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   27-MAR-2024, entry version 145.
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";
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; 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; 46.
DR   IntAct; Q6UXB4; 27.
DR   STRING; 9606.ENSP00000327599; -.
DR   GlyCosmos; Q6UXB4; 2 sites, No reported glycans.
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; 9606-ENSP00000327599; -.
DR   PeptideAtlas; Q6UXB4; -.
DR   ProteomicsDB; 67585; -.
DR   Antibodypedia; 2674; 113 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   AGR; HGNC:24591; -.
DR   CTD; 339390; -.
DR   DisGeNET; 339390; -.
DR   GeneCards; CLEC4G; -.
DR   HGNC; HGNC:24591; CLEC4G.
DR   HPA; ENSG00000182566; Tissue enhanced (brain, liver).
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; 5320795at2759; -.
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 1138 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 92 other cell types or tissues.
DR   ExpressionAtlas; Q6UXB4; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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:0006955; P:immune response; IBA:GO_Central.
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; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22802:SF245; C-TYPE LECTIN DOMAIN FAMILY 4 MEMBER G; 1.
DR   PANTHER; PTHR22802; C-TYPE LECTIN SUPERFAMILY MEMBER; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   Genevisible; Q6UXB4; HS.
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
//