QEQSEQDTIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK
AAVGELPEKS KLQEIYQELT QLKAAVGELP EKSKLQEIYQ ELTQLKAAVG ELPEKSKLQE
IYQELTQLKA AVGELPEKSK LQEIYQELTQ LKAAVGELPE KSKLQETYQE LTQLKAAVGE
LPEKSKLQEI YQELTQLKAA VGELPEKSEL QEIYQELTQL KAALGKLPDQ SKQQQIYQEL
TDLKTAFERL CRHCPKDWTF FQGNCYFMSN SQRNWHNSVT ACREVRAQLV VIKSAEEQNF
LQLQTSRSNR FSWMGLSDLN QEGTWQWVDG SPLSPSFQRY WNSGEPNNSG NEDCAEFSGS
GWNDNRCDID NYWICKKPAV CFRDE
