ID   FGL1_BOVIN              Reviewed;         312 AA.
AC   Q3SZZ7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Fibrinogen-like protein 1;
DE   Flags: Precursor;
GN   Name=FGL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q08830}.
CC       Note=Secreted in the blood plasma. {ECO:0000250|UniProtKB:Q08830}.
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; BC102634; AAI02635.1; -; mRNA.
DR   RefSeq; NP_001029485.1; NM_001034313.2.
DR   AlphaFoldDB; Q3SZZ7; -.
DR   SMR; Q3SZZ7; -.
DR   STRING; 9913.ENSBTAP00000021534; -.
DR   PaxDb; Q3SZZ7; -.
DR   PRIDE; Q3SZZ7; -.
DR   Ensembl; ENSBTAT00000021534; ENSBTAP00000021534; ENSBTAG00000016177.
DR   GeneID; 508090; -.
DR   KEGG; bta:508090; -.
DR   CTD; 2267; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016177; -.
DR   VGNC; VGNC:28992; FGL1.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000160647; -.
DR   HOGENOM; CLU_038628_1_3_1; -.
DR   InParanoid; Q3SZZ7; -.
DR   OMA; EQSGWWF; -.
DR   OrthoDB; 523014at2759; -.
DR   TreeFam; TF336658; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000016177; Expressed in liver and 106 other tissues.
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:0072574; P:hepatocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0050776; P:regulation of immune response; ISS:UniProtKB.
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..312
FT                   /note="Fibrinogen-like protein 1"
FT                   /id="PRO_0000273190"
FT   DOMAIN          74..306
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   COILED          39..60
FT                   /evidence="ECO:0000255"
FT   DISULFID        26
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        83..112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        248..261
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ   SEQUENCE   312 AA;  36139 MW;  39315DFD15A793AD CRC64;
     MAKMFSFILV TTALVMGRGS SALENCLQEQ ARLRAQVYLL ETRVKQQQVK ISQLLHEKQV
     QLLDKGEENS VIDLGGKRQY ADCSEIFNDG YKQSGFYKIK PLQSPAEFSV YCDMSDGGGW
     TVIQRRSDGS ENFNRDWSDY ENGFGNFVQK NGEYWLGNRN LHLLTTQGDY TLKIDLADFE
     KNSRYAQYKN FKVGDEKNSY DLHIGEYSGT AGDSLTGNFH PEVQWWASHQ RMKFSTWDRD
     NDNYEGNCAK EDQSGWWFNR CHSANLNGFY HKGPYTAKTD NGIVWHTWHG WWYSLKSVVM
     KIRPNDFIPN IV