FGL2_HUMAN
ID FGL2_HUMAN Reviewed; 439 AA.
AC Q14314;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Fibroleukin;
DE AltName: Full=Fibrinogen-like protein 2;
DE AltName: Full=pT49;
DE Flags: Precursor;
GN Name=FGL2;
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].
RC TISSUE=Small intestine;
RX PubMed=7642106; DOI=10.1016/0378-1119(95)00240-7;
RA Ruegg C., Pytela R.;
RT "Sequence of a human transcript expressed in T-lymphocytes and encoding a
RT fibrinogen-like protein.";
RL Gene 160:257-262(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yuwaraj S., Liu M., Marsden P., Levy G.;
RT "Cloning and characterization of Hfgl2: the human counterpart to the mouse
RT gene Fgl2.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-53.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Pancreas;
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 [5]
RP CHARACTERIZATION.
RX PubMed=9647217;
RA Marazzi S., Blum S., Hartmann R., Gundersen D., Schreyer M., Argraves S.,
RA von Fliedner V., Pytela R., Ruegg C.;
RT "Characterization of human fibroleukin, a fibrinogen-like protein secreted
RT by T lymphocytes.";
RL J. Immunol. 161:138-147(1998).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179 AND ASN-336.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-179 AND ASN-336.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: May play a role in physiologic lymphocyte functions at
CC mucosal sites.
CC -!- SUBUNIT: Homotetramer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in cytotoxic T-cells.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/fgl2/";
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DR EMBL; Z36531; CAA85298.1; -; mRNA.
DR EMBL; AF104015; AAD10825.1; -; Genomic_DNA.
DR EMBL; AF104014; AAD10825.1; JOINED; Genomic_DNA.
DR EMBL; AF468959; AAL68855.1; -; Genomic_DNA.
DR EMBL; BC033820; AAH33820.1; -; mRNA.
DR EMBL; BC073986; AAH73986.1; -; mRNA.
DR CCDS; CCDS5591.1; -.
DR PIR; I37391; I37391.
DR RefSeq; NP_006673.1; NM_006682.2.
DR AlphaFoldDB; Q14314; -.
DR SMR; Q14314; -.
DR BioGRID; 116083; 14.
DR IntAct; Q14314; 12.
DR STRING; 9606.ENSP00000248598; -.
DR GlyConnect; 1241; 18 N-Linked glycans (3 sites).
DR GlyGen; Q14314; 7 sites, 17 N-linked glycans (3 sites), 3 O-linked glycans (2 sites).
DR iPTMnet; Q14314; -.
DR PhosphoSitePlus; Q14314; -.
DR BioMuta; FGL2; -.
DR DMDM; 12230074; -.
DR REPRODUCTION-2DPAGE; Q14314; -.
DR CPTAC; CPTAC-2213; -.
DR CPTAC; CPTAC-2214; -.
DR EPD; Q14314; -.
DR jPOST; Q14314; -.
DR MassIVE; Q14314; -.
DR PaxDb; Q14314; -.
DR PeptideAtlas; Q14314; -.
DR PRIDE; Q14314; -.
DR ProteomicsDB; 59959; -.
DR Antibodypedia; 15028; 392 antibodies from 31 providers.
DR DNASU; 10875; -.
DR Ensembl; ENST00000248598.6; ENSP00000248598.5; ENSG00000127951.8.
DR GeneID; 10875; -.
DR KEGG; hsa:10875; -.
DR MANE-Select; ENST00000248598.6; ENSP00000248598.5; NM_006682.3; NP_006673.1.
DR UCSC; uc003ugb.4; human.
DR CTD; 10875; -.
DR DisGeNET; 10875; -.
DR GeneCards; FGL2; -.
DR HGNC; HGNC:3696; FGL2.
DR HPA; ENSG00000127951; Tissue enhanced (lymphoid).
DR MIM; 605351; gene.
DR neXtProt; NX_Q14314; -.
DR OpenTargets; ENSG00000127951; -.
DR PharmGKB; PA28134; -.
DR VEuPathDB; HostDB:ENSG00000127951; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157946; -.
DR HOGENOM; CLU_038628_3_0_1; -.
DR InParanoid; Q14314; -.
DR OMA; TNFNRTW; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; Q14314; -.
DR TreeFam; TF336658; -.
DR PathwayCommons; Q14314; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q14314; -.
DR BioGRID-ORCS; 10875; 6 hits in 1062 CRISPR screens.
DR ChiTaRS; FGL2; human.
DR GeneWiki; FGL2; -.
DR GenomeRNAi; 10875; -.
DR Pharos; Q14314; Tbio.
DR PRO; PR:Q14314; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14314; protein.
DR Bgee; ENSG00000127951; Expressed in monocyte and 196 other tissues.
DR ExpressionAtlas; Q14314; baseline and differential.
DR Genevisible; Q14314; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005577; C:fibrinogen complex; TAS:ProtInc.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0002617; P:negative regulation of macrophage antigen processing and presentation; IEA:Ensembl.
DR GO; GO:0043381; P:negative regulation of memory T cell differentiation; IEA:Ensembl.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR033083; Fgl2.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF189; PTHR19143:SF189; 2.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..439
FT /note="Fibroleukin"
FT /id="PRO_0000009106"
FT DOMAIN 204..436
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..165
FT /evidence="ECO:0000255"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 213..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 371..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT VARIANT 53
FT /note="G -> E (in dbSNP:rs2075761)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013066"
SQ SEQUENCE 439 AA; 50229 MW; DF34656288E49E68 CRC64;
MKLANWYWLS SAVLATYGFL VVANNETEEI KDERAKDVCP VRLESRGKCE EAGECPYQVS
LPPLTIQLPK QFSRIEEVFK EVQNLKEIVN SLKKSCQDCK LQADDNGDPG RNGLLLPSTG
APGEVGDNRV RELESEVNKL SSELKNAKEE INVLHGRLEK LNLVNMNNIE NYVDSKVANL
TFVVNSLDGK CSKCPSQEQI QSRPVQHLIY KDCSDYYAIG KRSSETYRVT PDPKNSSFEV
YCDMETMGGG WTVLQARLDG STNFTRTWQD YKAGFGNLRR EFWLGNDKIH LLTKSKEMIL
RIDLEDFNGV ELYALYDQFY VANEFLKYRL HVGNYNGTAG DALRFNKHYN HDLKFFTTPD
KDNDRYPSGN CGLYYSSGWW FDACLSANLN GKYYHQKYRG VRNGIFWGTW PGVSEAHPGG
YKSSFKEAKM MIRPKHFKP
