FIBG_XENLA
ID FIBG_XENLA Reviewed; 438 AA.
AC P17634;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Fibrinogen gamma chain;
DE Flags: Precursor;
GN Name=fgg;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2334684; DOI=10.1021/bi00462a024;
RA Pastori R.L., Moskaitis J.E., Smith L.H. Jr., Schoenberg D.R.;
RT "Estrogen regulation of Xenopus laevis gamma-fibrinogen gene expression.";
RL Biochemistry 29:2599-2605(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-58.
RC TISSUE=Liver;
RX PubMed=2289632; DOI=10.1016/0303-7207(90)90145-x;
RA Bhattacharya A., Shepard A.R., Moser D.R., Holland L.J.;
RT "Isolation and characterization of cDNA clones for the gamma subunit of
RT Xenopus fibrinogen, the product of a coordinately regulated gene family.";
RL Mol. Cell. Endocrinol. 72:213-220(1990).
CC -!- FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta
CC (FGB), polymerizes to form an insoluble fibrin matrix. Has a major
CC function in hemostasis as one of the primary components of blood clots.
CC {ECO:0000250|UniProtKB:E9PV24}.
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 (By similarity). {ECO:0000250|UniProtKB:P02679}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02679}.
CC -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide chains
CC connects the central nodule to the C-terminal domains (distal nodules).
CC The long C-terminal ends of the alpha chains fold back, contributing a
CC fourth strand to the coiled coil structure.
CC {ECO:0000250|UniProtKB:P02679}.
CC -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which
CC cleaves fibrinopeptides A and B from alpha and beta chains, and thus
CC exposes the N-terminal polymerization sites responsible for the
CC formation of the soft clot. The soft clot is converted into the hard
CC clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine
CC cross-linking between gamma chains (stronger) and between alpha chains
CC (weaker) of different monomers.
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DR EMBL; J02894; AAA49709.1; -; mRNA.
DR EMBL; M35548; AAA03247.1; -; mRNA.
DR PIR; A32670; A32670.
DR AlphaFoldDB; P17634; -.
DR SMR; P17634; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
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; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR InterPro; IPR037581; Fibrinogen_gamma.
DR PANTHER; PTHR19143:SF338; PTHR19143:SF338; 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; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 2: Evidence at transcript level;
KW Blood coagulation; Calcium; Coiled coil; Disulfide bond; Glycoprotein;
KW Hemostasis; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT CHAIN 26..438
FT /note="Fibrinogen gamma chain"
FT /id="PRO_0000009103"
FT DOMAIN 167..414
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT BINDING 341
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04115"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32
FT /note="Interchain (with C-33)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 33
FT /note="Interchain (with C-32)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 43
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 47
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 158
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 162
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 176..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 349..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
SQ SEQUENCE 438 AA; 50064 MW; 69B1F01BB6716F60 CRC64;
MTRLPKQGLL LLQSLALLSS AFGNIIPNTD NCCILDGRFG EYCPTTCGIS DFLNRYQENV
DTDLQYLENL LTQISNSTSG TTIIVEHLID SGKKPATSPQ TAIDPMTQKS KTCWMKLTDM
KNYYQYEENI LYLQEVYSSN QNKIFLLKQK IANLELQCQQ PCRDTVQIQE FTGKDCQEVA
NKGARLSGLY YIKPLKAKQQ FLVYCEIEPS GSAWTVIQRR LDGSVNFHKN WVQYREGFGY
LSPNDKTEFW LGNEKIHLLS TQSTIPYVMR IELEDWSNQK STADYSTFRL GSEKDNYRFT
YAYFIGGDAG DAFDGFDFGD DPSDKFYTSH NGMQFSTFDK DNDKFDGNCA EQDGSGWWMN
RCHAAHLNGK YYQGGTYSEA DSGPSGYDNG IIWATWRRRW YSMKSVTMKI MPLNRYGAEG
QQTLGGSKKS DFENRGDF
