CLC4M_GORGO
ID CLC4M_GORGO Reviewed; 376 AA.
AC Q8HY06;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Ggo-3;
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; AY078855; AAL89534.1; -; Genomic_DNA.
DR EMBL; AY078849; AAL89534.1; JOINED; Genomic_DNA.
DR EMBL; AY078850; AAL89534.1; JOINED; Genomic_DNA.
DR EMBL; AY078851; AAL89534.1; JOINED; Genomic_DNA.
DR EMBL; AY078852; AAL89534.1; JOINED; Genomic_DNA.
DR EMBL; AY078853; AAL89534.1; JOINED; Genomic_DNA.
DR EMBL; AY078854; AAL89534.1; JOINED; Genomic_DNA.
DR RefSeq; XP_004059943.1; XM_004059895.1.
DR AlphaFoldDB; Q8HY06; -.
DR BMRB; Q8HY06; -.
DR SMR; Q8HY06; -.
DR STRING; 9593.ENSGGOP00000021876; -.
DR Ensembl; ENSGGOT00000026262; ENSGGOP00000021876; ENSGGOG00000015715.
DR GeneID; 101152880; -.
DR KEGG; ggo:101152880; -.
DR CTD; 10332; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000167383; -.
DR HOGENOM; CLU_049894_7_3_1; -.
DR InParanoid; Q8HY06; -.
DR OMA; QLQTCNT; -.
DR OrthoDB; 1509611at2759; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000015715; Expressed in liver and 1 other tissue.
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 3: Inferred from homology;
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..376
FT /note="C-type lectin domain family 4 member M"
FT /id="PRO_0000046625"
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..376
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 DOMAIN 251..367
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 108..246
FT /note="6 X approximate tandem repeats"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 355
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 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 242..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 245..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 273..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 345..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 376 AA; 42721 MW; CB6D0B03CDCB9A9B CRC64;
MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA LVLQLLSFTL
LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK
AAVGELPEKS KLQEIYQELT QLKAAVGELP EKSKLQEIYQ ELTQLKAAVG ELPEKSKLQE
IYQELTRLKA AVGELPEKSK LQEIYQELTQ LKAALGKLPD QSKQQQIYQE LTDLKTAFER
LCRHCPKDWT FFQGNCYFMS NSQRNWHNSV TACQEVRAQL VVIKSAEEQN FLQLQTSRSN
RFSWMGLSDL NQEGTWQWVD GSPLSPSFQR YWNSGEPNNS GNEDCAEFSG SGWNDNRCDV
DNYWICKKPT VCFRDE
