CLCL1_HUMAN
ID CLCL1_HUMAN Reviewed; 167 AA.
AC Q8IZS7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=C-type lectin-like domain family 1;
DE AltName: Full=Dendritic cell-associated lectin 1;
DE Short=DC-associated lectin-1;
DE Short=DCAL-1;
GN Name=CLECL1; Synonyms=DCAL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=B-cell;
RX PubMed=12421943; DOI=10.4049/jimmunol.169.10.5638;
RA Ryan E.J., Marshall A.J., Magaletti D., Floyd H., Draves K.E., Olson N.E.,
RA Clark E.A.;
RT "Dendritic cell-associated lectin-1: a novel dendritic cell-associated, C-
RT type lectin-like molecule enhances T cell secretion of IL-4.";
RL J. Immunol. 169:5638-5648(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May function in mediating immune cell-cell interactions. May
CC act as a T-cell costimulatory molecule, enhancing anti-CD3-induced
CC proliferation. May play a role in the interaction of dendritic cells
CC with T-cells and the cells of the adaptive immune response.
CC {ECO:0000269|PubMed:12421943}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12421943};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:12421943}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, and tonsil. Lower
CC expression in peripheral blood, bone marrow, and colon. No expression
CC detected in thymus. Highly expressed in dendritic and B-cells.
CC {ECO:0000269|PubMed:12421943}.
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DR EMBL; AF518873; AAN64752.1; -; mRNA.
DR EMBL; BC093857; AAH93857.1; -; mRNA.
DR EMBL; BC093859; AAH93859.1; -; mRNA.
DR RefSeq; NP_001240679.1; NM_001253750.1.
DR RefSeq; NP_001254630.1; NM_001267701.1.
DR RefSeq; NP_742001.1; NM_172004.3.
DR AlphaFoldDB; Q8IZS7; -.
DR SMR; Q8IZS7; -.
DR BioGRID; 127755; 1.
DR STRING; 9606.ENSP00000483624; -.
DR GlyGen; Q8IZS7; 3 sites.
DR iPTMnet; Q8IZS7; -.
DR PhosphoSitePlus; Q8IZS7; -.
DR BioMuta; CLECL1; -.
DR DMDM; 74728443; -.
DR PaxDb; Q8IZS7; -.
DR PeptideAtlas; Q8IZS7; -.
DR PRIDE; Q8IZS7; -.
DR Antibodypedia; 53007; 54 antibodies from 18 providers.
DR DNASU; 160365; -.
DR GeneID; 160365; -.
DR UCSC; uc001qwj.4; human.
DR CTD; 160365; -.
DR DisGeNET; 160365; -.
DR GeneCards; CLECL1; -.
DR HGNC; HGNC:24462; CLECL1.
DR HPA; ENSG00000184293; Group enriched (intestine, lymphoid tissue).
DR MIM; 607467; gene.
DR neXtProt; NX_Q8IZS7; -.
DR PharmGKB; PA162382341; -.
DR VEuPathDB; HostDB:ENSG00000184293; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_1660173_0_0_1; -.
DR InParanoid; Q8IZS7; -.
DR OrthoDB; 1178201at2759; -.
DR PhylomeDB; Q8IZS7; -.
DR TreeFam; TF342285; -.
DR PathwayCommons; Q8IZS7; -.
DR SignaLink; Q8IZS7; -.
DR BioGRID-ORCS; 160365; 17 hits in 1064 CRISPR screens.
DR GenomeRNAi; 160365; -.
DR Pharos; Q8IZS7; Tbio.
DR PRO; PR:Q8IZS7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IZS7; protein.
DR Bgee; ENSG00000184293; Expressed in tendon of biceps brachii and 153 other tissues.
DR ExpressionAtlas; Q8IZS7; baseline and differential.
DR Genevisible; Q8IZS7; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0097323; P:B cell adhesion; IDA:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Lectin; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..167
FT /note="C-type lectin-like domain family 1"
FT /id="PRO_0000317461"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 116..167
FT /note="C-type lectin; atypical"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 167 AA; 19115 MW; 581A6F08DB32A53C CRC64;
MVSNFFHVIQ VFEKSATLIS KTEHIGFVIY SWRKSTTHLG SRRKFAISIY LSEVSLQKYD
CPFSGTSFVV FSLFLICAMA GDVVYADIKT VRTSPLELAF PLQRSVSFNF STVHKSCPAK
DWKVHKGKCY WIAETKKSWN KSQNDCAINN SYLMVIQDIT AMVRFNI