ID   FGL1_RAT                Reviewed;         314 AA.
AC   Q5M8C6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Fibrinogen-like protein 1 {ECO:0000303|PubMed:18039467};
DE   Flags: Precursor;
GN   Name=Fgl1 {ECO:0000303|PubMed:18039467, ECO:0000312|RGD:620169};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
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   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18039467; DOI=10.1016/j.bbrc.2007.11.069;
RA   Liu Z., Ukomadu C.;
RT   "Fibrinogen-like protein 1, a hepatocyte derived protein is an acute phase
RT   reactant.";
RL   Biochem. Biophys. Res. Commun. 365:729-734(2008).
CC   -!- FUNCTION: Immune suppressive molecule that inhibits antigen-specific T-
CC       cell activation by acting as a major ligand of LAG3. Responsible for
CC       LAG3 T-cell inhibitory function. Binds LAG3 independently from MHC
CC       class II (MHC-II). Secreted by, and promotes growth of, hepatocytes.
CC       {ECO:0000250|UniProtKB:Q08830}.
CC   -!- SUBUNIT: Homodimer. Interacts (via the Fibrinogen C-terminal domain)
CC       with LAG3 (via Ig-like domains 1 and 2).
CC       {ECO:0000250|UniProtKB:Q08830}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18039467}.
CC       Note=Secreted in the blood plasma. {ECO:0000269|PubMed:18039467}.
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DR   EMBL; BC088107; AAH88107.1; -; mRNA.
DR   RefSeq; NP_742007.1; NM_172010.1.
DR   AlphaFoldDB; Q5M8C6; -.
DR   SMR; Q5M8C6; -.
DR   STRING; 10116.ENSRNOP00000014248; -.
DR   PaxDb; Q5M8C6; -.
DR   Ensembl; ENSRNOT00000014248; ENSRNOP00000014248; ENSRNOG00000010714.
DR   GeneID; 246186; -.
DR   KEGG; rno:246186; -.
DR   CTD; 2267; -.
DR   RGD; 620169; Fgl1.
DR   eggNOG; KOG2579; Eukaryota.
DR   InParanoid; Q5M8C6; -.
DR   OMA; EQSGWWF; -.
DR   PhylomeDB; Q5M8C6; -.
DR   PRO; PR:Q5M8C6; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000010714; Expressed in liver and 12 other tissues.
DR   ExpressionAtlas; Q5M8C6; baseline and differential.
DR   Genevisible; Q5M8C6; RN.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0060612; P:adipose tissue development; ISO:RGD.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR   GO; GO:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR   GO; GO:0050776; P:regulation of immune response; ISS:UniProtKB.
DR   GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 1.
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   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   2: Evidence at transcript level;
KW   Adaptive immunity; Coiled coil; Disulfide bond; Immunity;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250|UniProtKB:Q08830"
FT   CHAIN           23..314
FT                   /note="Fibrinogen-like protein 1"
FT                   /id="PRO_0000322980"
FT   DOMAIN          76..308
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   COILED          28..62
FT                   /evidence="ECO:0000255"
FT   DISULFID        28
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        85..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        250..263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   314 AA;  36476 MW;  FD1E8A7EA4941B04 CRC64;
     MGEIRSFVLI TVALILGKES WVLGDENCLQ EQVRLRAQVR QLETRVKQQQ VVIAQLLHEK
     EVQFLDRGQE DSFIDLGGKR HYADCSEIYN DGFKHSGFYK IKPLQSLAEF SVYCDMSDGG
     GWTVIQRRSD GSENFNRGWN DYENGFGNFV QSNGEYWLGN KNINLLTMQG DYTLKIDLTD
     FEKNSRFAQY EKFKVGDEKS FYELNIGEYS GTAGDSLSGT FHPEVQWWAS HQTMKFSTRD
     RDNDNYNGNC AEEEQSGWWF NRCHSANLNG VYYQGPYRAE TDNGVVWYTW RGWWYSLKSV
     VMKIRPSDFI PNIV