ID   FGL2_BOVIN              Reviewed;         441 AA.
AC   Q29RY7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Fibroleukin;
DE   AltName: Full=Fibrinogen-like protein 2;
DE   Flags: Precursor;
GN   Name=FGL2;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in physiologic lymphocyte functions at
CC       mucosal sites. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; BC113335; AAI13336.1; -; mRNA.
DR   RefSeq; NP_001039562.1; NM_001046097.1.
DR   AlphaFoldDB; Q29RY7; -.
DR   SMR; Q29RY7; -.
DR   STRING; 9913.ENSBTAP00000012815; -.
DR   PaxDb; Q29RY7; -.
DR   PRIDE; Q29RY7; -.
DR   Ensembl; ENSBTAT00000012815; ENSBTAP00000012815; ENSBTAG00000009717.
DR   GeneID; 511711; -.
DR   KEGG; bta:511711; -.
DR   CTD; 10875; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009717; -.
DR   VGNC; VGNC:28993; FGL2.
DR   eggNOG; KOG2579; Eukaryota.
DR   GeneTree; ENSGT00940000157946; -.
DR   HOGENOM; CLU_038628_3_0_1; -.
DR   InParanoid; Q29RY7; -.
DR   OMA; TNFNRTW; -.
DR   OrthoDB; 357340at2759; -.
DR   TreeFam; TF336658; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 4.
DR   Bgee; ENSBTAG00000009717; Expressed in neutrophil and 104 other tissues.
DR   GO; GO:0009986; C:cell surface; ISS:AgBase.
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:0016504; F:peptidase activator activity; ISS:AgBase.
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   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..441
FT                   /note="Fibroleukin"
FT                   /id="PRO_0000244381"
FT   DOMAIN          206..438
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          102..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          73..167
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:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   441 AA;  50684 MW;  6EBAD6EDE116B8AD CRC64;
     MKLANWCWLS STVLATYGFL VVANNETEEI KDEAAQNACR VRLESRGRCE EEGECPYQVN
     LPPLTIQLPK QFSRIEEVFK EVQNLKEIVN SLKKTCQDCK LQADDSRDPG RNGLLLPGTG
     APGETGDNRV RELEGEVNKL SSDLKNAKEE IDVLQGRLEK LNLVNMNNIE QYVDSKVANL
     TFVVNSLDGK CSSKCPRQEQ IQSLPVQQHL IYKDCSEYYT IGKRSSELYR VTPEPRNSSF
     EVFCDMETMA GGWTVLQARV DGSTNFTRTW QDYKVGFGNL RREFWLGNDK IHLLTKSKDM
     ILRIDLEDFN GIKLYALYDH FYVANEFLKY RLHIGNYNGT AGDALRFSKH YNHDLKFFTT
     PDRDNDRYPS GNCGLYYSSG WWFDACLSAN LNGKYYHQKY RGVRNGIFWG TWPGISEAQP
     GGYKSSFKEV KMMIRPKHFK P