UniProtKB - P04115 (FIBG_PETMA)
Protein
Fibrinogen gamma chain
Gene
FGG
Organism
Petromyzon marinus (Sea lamprey)
Status
Functioni
Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 340 | CalciumCombined sources2 Publications | 1 | |
Metal bindingi | 342 | CalciumCombined sources2 Publications | 1 | |
Metal bindingi | 344 | Calcium; via carbonyl oxygenCombined sources2 Publications | 1 | |
Metal bindingi | 346 | Calcium; via carbonyl oxygenCombined sources2 Publications | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- signaling receptor binding Source: InterPro
GO - Biological processi
- platelet activation Source: InterPro
- protein polymerization Source: InterPro
Keywordsi
Biological process | Blood coagulation, Hemostasis |
Ligand | Calcium, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Fibrinogen gamma chain |
Gene namesi | Name:FGG |
Organismi | Petromyzon marinus (Sea lamprey) |
Taxonomic identifieri | 7757 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Cyclostomata › Hyperoartia › Petromyzontiformes › Petromyzontidae › Petromyzon |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- fibrinogen complex Source: InterPro
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | By similarityAdd BLAST | 24 | |
ChainiPRO_0000009102 | 25 – 432 | Fibrinogen gamma chainAdd BLAST | 408 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 32 | Interchain (with gamma chain)PROSITE-ProRule annotation | ||
Disulfide bondi | 42 | Interchain (with beta chain)PROSITE-ProRule annotation | ||
Disulfide bondi | 46 | Interchain (with alpha chain)PROSITE-ProRule annotation | ||
Disulfide bondi | 158 | Interchain (with beta chain) | ||
Disulfide bondi | 162 | Interchain (with gamma chain) | ||
Disulfide bondi | 178 ↔ 207 | 2 Publications | ||
Glycosylationi | 227 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 348 ↔ 361 | 2 Publications |
Post-translational modificationi
Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Keywords - PTMi
Disulfide bond, GlycoproteinPTM databases
iPTMneti | P04115 |
Interactioni
Subunit structurei
Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.
2 PublicationsGO - Molecular functioni
- signaling receptor binding Source: InterPro
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P04115 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P04115 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 169 – 412 | Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST | 244 |
Domaini
A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.2 Publications
Keywords - Domaini
Coiled coil, SignalFamily and domain databases
CDDi | cd00087, FReD, 1 hit |
Gene3Di | 3.90.215.10, 1 hit 4.10.530.10, 1 hit |
InterProi | View protein in InterPro IPR036056, Fibrinogen-like_C IPR014716, Fibrinogen_a/b/g_C_1 IPR014715, Fibrinogen_a/b/g_C_2 IPR002181, Fibrinogen_a/b/g_C_dom IPR012290, Fibrinogen_a/b/g_coil_dom IPR020837, Fibrinogen_CS IPR037581, Fibrinogen_gamma |
PANTHERi | PTHR19143:SF338, PTHR19143:SF338, 1 hit |
Pfami | View protein in Pfam PF08702, Fib_alpha, 1 hit PF00147, Fibrinogen_C, 1 hit |
SMARTi | View protein in SMART SM00186, FBG, 1 hit SM01212, Fib_alpha, 1 hit |
SUPFAMi | SSF56496, SSF56496, 1 hit |
PROSITEi | View protein in PROSITE PS00514, FIBRINOGEN_C_1, 1 hit PS51406, FIBRINOGEN_C_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P04115-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGRIGTPVFL AFLSALTCSL QVHAQVRDLK QCSNDPEFGR YCPTTCGVAD
60 70 80 90 100
VLSKYAKGVD EDSSFIDSVL TQLAAKHGIV EGNVNIVNED VRITRDEAQI
110 120 130 140 150
IKDSGQKTVQ KILEEVRILE QIGVSHDAQI QELSEMWRVN QQFVTRLQQQ
160 170 180 190 200
LVDIRQTCSR SCQDTTANKI SPITGKDCQQ VVDNGGKDSG LYYIKPLKAK
210 220 230 240 250
QPFLVFCEIE NGNGWTVIQH RHDGSVNFTR DWVSYREGFG YLAPTLTTEF
260 270 280 290 300
WLGNEKIHLL TGQQAYRLRI DLTDWENTHR YADYGHFKLT PESDEYRLFY
310 320 330 340 350
SMYLDGDAGN AFDGFDFGDD PQDKFYTTHL GMLFSTPERD NDKYEGSCAE
360 370 380 390 400
QDGSGWWMNR CHAGHLNGKY YFGGNYRKTD VEFPYDDGII WATWHDRWYS
410 420 430
LKMTTMKLLP MGRDLSGHGG QQQSKGNSRG DN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K03049 mRNA Translation: AAA49262.1 |
PIRi | A03129, FGLMGS |
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K03049 mRNA Translation: AAA49262.1 |
PIRi | A03129, FGLMGS |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1LWU | X-ray | 2.80 | C/F/I/L | 103-425 | [»] | |
1N73 | X-ray | 2.90 | C/F | 103-432 | [»] | |
SMRi | P04115 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
PTM databases
iPTMneti | P04115 |
Miscellaneous databases
EvolutionaryTracei | P04115 |
Family and domain databases
CDDi | cd00087, FReD, 1 hit |
Gene3Di | 3.90.215.10, 1 hit 4.10.530.10, 1 hit |
InterProi | View protein in InterPro IPR036056, Fibrinogen-like_C IPR014716, Fibrinogen_a/b/g_C_1 IPR014715, Fibrinogen_a/b/g_C_2 IPR002181, Fibrinogen_a/b/g_C_dom IPR012290, Fibrinogen_a/b/g_coil_dom IPR020837, Fibrinogen_CS IPR037581, Fibrinogen_gamma |
PANTHERi | PTHR19143:SF338, PTHR19143:SF338, 1 hit |
Pfami | View protein in Pfam PF08702, Fib_alpha, 1 hit PF00147, Fibrinogen_C, 1 hit |
SMARTi | View protein in SMART SM00186, FBG, 1 hit SM01212, Fib_alpha, 1 hit |
SUPFAMi | SSF56496, SSF56496, 1 hit |
PROSITEi | View protein in PROSITE PS00514, FIBRINOGEN_C_1, 1 hit PS51406, FIBRINOGEN_C_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FIBG_PETMA | |
Accessioni | P04115Primary (citable) accession number: P04115 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1986 |
Last sequence update: | November 1, 1986 | |
Last modified: | October 7, 2020 | |
This is version 100 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references