FGL2_MOUSE
ID FGL2_MOUSE Reviewed; 432 AA.
AC P12804;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Fibroleukin;
DE AltName: Full=Cytotoxic T-lymphocyte-specific protein;
DE AltName: Full=Fibrinogen-like protein 2;
DE AltName: Full=Prothrombinase;
DE Flags: Precursor;
GN Name=Fgl2; Synonyms=Fiblp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Cytotoxic T-cell;
RX PubMed=3550794; DOI=10.1073/pnas.84.6.1609;
RA Koyama T., Hall L.R., Haser W.G., Tonegawa S., Saito H.;
RT "Structure of a cytotoxic T-lymphocyte-specific gene shows a strong
RT homology to fibrinogen beta and gamma chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1609-1613(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=BALB/cJ; TISSUE=Peritoneal macrophage;
RX PubMed=7609073; DOI=10.1128/jvi.69.8.5033-5038.1995;
RA Parr R.L., Fung L., Reneker J., Myers-Mason N., Leibowitz J.L., Levy G.;
RT "Association of mouse fibrinogen-like protein with murine hepatitis virus-
RT induced prothrombinase activity.";
RL J. Virol. 69:5033-5038(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 INDUCTION BY MHV-3 NUCLEOCAPSID PROTEIN.
RX PubMed=10187767; DOI=10.1074/jbc.274.15.9930;
RA Ning Q., Liu M., Kongkham P., Lai M.M.C., Marsden P.A., Tseng J.,
RA Pereira B., Belyavskyi M., Leibowitz J., Phillips M.J., Levy G.A.;
RT "The nucleocapsid protein of murine hepatitis virus type 3 induces
RT transcription of the novel fgl2 prothrombinase gene.";
RL J. Biol. Chem. 274:9930-9936(1999).
CC -!- FUNCTION: Converts prothrombin to thrombin.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in cytotoxic T-cells.
CC -!- INDUCTION: In macrophages, during infection by mouse hepatitis virus
CC strain 3 (MHV-3). {ECO:0000269|PubMed:10187767}.
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DR EMBL; M16238; AAA37624.1; -; Genomic_DNA.
DR EMBL; M15761; AAA37624.1; JOINED; Genomic_DNA.
DR EMBL; S78773; AAB34823.1; -; mRNA.
DR EMBL; BC028893; AAH28893.1; -; mRNA.
DR CCDS; CCDS19103.1; -.
DR PIR; A27447; A27447.
DR PIR; I56934; I56934.
DR RefSeq; NP_032039.2; NM_008013.4.
DR AlphaFoldDB; P12804; -.
DR SMR; P12804; -.
DR STRING; 10090.ENSMUSP00000046131; -.
DR GlyGen; P12804; 5 sites.
DR PhosphoSitePlus; P12804; -.
DR EPD; P12804; -.
DR PaxDb; P12804; -.
DR PeptideAtlas; P12804; -.
DR PRIDE; P12804; -.
DR ProteomicsDB; 271587; -.
DR Antibodypedia; 15028; 392 antibodies from 31 providers.
DR DNASU; 14190; -.
DR Ensembl; ENSMUST00000035799; ENSMUSP00000046131; ENSMUSG00000039899.
DR GeneID; 14190; -.
DR KEGG; mmu:14190; -.
DR UCSC; uc008wom.2; mouse.
DR CTD; 10875; -.
DR MGI; MGI:103266; Fgl2.
DR VEuPathDB; HostDB:ENSMUSG00000039899; -.
DR eggNOG; KOG2579; Eukaryota.
DR GeneTree; ENSGT00940000157946; -.
DR HOGENOM; CLU_038628_3_0_1; -.
DR InParanoid; P12804; -.
DR OMA; TNFNRTW; -.
DR OrthoDB; 357340at2759; -.
DR PhylomeDB; P12804; -.
DR TreeFam; TF336658; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14190; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Fgl2; mouse.
DR PRO; PR:P12804; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P12804; protein.
DR Bgee; ENSMUSG00000039899; Expressed in ascending aorta and 175 other tissues.
DR ExpressionAtlas; P12804; baseline and differential.
DR Genevisible; P12804; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:MGI.
DR GO; GO:0002605; P:negative regulation of dendritic cell antigen processing and presentation; IMP:MGI.
DR GO; GO:0002617; P:negative regulation of macrophage antigen processing and presentation; IMP:MGI.
DR GO; GO:0043381; P:negative regulation of memory T cell differentiation; IMP:MGI.
DR GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:MGI.
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; Cytolysis; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..432
FT /note="Fibroleukin"
FT /id="PRO_0000009107"
FT DOMAIN 197..429
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 100..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..157
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 206..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 364..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT CONFLICT 332
FT /note="A -> G (in Ref. 2; AAB34823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 48951 MW; 2B297F69CCB4A782 CRC64;
MRLPGWLWLS SAVLAACRAV EEHNLTEGLE DASAQAACPA RLEGSGRCEG SQCPFQLTLP
TLTIQLPRQL GSMEEVLKEV RTLKEAVDSL KKSCQDCKLQ ADDHRDPGGN GGNGAETAED
SRVQELESQV NKLSSELKNA KDQIQGLQGR LETLHLVNMN NIENYVDNKV ANLTVVVNSL
DGKCSKCPSQ EHMQSQPVQH LIYKDCSDHY VLGRRSSGAY RVTPDHRNSS FEVYCDMETM
GGGWTVLQAR LDGSTNFTRE WKDYKAGFGN LEREFWLGND KIHLLTKSKE MILRIDLEDF
NGLTLYALYD QFYVANEFLK YRLHIGNYNG TAGDALRFSR HYNHDLRFFT TPDRDNDRYP
SGNCGLYYSS GWWFDSCLSA NLNGKYYHQK YKGVRNGIFW GTWPGINQAQ PGGYKSSFKQ
AKMMIRPKNF KP
