FIBG_PETMA
ID FIBG_PETMA Reviewed; 432 AA.
AC P04115;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Fibrinogen gamma chain;
DE Flags: Precursor;
GN Name=FGG;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2581603; DOI=10.1021/bi00322a014;
RA Strong D.D., Moore M., Cottrell B.A., Bohonus V.L., Pontes M., Evans B.,
RA Riley M., Doolittle R.F.;
RT "Lamprey fibrinogen gamma chain: cloning, cDNA sequencing, and general
RT characterization.";
RL Biochemistry 24:92-101(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 103-425 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-227, AND SUBUNIT.
RX PubMed=12162736; DOI=10.1021/bi020299t;
RA Yang Z., Spraggon G., Pandi L., Everse S.J., Riley M., Doolittle R.F.;
RT "Crystal structure of fragment D from lamprey fibrinogen complexed with the
RT peptide Gly-His-Arg-Pro-amide.";
RL Biochemistry 41:10218-10224(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 103-432 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-227, SUBCELLULAR LOCATION, SUBUNIT,
RP AND COILED COIL DOMAIN.
RX PubMed=12501189; DOI=10.1021/bi026666i;
RA Yang Z., Pandi L., Doolittle R.F.;
RT "The crystal structure of fragment double-D from cross-linked lamprey
RT fibrin reveals isopeptide linkages across an unexpected D-D interface.";
RL Biochemistry 41:15610-15617(2002).
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 {ECO:0000269|PubMed:12162736, ECO:0000269|PubMed:12501189}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12501189}.
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:0000269|PubMed:12162736, ECO:0000269|PubMed:12501189}.
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; K03049; AAA49262.1; -; mRNA.
DR PIR; A03129; FGLMGS.
DR PDB; 1LWU; X-ray; 2.80 A; C/F/I/L=103-425.
DR PDB; 1N73; X-ray; 2.90 A; C/F=103-432.
DR PDBsum; 1LWU; -.
DR PDBsum; 1N73; -.
DR AlphaFoldDB; P04115; -.
DR SMR; P04115; -.
DR STRING; 7757.ENSPMAP00000001295; -.
DR iPTMnet; P04115; -.
DR EvolutionaryTrace; P04115; -.
DR Proteomes; UP000245300; Unplaced.
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 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium; Coiled coil; Disulfide bond;
KW Glycoprotein; Hemostasis; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..432
FT /note="Fibrinogen gamma chain"
FT /id="PRO_0000009102"
FT DOMAIN 169..412
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189, ECO:0007744|PDB:1LWU,
FT ECO:0007744|PDB:1N73"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189, ECO:0007744|PDB:1LWU,
FT ECO:0007744|PDB:1N73"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189, ECO:0007744|PDB:1LWU,
FT ECO:0007744|PDB:1N73"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189, ECO:0007744|PDB:1LWU,
FT ECO:0007744|PDB:1N73"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189"
FT DISULFID 32
FT /note="Interchain (with gamma chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 42
FT /note="Interchain (with beta chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 46
FT /note="Interchain (with alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 158
FT /note="Interchain (with beta chain)"
FT DISULFID 162
FT /note="Interchain (with gamma chain)"
FT DISULFID 178..207
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189"
FT DISULFID 348..361
FT /evidence="ECO:0000269|PubMed:12162736,
FT ECO:0000269|PubMed:12501189"
FT HELIX 108..157
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 178..182
FT /evidence="ECO:0007829|PDB:1LWU"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:1N73"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1LWU"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 402..412
FT /evidence="ECO:0007829|PDB:1LWU"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1N73"
SQ SEQUENCE 432 AA; 49203 MW; B503979B296DFB24 CRC64;
MGRIGTPVFL AFLSALTCSL QVHAQVRDLK QCSNDPEFGR YCPTTCGVAD VLSKYAKGVD
EDSSFIDSVL TQLAAKHGIV EGNVNIVNED VRITRDEAQI IKDSGQKTVQ KILEEVRILE
QIGVSHDAQI QELSEMWRVN QQFVTRLQQQ LVDIRQTCSR SCQDTTANKI SPITGKDCQQ
VVDNGGKDSG LYYIKPLKAK QPFLVFCEIE NGNGWTVIQH RHDGSVNFTR DWVSYREGFG
YLAPTLTTEF WLGNEKIHLL TGQQAYRLRI DLTDWENTHR YADYGHFKLT PESDEYRLFY
SMYLDGDAGN AFDGFDFGDD PQDKFYTTHL GMLFSTPERD NDKYEGSCAE QDGSGWWMNR
CHAGHLNGKY YFGGNYRKTD VEFPYDDGII WATWHDRWYS LKMTTMKLLP MGRDLSGHGG
QQQSKGNSRG DN
