ID A0A2K5EC93_AOTNA Unreviewed; 488 AA.
AC A0A2K5EC93;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Fibrinogen beta chain {ECO:0000313|Ensembl:ENSANAP00000030837.1};
GN Name=FGB {ECO:0000313|Ensembl:ENSANAP00000030837.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000030837.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000030837.1}
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 RefSeq; XP_012303939.1; XM_012448516.1.
DR AlphaFoldDB; A0A2K5EC93; -.
DR STRING; 37293.ENSANAP00000030837; -.
DR Ensembl; ENSANAT00000048877.1; ENSANAP00000030837.1; ENSANAG00000033162.1.
DR GeneID; 105714552; -.
DR CTD; 2244; -.
DR GeneTree; ENSGT00940000158122; -.
DR OMA; CIHADPD; -.
DR OrthoDB; 3134470at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone 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:0043152; P:induction of bacterial agglutination; 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: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 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 NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR47221; FIBRINOGEN ALPHA CHAIN; 1.
DR PANTHER; PTHR47221:SF2; FIBRINOGEN BETA 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:UP000233020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..488
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014373690"
FT DOMAIN 229..485
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT REGION 36..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 192..219
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 41..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 55314 MW; CAB501A7067A7EAB CRC64;
MVSWSFHKFK TMKHLLLLLL CVVLVKSQGG NDNTEGIFGA RGHRPLDKKR EEAPSLRPAP
PPISGGGYRA RPAKADQSQK KVERKAPDAG GCIHADPDLG VLCPTGCHLQ DALLQQEKPI
RNSVDELSNN VEAVSQTSSS TFQYMYLLKD MWQKRQKQVK DNENVVNEYS LELEKHHLYI
DETVNSNIPT NLRVLRSILE NLRSKIQKLE SDVSAQMEYC RTPCTVSCNI PVVSGKECEE
IIRKGGETSE MYLIQPDSSV KPYRVYCDMN TEGGGWTVIQ NRQDGSVDFG RKWDPYKQGF
GNIATNTDGK NYCGLPGEYW LGNDKISQLT KMGSTELLIE MEDWKGDKVK AEYGGFTIQN
EANKYQMSVN KYKGTAGNAL MDGASQLVGE NRTMTIHNGM FFSTYDRDND GWVTTDPRKQ
CSKEDGGGWW YNRCHAANPN GRYYWGGKYT WDMAKHGTDD GVVWMNWKGS WYSMKKMSMK
IRPFFPKQ
//
