CLC4G_HUMAN
ID CLC4G_HUMAN Reviewed; 293 AA.
AC Q6UXB4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=C-type lectin domain family 4 member G;
DE AltName: Full=Liver and lymph node sinusoidal endothelial cell C-type lectin {ECO:0000303|PubMed:14711836};
DE Short=LSECtin {ECO:0000303|PubMed:14711836};
GN Name=CLEC4G; ORFNames=UNQ431/PRO792;
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=Fetal liver;
RX PubMed=14711836; DOI=10.1074/jbc.m311227200;
RA Liu W., Tang L., Zhang G., Wei H., Cui Y., Guo L., Gou Z., Chen X.,
RA Jiang D., Zhu Y., Kang G., He F.;
RT "Characterization of a novel C-type lectin-like gene, LSECtin:
RT demonstration of carbohydrate binding and expression in sinusoidal
RT endothelial cells of liver and lymph node.";
RL J. Biol. Chem. 279:18748-18758(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
RN [4]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBOLAVIRUS
RP GLYCOPROTEIN AND SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=16051304; DOI=10.1016/j.virol.2005.06.026;
RA Gramberg T., Hofmann H., Moeller P., Lalor P.F., Marzi A., Geier M.,
RA Krumbiegel M., Winkler T., Kirchhoff F., Adams D.H., Becker S., Muench J.,
RA Poehlmann S.;
RT "LSECtin interacts with filovirus glycoproteins and the spike protein of
RT SARS coronavirus.";
RL Virology 340:224-236(2005).
RN [5]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS
RP GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=22156524; DOI=10.1128/jvi.06451-11;
RA Shimojima M., Stroher U., Ebihara H., Feldmann H., Kawaoka Y.;
RT "Identification of cell surface molecules involved in dystroglycan-
RT independent Lassa virus cell entry.";
RL J. Virol. 86:2067-2078(2012).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LYMPHOCYTIC
RP CHORIOMENINGITIS VIRUS GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=22673088; DOI=10.1292/jvms.12-0176;
RA Shimojima M., Kawaoka Y.;
RT "Cell surface molecules involved in infection mediated by lymphocytic
RT choriomeningitis virus glycoprotein.";
RL J. Vet. Med. Sci. 74:1363-1366(2012).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH JAPANESE ENCEPHALITIS
RP VIRUS ENVELOPE PROTEIN E (MICROBIAL INFECTION).
RX PubMed=24623090; DOI=10.1007/s00705-014-2042-2;
RA Shimojima M., Takenouchi A., Shimoda H., Kimura N., Maeda K.;
RT "Distinct usage of three C-type lectins by Japanese encephalitis virus: DC-
RT SIGN, DC-SIGNR, and LSECtin.";
RL Arch. Virol. 159:2023-2031(2014).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Binds mannose, N-acetylglucosamine (GlcNAc) and fucose, but
CC not galactose, in a Ca(2+)-dependent manner, in vitro.
CC {ECO:0000269|PubMed:14711836}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Japanese
CC encephalitis virus. {ECO:0000269|PubMed:24623090}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Ebolavirus.
CC {ECO:0000269|PubMed:16051304}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for SARS-CoV.
CC {ECO:0000269|PubMed:16051304}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Lassa virus and
CC Lymphocytic choriomeningitis virus glycoprotein (PubMed:22156524,
CC PubMed:22673088). {ECO:0000269|PubMed:22156524,
CC ECO:0000269|PubMed:22673088}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Japanese encephalitis
CC virus envelope protein E. {ECO:0000269|PubMed:24623090}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus glycoprotein.
CC {ECO:0000269|PubMed:16051304}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV spike
CC glycoprotein. {ECO:0000269|PubMed:16051304}.
CC -!- SUBUNIT: (Microbial infection) Interacts with lassa virus and
CC Lymphocytic choriomeningitis virus glycoprotein (PubMed:22156524,
CC PubMed:22673088). {ECO:0000269|PubMed:22156524,
CC ECO:0000269|PubMed:22673088}.
CC -!- INTERACTION:
CC Q6UXB4; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-2114729, EBI-11343438;
CC Q6UXB4; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-2114729, EBI-18013275;
CC Q6UXB4; O00559: EBAG9; NbExp=3; IntAct=EBI-2114729, EBI-8787095;
CC Q6UXB4; Q13347: EIF3I; NbExp=3; IntAct=EBI-2114729, EBI-354047;
CC Q6UXB4; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2114729, EBI-18304435;
CC Q6UXB4; P80217: IFI35; NbExp=4; IntAct=EBI-2114729, EBI-2115067;
CC Q6UXB4; Q9HCJ2: LRRC4C; NbExp=3; IntAct=EBI-2114729, EBI-3925442;
CC Q6UXB4; P54829: PTPN5; NbExp=3; IntAct=EBI-2114729, EBI-1220572;
CC Q6UXB4; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-2114729, EBI-17640454;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein {ECO:0000269|PubMed:14711836}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in fetal and adult liver and
CC in lymph nodes. Specifically expressed by endothelial cells lining
CC lymph node and liver sinuses (at protein level).
CC {ECO:0000269|PubMed:14711836}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=LSECtin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_416";
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DR EMBL; AY358431; AAQ88797.1; -; mRNA.
DR EMBL; BC093691; AAH93691.1; -; mRNA.
DR EMBL; BC093693; AAH93693.1; -; mRNA.
DR CCDS; CCDS12185.1; -.
DR RefSeq; NP_940894.1; NM_198492.3.
DR AlphaFoldDB; Q6UXB4; -.
DR SMR; Q6UXB4; -.
DR BioGRID; 130876; 45.
DR IntAct; Q6UXB4; 27.
DR STRING; 9606.ENSP00000327599; -.
DR GlyGen; Q6UXB4; 2 sites.
DR iPTMnet; Q6UXB4; -.
DR PhosphoSitePlus; Q6UXB4; -.
DR BioMuta; CLEC4G; -.
DR DMDM; 74738199; -.
DR jPOST; Q6UXB4; -.
DR MassIVE; Q6UXB4; -.
DR PaxDb; Q6UXB4; -.
DR PeptideAtlas; Q6UXB4; -.
DR PRIDE; Q6UXB4; -.
DR ProteomicsDB; 67585; -.
DR Antibodypedia; 2674; 101 antibodies from 23 providers.
DR DNASU; 339390; -.
DR Ensembl; ENST00000328853.11; ENSP00000327599.4; ENSG00000182566.15.
DR GeneID; 339390; -.
DR KEGG; hsa:339390; -.
DR MANE-Select; ENST00000328853.11; ENSP00000327599.4; NM_198492.4; NP_940894.1.
DR UCSC; uc002mhp.4; human.
DR CTD; 339390; -.
DR DisGeNET; 339390; -.
DR GeneCards; CLEC4G; -.
DR HGNC; HGNC:24591; CLEC4G.
DR HPA; ENSG00000182566; Tissue enhanced (adipose tissue, liver, lymphoid tissue).
DR MIM; 616256; gene.
DR neXtProt; NX_Q6UXB4; -.
DR OpenTargets; ENSG00000182566; -.
DR PharmGKB; PA142672104; -.
DR VEuPathDB; HostDB:ENSG00000182566; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161836; -.
DR HOGENOM; CLU_049894_7_2_1; -.
DR InParanoid; Q6UXB4; -.
DR OMA; GQEDCVM; -.
DR OrthoDB; 1442007at2759; -.
DR PhylomeDB; Q6UXB4; -.
DR TreeFam; TF333341; -.
DR PathwayCommons; Q6UXB4; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q6UXB4; -.
DR BioGRID-ORCS; 339390; 9 hits in 1060 CRISPR screens.
DR GenomeRNAi; 339390; -.
DR Pharos; Q6UXB4; Tbio.
DR PRO; PR:Q6UXB4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6UXB4; protein.
DR Bgee; ENSG00000182566; Expressed in right lobe of liver and 91 other tissues.
DR ExpressionAtlas; Q6UXB4; baseline and differential.
DR Genevisible; Q6UXB4; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0097367; F:carbohydrate derivative binding; IDA:FlyBase.
DR GO; GO:0070061; F:fructose binding; IDA:FlyBase.
DR GO; GO:0140081; F:glycosylated region protein binding; ISS:FlyBase.
DR GO; GO:0005537; F:mannose binding; IDA:FlyBase.
DR GO; GO:0030247; F:polysaccharide binding; IEA:Ensembl.
DR GO; GO:0120274; F:virus coreceptor activity; IGI:FlyBase.
DR GO; GO:0001618; F:virus receptor activity; IDA:FlyBase.
DR GO; GO:0046633; P:alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0046642; P:negative regulation of alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IEA:Ensembl.
DR GO; GO:0002710; P:negative regulation of T cell mediated immunity; IEA:Ensembl.
DR GO; GO:1903902; P:positive regulation of viral life cycle; IMP:FlyBase.
DR GO; GO:0002456; P:T cell mediated immunity; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IDA:FlyBase.
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; 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 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..293
FT /note="C-type lectin domain family 4 member G"
FT /id="PRO_0000223691"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 172..287
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT COILED 96..136
FT /evidence="ECO:0000255"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 264..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 293 AA; 32562 MW; 7AEA4ED8654CE577 CRC64;
MDTTRYSKWG GSSEEVPGGP WGRWVHWSRR PLFLALAVLV TTVLWAVILS ILLSKASTER
AALLDGHDLL RTNASKQTAA LGALKEEVGD CHSCCSGTQA QLQTTRAELG EAQAKLMEQE
SALRELRERV TQGLAEAGRG REDVRTELFR ALEAVRLQNN SCEPCPTSWL SFEGSCYFFS
VPKTTWAAAQ DHCADASAHL VIVGGLDEQG FLTRNTRGRG YWLGLRAVRH LGKVQGYQWV
DGVSLSFSHW NQGEPNDAWG RENCVMMLHT GLWNDAPCDS EKDGWICEKR HNC
