FGL1_MESAU
ID FGL1_MESAU Reviewed; 314 AA.
AC P86239; A0A1U7Q3U4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Fibrinogen-like protein 1 {ECO:0000250|UniProtKB:Q08830};
DE Flags: Precursor;
GN Name=FGL1 {ECO:0000250|UniProtKB:Q08830};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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}.
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DR RefSeq; XP_005066704.1; XM_005066647.2.
DR AlphaFoldDB; P86239; -.
DR SMR; P86239; -.
DR STRING; 10036.XP_005066704.1; -.
DR Ensembl; ENSMAUT00000021626; ENSMAUP00000017672; ENSMAUG00000016483.
DR GeneID; 101840333; -.
DR CTD; 2267; -.
DR eggNOG; KOG2579; Eukaryota.
DR OrthoDB; 523014at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
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 1: Evidence at protein 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 /evidence="ECO:0000255"
FT /id="PRO_0000394415"
FT DOMAIN 76..308
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT COILED 25..59
FT /evidence="ECO:0000255"
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; 36887 MW; 6FDE27037ED7E1B8 CRC64;
MGEIRSFLLV TIALMMGREI WALENSKCLL EQERLRAQVQ QLETRVKQQQ ARIAQLMHEK
EVQLLDKGQE DNFFDLGGKR QYADCSEIYN DGFKQSGFYK IKPHQSQAIF SVYCDMSDGG
GWTVIQRRSD GRENFNRCWN DYENGFGNFV QNNGEYWLGN KNINLLTMQG DYTLKIDLTD
FEKNSRFAQY KHFKVGDKKS FYELNFGEYS GTAGDSLSGT YHPEMQWWAS HQRMKFSTRD
RDNDNYKGNC AEEEQSGWWF NRCHSANLNG VYYQGPYTAE TDNGVVWYTW HGWWYSLKSV
VMKIRPNDFI PNVI
