CLC5A_PIG
ID CLC5A_PIG Reviewed; 185 AA.
AC Q9GLF3; Q9GLF4;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=C-type lectin domain family 5 member A;
DE AltName: Full=C-type lectin superfamily member 5;
DE AltName: Full=Myeloid DAP12-associating lectin 1;
DE Short=MDL-1;
GN Name=CLEC5A; Synonyms=CLECSF5, MDL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH TYROBP.
RX PubMed=11414735; DOI=10.1006/cimm.2001.1782;
RA Yim D., Jie H.-B., Sotiriadis J., Kim Y.-S., Kim Y.B.;
RT "Molecular cloning and expression pattern of porcine myeloid DAP12-
RT associating lectin-1.";
RL Cell. Immunol. 209:42-48(2001).
CC -!- FUNCTION: Functions as a positive regulator of osteoclastogenesis (By
CC similarity). Cell surface receptor that signals via TYROBP
CC (PubMed:11414735). Regulates inflammatory responses (By similarity).
CC {ECO:0000250|UniProtKB:Q9R007, ECO:0000269|PubMed:11414735}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (By similarity). The
CC majority of CLEC5A is expressed as a monomeric form on macrophages (By
CC similarity). Interacts with TYROBP/DAP12 (PubMed:11414735). The
CC interaction with TYROBP is required for CLEC5 cell surface expression
CC (PubMed:11414735). Interacts with HCST/DAP10 (By similarity). Forms a
CC CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on
CC TYROBP (By similarity). {ECO:0000250|UniProtKB:Q9NY25,
CC ECO:0000250|UniProtKB:Q9R007, ECO:0000269|PubMed:11414735}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY25};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NY25}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GLF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GLF3-2; Sequence=VSP_012841;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in monocytes and
CC macrophages. {ECO:0000269|PubMed:11414735}.
CC -!- PTM: N-glycosylated. Contains sialic acid residues.
CC {ECO:0000250|UniProtKB:Q9R007}.
CC -!- MISCELLANEOUS: Acts as a key regulator of synovial injury and bone
CC erosion during autoimmune joint inflammation when its activation leads
CC to enhanced recruitment of inflammatory macrophages and neutrophils to
CC the joints. {ECO:0000250|UniProtKB:Q9R007}.
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DR EMBL; AF285449; AAG29427.1; -; mRNA.
DR EMBL; AF285450; AAG29428.1; -; mRNA.
DR RefSeq; NP_999155.1; NM_213990.1. [Q9GLF3-1]
DR RefSeq; XP_005657788.1; XM_005657731.2. [Q9GLF3-1]
DR AlphaFoldDB; Q9GLF3; -.
DR SMR; Q9GLF3; -.
DR STRING; 9823.ENSSSCP00000024397; -.
DR PaxDb; Q9GLF3; -.
DR Ensembl; ENSSSCT00000031347; ENSSSCP00000024397; ENSSSCG00000021933. [Q9GLF3-1]
DR Ensembl; ENSSSCT00035055257; ENSSSCP00035022223; ENSSSCG00035041588. [Q9GLF3-1]
DR Ensembl; ENSSSCT00070042942; ENSSSCP00070036128; ENSSSCG00070021595. [Q9GLF3-1]
DR GeneID; 397050; -.
DR KEGG; ssc:397050; -.
DR CTD; 23601; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00910000144330; -.
DR InParanoid; Q9GLF3; -.
DR OMA; WHWIDNS; -.
DR OrthoDB; 1548780at2759; -.
DR Reactome; R-SSC-2172127; DAP12 interactions.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Proteomes; UP000008227; Chromosome 18.
DR Proteomes; UP000314985; Chromosome 18.
DR ExpressionAtlas; Q9GLF3; baseline and differential.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; ISS:UniProtKB.
DR CDD; cd03593; CLECT_NK_receptors_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; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunity; Lectin; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="C-type lectin domain family 5 member A"
FT /id="PRO_0000046634"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 75..181
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 96..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 158..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 28..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11414735"
FT /id="VSP_012841"
SQ SEQUENCE 185 AA; 20835 MW; DA6EC0AF58BC95CE CRC64;
MNWHMIISGL IVVVLKIVGM TFFLLYFPQI FGEHNVSFSP TERPGTVPQI FGSSNVSFTP
TESFGTVCPT GWDFHQGRCF FLSTSENSWN NSMNFCKQKG STLAIVNTPE KLKFLQNISG
AEKYFIGLLY QPAEKMWRWI NNSVFNGSVI SHSHNFNCVT IGLTKTFDAA SCDVNYRSIC
EKSAQ
