ID A0A452RFM3_URSAM Unreviewed; 437 AA.
AC A0A452RFM3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Fibrinogen gamma chain {ECO:0000313|Ensembl:ENSUAMP00000017574.1};
GN Name=FGG {ECO:0000313|Ensembl:ENSUAMP00000017574.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000017574.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000017574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-
CC identical chains (alpha, beta and gamma). The 2 heterotrimers are in
CC head to head conformation with the N-termini in a small central domain.
CC {ECO:0000256|ARBA:ARBA00025974}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; A0A452RFM3; -.
DR STRING; 9643.ENSUAMP00000017574; -.
DR Ensembl; ENSUAMT00000019668.1; ENSUAMP00000017574.1; ENSUAMG00000013939.1.
DR GeneTree; ENSGT00940000158467; -.
DR OMA; TYHNGMR; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl.
DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 1.20.5.50; -; 2.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 4.10.530.10; Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2; 1.
DR InterPro; IPR037579; Fibrinogen.
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; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1.
DR PANTHER; PTHR47221:SF4; FIBRINOGEN GAMMA CHAIN; 1.
DR Pfam; PF08702; Fib_alpha; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SMART; SM01212; Fib_alpha; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF58010; Fibrinogen coiled-coil and central regions; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 4: Predicted;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019396053"
FT DOMAIN 170..416
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT COILED 133..160
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 437 AA; 49484 MW; B0A2B20614830C7E CRC64;
MTWSLNRQGL ILYLYALSLL PSTCLAYVAT RDNCCILDER FGSYCPTTCG IADFLSTYQT
GVDNDLRSLE DLFRRIENKT AEAKEVIKSI QVTYNPSEPP KPNRIVSATK DSKKMMEEII
KYEALVGSHE SNIRFLQEIY NSNNQKINNL KQKVAQLEAK CQEPCRDTVQ IHDITGKDCQ
DIANKGAKES GLYFLKPLKA KQQFLVYCEI DGTGNGWTVL QKRLDGSLDF KKNWIQYKEG
FGHLSPTGNT EFWLGNEKIH LISTQSAIPY ALRIQLEDWN GRTSTADYAM FKVGPEADKY
RLTYAYFIGG DAGDAFDGYD FGDDPSDKFF TSHNGMQFST WDNDNDKYEG NCAEQDGSGW
WMNKCHAGHL NGVYYQGGTY SKTSTPNGYD NGIIWATWQS RWYSMKKTTM KIIPFNRLAI
GEGQQHHLGG AKQAGDI
//
