CLC4M_SYMSY
ID CLC4M_SYMSY Reviewed; 422 AA.
AC Q8HY11;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Symphalangus syndactylus (Siamang) (Hylobates syndactylus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Symphalangus.
OX NCBI_TaxID=9590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate B1533;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY078820; AAL89529.1; -; Genomic_DNA.
DR EMBL; AY078814; AAL89529.1; JOINED; Genomic_DNA.
DR EMBL; AY078815; AAL89529.1; JOINED; Genomic_DNA.
DR EMBL; AY078816; AAL89529.1; JOINED; Genomic_DNA.
DR EMBL; AY078817; AAL89529.1; JOINED; Genomic_DNA.
DR EMBL; AY078818; AAL89529.1; JOINED; Genomic_DNA.
DR EMBL; AY078819; AAL89529.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8HY11; -.
DR SMR; Q8HY11; -.
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..422
FT /note="C-type lectin domain family 4 member M"
FT /id="PRO_0000046629"
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..422
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 DOMAIN 297..413
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 108..292
FT /note="8 X approximate tandem repeats"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 401
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 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 288..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 291..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 319..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 391..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 422 AA; 48031 MW; 1F24460CBF991DC3 CRC64;
MSDSKEPRVQ PLGLLEEDPT TSGIRLFPRD FQFQQTHGHK SSTGCLGHGP LVLQLLSFAL
LAGVLVAILV QVYKVPSSLS QEQSEQDVIY QNLTQLKAAV GELSEKSKLQ EIYQELTQLK
AAVGELPEKS KQQEIYQELT QLKASVGELP EKSQLQEIYQ ELTRLKAAVG ELPEESRLQE
IYQELTRLKA AVGELPEKSR LQEIYQELTR LKAAVGELPE KSRLQEIYQE LTRLKAAVGE
LPEKSKLQEI YQELTRLKAA VGELPDQSKQ QQIYQELTDL KTAFERLCCR CPKDWTFFQG
NCYFMSNSQR NWHDSVTACQ EVGAQLVVIK SAEEQNFLQL QTSRSNRFSW MGLSDLNQEG
TWQWVDGSPL SSSFQRYWNS GEPNNSGDED CAEFSGSGWN DNRCNVDNYW ICKKPIACFR
DE
