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Protein

Prothrombin

Gene

F2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing.1 Publication

Miscellaneous

Prothrombin is activated on the surface of a phospholipid membrane that binds the amino end of prothrombin and factors Va and Xa in Ca-dependent interactions; factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. The activation process starts slowly because factor V itself has to be activated by the initial, small amounts of thrombin.
It is not known whether 1 or 2 smaller activation peptides, with additional cleavage after Arg-314, are released in natural blood clotting.
Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.
The cleavage after Arg-198, observed in vitro, does not occur in plasma.

Catalytic activityi

Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.

Enzyme regulationi

Inhibited by SERPINA5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei406Charge relay system1
Active sitei462Charge relay system1
Active sitei568Charge relay system1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • growth factor activity Source: BHF-UCL
  • heparin binding Source: UniProtKB
  • lipopolysaccharide binding Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB
  • signaling receptor binding Source: UniProtKB
  • thrombospondin receptor activity Source: BHF-UCL

GO - Biological processi

  • acute-phase response Source: UniProtKB-KW
  • antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
  • blood coagulation Source: Reactome
  • blood coagulation, intrinsic pathway Source: Reactome
  • cell surface receptor signaling pathway Source: BHF-UCL
  • cellular protein metabolic process Source: Reactome
  • cytolysis by host of symbiont cells Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • fibrinolysis Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: Reactome
  • multicellular organism development Source: ProtInc
  • negative regulation of astrocyte differentiation Source: BHF-UCL
  • negative regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • negative regulation of fibrinolysis Source: BHF-UCL
  • negative regulation of platelet activation Source: BHF-UCL
  • negative regulation of proteolysis Source: BHF-UCL
  • neutrophil mediated killing of gram-negative bacterium Source: UniProtKB
  • platelet activation Source: BHF-UCL
  • positive regulation of blood coagulation Source: BHF-UCL
  • positive regulation of cell growth Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of collagen biosynthetic process Source: BHF-UCL
  • positive regulation of JAK-STAT cascade Source: BHF-UCL
  • positive regulation of lipid kinase activity Source: BHF-UCL
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  • positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway Source: BHF-UCL
  • positive regulation of protein localization to nucleus Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of reactive oxygen species metabolic process Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  • proteolysis Source: ProtInc
  • regulation of blood coagulation Source: UniProtKB
  • regulation of cell shape Source: Ensembl
  • regulation of complement activation Source: Reactome
  • regulation of cytosolic calcium ion concentration Source: BHF-UCL
  • response to wounding Source: BHF-UCL

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processAcute phase, Blood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

BRENDAi3.4.21.5 2681
ReactomeiR-HSA-140837 Intrinsic Pathway of Fibrin Clot Formation
R-HSA-140875 Common Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-375276 Peptide ligand-binding receptors
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-416476 G alpha (q) signalling events
R-HSA-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-HSA-76009 Platelet Aggregation (Plug Formation)
R-HSA-977606 Regulation of Complement cascade
SABIO-RKiP00734
SIGNORiP00734

Protein family/group databases

MEROPSiS01.217
MoonDBiP00734 Curated

Names & Taxonomyi

Protein namesi
Recommended name:
Prothrombin (EC:3.4.21.5)
Alternative name(s):
Coagulation factor II
Cleaved into the following 4 chains:
Gene namesi
Name:F2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000180210.14
HGNCiHGNC:3535 F2
MIMi176930 gene
neXtProtiNX_P00734

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor II deficiency (FA2D)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA very rare blood coagulation disorder characterized by mucocutaneous bleeding symptoms. The severity of the bleeding manifestations correlates with blood factor II levels.
See also OMIM:613679
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05523272E → G in FA2D; Shanghai. 1 Publication1
Natural variantiVAR_006711200E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 PublicationsCorresponds to variant dbSNP:rs62623459EnsemblClinVar.1
Natural variantiVAR_006712314R → C in FA2D; Barcelona/Madrid. 1 PublicationCorresponds to variant dbSNP:rs121918477EnsemblClinVar.1
Natural variantiVAR_006713314R → H in FA2D; Padua-1. 1 PublicationCorresponds to variant dbSNP:rs754231232Ensembl.1
Natural variantiVAR_006714380M → T in FA2D; Himi-1. 1 PublicationCorresponds to variant dbSNP:rs121918481EnsemblClinVar.1
Natural variantiVAR_006715425R → C in FA2D; Quick-1. 1 PublicationCorresponds to variant dbSNP:rs121918479EnsemblClinVar.1
Natural variantiVAR_006716431R → H in FA2D; Himi-2. 1 PublicationCorresponds to variant dbSNP:rs121918482EnsemblClinVar.1
Natural variantiVAR_006717461R → W in FA2D; Tokushima. 3 PublicationsCorresponds to variant dbSNP:rs121918478EnsemblClinVar.1
Natural variantiVAR_006718509E → A in FA2D; Salakta/Frankfurt. 2 Publications1
Natural variantiVAR_006719601G → V in FA2D; Quick-2. 1 PublicationCorresponds to variant dbSNP:rs121918480EnsemblClinVar.1
Ischemic stroke (ISCHSTR)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.
See also OMIM:601367
Thrombophilia due to thrombin defect (THPH1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry. A common genetic variation in the 3-prime untranslated region of the prothrombin gene is associated with elevated plasma prothrombin levels and an increased risk of venous thrombosis.
Disease descriptionA multifactorial disorder of hemostasis characterized by abnormal platelet aggregation in response to various agents and recurrent thrombi formation.
See also OMIM:188050
Pregnancy loss, recurrent, 2 (RPRGL2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.
See also OMIM:614390

Pharmaceutical usei

The peptide TP508 also known as Chrysalin (Orthologic) could be used to accelerate repair of both soft and hard tissues.

Keywords - Diseasei

Disease mutation, Thrombophilia

Organism-specific databases

DisGeNETi2147
GeneReviewsiF2
MalaCardsiF2
MIMi188050 phenotype
601367 phenotype
613679 phenotype
614390 phenotype
OpenTargetsiENSG00000180210
Orphaneti329217 Cerebral sinovenous thrombosis
325 Congenital factor II deficiency
64738 Non rare thrombophilia
PharmGKBiPA157

Chemistry databases

ChEMBLiCHEMBL204
DrugBankiDB07211 (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE
DB06850 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07091 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB06845 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide
DB07088 (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide
DB07131 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide
DB07095 (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide
DB07897 1-(HYDROXYMETHYLENEAMINO)-8-HYDROXY-OCTANE
DB06878 1-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)-L-prolinamide
DB06947 1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB06869 1-[2-AMINO-2-CYCLOHEXYL-ACETYL]-PYRROLIDINE-3-CARBOXYLIC ACID 5-CHLORO-2-(2-ETHYLCARBAMOYL-ETHOXY)-BENZYLAMIDE
DB06929 1-butanoyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB07400 1-ETHOXYCARBONYL-D-PHE-PRO-2(4-AMINOBUTYL)HYDRAZINE
DB04771 1-GUANIDINO-4-(N-NITRO-BENZOYLAMINO-L-LEUCYL-L-PROLYLAMINO)BUTANE
DB04772 1-GUANIDINO-4-(N-PHENYLMETHANESULFONYL-L-LEUCYL-L-PROLYLAMINO)BUTANE
DB06854 2-(2-HYDROXY-BIPHENYL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE
DB02193 2-(2-Hydroxy-Phenyl)-1h-Benzoimidazole-5-Carboxamidine
DB07277 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE
DB07278 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHENESULFONAMIDE
DB07105 2-[2-(4-CHLORO-PHENYLSULFANYL)-ACETYLAMINO]-3-(4-GUANIDINO-PHENYL)-PROPIONAMIDE
DB07366 2-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTER
DB08254 2-NAPHTHALENESULFONIC ACID
DB07718 3-(4-HYDROXY-PHENYL)PYRUVIC ACID
DB07639 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER
DB07190 3-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamide
DB07508 4-(5-BENZENESULFONYLAMINO-1-METHYL-1H-BENZOIMIDAZOL-2-YLMETHYL)-BENZAMIDINE
DB07809 4-({[4-(3-METHYLBENZOYL)PYRIDIN-2-YL]AMINO}METHYL)BENZENECARBOXIMIDAMIDE
DB08061 4-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINE
DB03136 4-Iodobenzo[B]Thiophene-2-Carboxamidine
DB07440 4-TERT-BUTYLBENZENESULFONIC ACID
DB07376 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID)
DB06861 6-(2-HYDROXY-CYCLOPENTYL)-7-OXO-HEPTANAMIDINE
DB06866 6-CARBAMIMIDOYL-2-[2-HYDROXY-5-(3-METHOXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID
DB06865 6-CARBAMIMIDOYL-2-[2-HYDROXY-6-(4-HYDROXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID
DB03865 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine
DB07934 [[CYCLOHEXANESULFONYL-GLYCYL]-3[PYRIDIN-4-YL-AMINOMETHYL]ALANYL]PIPERIDINE
DB08422 [PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINE
DB07659 AC-(D)PHE-PRO-BOROHOMOLYS-OH
DB07660 AC-(D)PHE-PRO-BOROHOMOORNITHINE-OH
DB07658 AC-(D)PHE-PRO-BOROLYS-OH
DB00025 Antihemophilic Factor (Recombinant)
DB00278 Argatroban
DB08624 BENZOTHIAZOLE
DB01766 Beta-(2-Naphthyl)-Alanine
DB07083 beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide
DB00006 Bivalirudin
DB06404 C1 Esterase Inhibitor (Human)
DB09228 C1 Esterase Inhibitor (Recombinant)
DB00100 Coagulation Factor IX (Recombinant)
DB03159 CRA_8696
DB06911 D-leucyl-N-(3-chlorobenzyl)-L-prolinamide
DB06996 D-leucyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB06919 D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide
DB07027 D-phenylalanyl-N-(3-fluorobenzyl)-L-prolinamide
DB07133 D-phenylalanyl-N-(3-methylbenzyl)-L-prolinamide
DB06841 D-phenylalanyl-N-[(1S)-4-{[amino(iminio)methyl]amino}-1-(chloroacetyl)butyl]-L-prolinamide
DB07143 D-phenylalanyl-N-benzyl-L-prolinamide
DB07005 D-phenylalanyl-N-{4-[amino(iminio)methyl]benzyl}-L-prolinamide
DB06695 Dabigatran etexilate
DB00055 Drotrecogin alfa
DB03847 Gamma-Carboxy-Glutamic Acid
DB01767 Hemi-Babim
DB00001 Lepirudin
DB04136 Lysophosphotidylserine
DB00170 Menadione
DB06838 methyl L-phenylalaninate
DB08187 METHYL-PHE-PRO-AMINO-CYCLOHEXYLGLYCINE
DB06868 N-(3-chlorobenzyl)-1-(4-methylpentanoyl)-L-prolinamide
DB06942 N-(4-carbamimidoylbenzyl)-1-(3-phenylpropanoyl)-L-prolinamide
DB06936 N-(4-carbamimidoylbenzyl)-1-(4-methylpentanoyl)-L-prolinamide
DB07165 N-(5-CHLORO-BENZO[B]THIOPHEN-3-YLMETHYL)-2-[6-CHLORO-OXO-3-(2-PYRIDIN-2-YL-ETHYLAMINO)-2H-PYRAZIN-1-YL]-ACETAMIDE
DB06859 N-ALLYL-5-AMIDINOAMINOOXY-PROPYLOXY-3-CHLORO-N-CYCLOPENTYLBENZAMIDE
DB06853 N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB06858 N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide
DB07279 N-ETHYL-N-ISOPROPYL-3-METHYL-5-{[(2S)-2-(PYRIDIN-4-YLAMINO)PROPYL]OXY}BENZAMIDE
DB07944 N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE
DB01123 Proflavine
DB04786 Suramin
DB05777 Thrombomodulin Alfa
DB04697 TRANS-4-(GUANIDINOMETHYL)-CYCLOHEXANE-L-YL-D-3-CYCLOHEXYLALANYL-L-AZETIDINE-2-YL-D-TYROSINYL-L-HOMOARGININAMIDE
DB04898 Ximelagatran
DB08152 {(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate
GuidetoPHARMACOLOGYi2362

Polymorphism and mutation databases

BioMutaiF2
DMDMi135807

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002815925 – 432 PublicationsAdd BLAST19
ChainiPRO_000002816044 – 622ProthrombinAdd BLAST579
PeptideiPRO_000002816144 – 198Activation peptide fragment 1Add BLAST155
PeptideiPRO_0000028162199 – 327Activation peptide fragment 2Add BLAST129
ChainiPRO_0000028163328 – 363Thrombin light chainAdd BLAST36
ChainiPRO_0000028164364 – 622Thrombin heavy chainAdd BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei494-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei504-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi60 ↔ 65
Modified residuei624-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei634-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei684-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 103
Disulfide bondi108 ↔ 186
Glycosylationi121N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi129 ↔ 169
Glycosylationi143N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi157 ↔ 181
Disulfide bondi213 ↔ 291
Disulfide bondi234 ↔ 274
Disulfide bondi262 ↔ 286
Disulfide bondi336 ↔ 482Interchain (between light and heavy chains)
Disulfide bondi391 ↔ 407
Glycosylationi416N-linked (GlcNAc...) (complex) asparagine5 Publications1
Disulfide bondi536 ↔ 550By similarity
Disulfide bondi564 ↔ 594By similarity

Post-translational modificationi

The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin.2 Publications
N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei198 – 199Cleavage; by thrombin2
Sitei327 – 328Cleavage; by factor Xa2
Sitei363 – 364Cleavage; by factor Xa2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP00734
PaxDbiP00734
PeptideAtlasiP00734
PRIDEiP00734
ProteomicsDBi51269
TopDownProteomicsiP00734

2D gel databases

SWISS-2DPAGEiP00734

PTM databases

GlyConnecti518
iPTMnetiP00734
PhosphoSitePlusiP00734
UniCarbKBiP00734

Miscellaneous databases

PMAP-CutDBiP00734

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000180210
CleanExiHS_F2
ExpressionAtlasiP00734 baseline and differential
GenevisibleiP00734 HS

Organism-specific databases

HPAiCAB016780
CAB018650
HPA051476
HPA054698

Interactioni

Subunit structurei

Heterodimer (named alpha-thrombin) of a light and a heavy chain; disulfide-linked. Forms a heterodimer with SERPINA5.7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • growth factor activity Source: BHF-UCL
  • signaling receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108447, 16 interactors
DIPiDIP-6115N
IntActiP00734, 13 interactors
STRINGi9606.ENSP00000308541

Chemistry databases

BindingDBiP00734

Structurei

Secondary structure

1622
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 60Combined sources14
Helixi67 – 74Combined sources8
Helixi77 – 89Combined sources13
Turni90 – 92Combined sources3
Helixi97 – 105Combined sources9
Beta strandi107 – 109Combined sources3
Turni112 – 115Combined sources4
Beta strandi124 – 126Combined sources3
Beta strandi128 – 130Combined sources3
Turni144 – 146Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi167 – 173Combined sources7
Beta strandi177 – 180Combined sources4
Turni186 – 188Combined sources3
Beta strandi191 – 193Combined sources3
Beta strandi211 – 214Combined sources4
Helixi216 – 218Combined sources3
Beta strandi229 – 231Combined sources3
Beta strandi233 – 235Combined sources3
Beta strandi237 – 239Combined sources3
Helixi240 – 246Combined sources7
Beta strandi247 – 249Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi273 – 275Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi283 – 285Combined sources3
Helixi295 – 297Combined sources3
Beta strandi322 – 324Combined sources3
Turni326 – 328Combined sources3
Helixi329 – 333Combined sources5
Turni334 – 337Combined sources4
Turni340 – 342Combined sources3
Helixi343 – 345Combined sources3
Helixi352 – 358Combined sources7
Beta strandi361 – 367Combined sources7
Helixi369 – 371Combined sources3
Beta strandi372 – 374Combined sources3
Helixi375 – 377Combined sources3
Beta strandi378 – 383Combined sources6
Turni384 – 387Combined sources4
Beta strandi388 – 395Combined sources8
Beta strandi397 – 403Combined sources7
Helixi405 – 407Combined sources3
Beta strandi408 – 410Combined sources3
Helixi411 – 413Combined sources3
Turni415 – 417Combined sources3
Helixi419 – 421Combined sources3
Beta strandi422 – 427Combined sources6
Beta strandi430 – 433Combined sources4
Turni436 – 438Combined sources3
Beta strandi440 – 449Combined sources10
Turni455 – 458Combined sources4
Beta strandi464 – 470Combined sources7
Beta strandi475 – 477Combined sources3
Helixi486 – 492Combined sources7
Beta strandi495 – 497Combined sources3
Beta strandi498 – 504Combined sources7
Beta strandi507 – 510Combined sources4
Turni513 – 515Combined sources3
Beta strandi516 – 518Combined sources3
Beta strandi524 – 530Combined sources7
Helixi533 – 538Combined sources6
Beta strandi540 – 542Combined sources3
Beta strandi548 – 551Combined sources4
Helixi555 – 557Combined sources3
Turni565 – 569Combined sources5
Beta strandi571 – 575Combined sources5
Turni577 – 579Combined sources3
Beta strandi582 – 590Combined sources9
Beta strandi592 – 595Combined sources4
Beta strandi596 – 598Combined sources3
Beta strandi601 – 605Combined sources5
Helixi607 – 609Combined sources3
Helixi610 – 619Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2CX-ray2.10H364-622[»]
L328-363[»]
1A3BX-ray1.80H364-622[»]
L328-363[»]
1A3EX-ray1.85H364-622[»]
L328-363[»]
1A46X-ray2.12H364-622[»]
L328-363[»]
1A4WX-ray1.80H364-622[»]
L328-363[»]
1A5GX-ray2.06H364-622[»]
L328-363[»]
1A61X-ray2.20H364-622[»]
L328-363[»]
1ABIX-ray2.30H364-622[»]
L328-363[»]
1ABJX-ray2.40H364-622[»]
L328-363[»]
1AD8X-ray2.00H364-622[»]
L328-363[»]
1AE8X-ray2.00H364-622[»]
L328-363[»]
1AFEX-ray2.00H364-622[»]
L328-363[»]
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L334-363[»]
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L334-360[»]
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L328-363[»]
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L334-361[»]
4AYVX-ray2.80A332-361[»]
B364-620[»]
4AYYX-ray2.60A332-361[»]
B364-620[»]
4AZ2X-ray2.60A332-361[»]
B364-620[»]
4BAHX-ray1.94A328-363[»]
B364-622[»]
4BAKX-ray1.94A328-363[»]
B364-622[»]
4BAMX-ray1.88A328-363[»]
B364-622[»]
4BANX-ray1.87A328-363[»]
B364-622[»]
4BAOX-ray1.87A328-363[»]
B364-622[»]
4BAQX-ray1.89A328-363[»]
B364-622[»]
4BOHX-ray2.60A/H364-622[»]
B/L328-363[»]
4CH2X-ray1.60A/C328-363[»]
B/D364-622[»]
4CH8X-ray1.75A/C/E/G328-363[»]
B/D/F/H364-622[»]
4DIHX-ray1.80H364-622[»]
L328-363[»]
4DIIX-ray2.05H364-622[»]
L328-363[»]
4DT7X-ray1.90A/C332-363[»]
B/D364-622[»]
4DY7X-ray2.80A/D315-363[»]
B/E364-622[»]
4E05X-ray2.30H364-622[»]
L328-363[»]
4E06X-ray3.20H364-622[»]
L328-363[»]
4E7RX-ray2.25G/H364-622[»]
L/M328-363[»]
4H6SX-ray2.19A333-363[»]
B364-622[»]
4H6TX-ray2.40A317-622[»]
4HFPX-ray2.40A/C333-363[»]
B/D364-622[»]
4HTCX-ray2.30H364-622[»]
L328-363[»]
4HZHX-ray3.30A/B90-622[»]
4I7YX-ray2.40H364-622[»]
L328-363[»]
4LOYX-ray1.77H364-620[»]
L334-360[»]
4LXBX-ray1.61H364-622[»]
L328-363[»]
4LZ1X-ray1.65H364-622[»]
L328-363[»]
4LZ4X-ray2.56A/C328-363[»]
B/D364-622[»]
4MLFX-ray2.20A331-363[»]
B364-622[»]
4NZQX-ray2.81A44-622[»]
4O03X-ray3.38A44-622[»]
4RKJX-ray1.70A330-363[»]
B364-622[»]
4RKOX-ray1.84A322-363[»]
B364-622[»]
4RN6X-ray3.00A/B333-622[»]
4THNX-ray2.50H364-622[»]
L328-363[»]
4UD9X-ray1.12H364-622[»]
L333-360[»]
4UDWX-ray1.16H364-621[»]
L333-360[»]
4UE7X-ray1.13H364-621[»]
L333-360[»]
4UEHX-ray1.16H364-621[»]
L333-361[»]
4UFDX-ray1.43H364-621[»]
L333-360[»]
4UFEX-ray1.59H364-621[»]
L333-361[»]
4UFFX-ray1.55H364-621[»]
L333-361[»]
4UFGX-ray1.65H364-621[»]
L333-361[»]
4YESX-ray1.50A328-363[»]
B364-622[»]
5A2MX-ray1.40H364-621[»]
L333-361[»]
5AF9X-ray1.18H364-621[»]
L333-361[»]
5AFYX-ray1.12H364-621[»]
L333-361[»]
5AFZX-ray1.53H364-621[»]
L333-361[»]
5AHGX-ray1.24H364-621[»]
L333-361[»]
5CMXX-ray2.98H364-622[»]
L328-363[»]
5DO4X-ray1.86H364-621[»]
L328-363[»]
5E8EX-ray1.90H364-622[»]
L328-363[»]
5EDKX-ray3.21A44-622[»]
5EDMX-ray2.20A44-622[»]
5EW1X-ray2.95H364-622[»]
L328-363[»]
5EW2X-ray3.59H364-622[»]
L328-363[»]
5GDSX-ray2.10H364-622[»]
L328-363[»]
5GIMX-ray2.09A328-363[»]
5JDUX-ray1.70A/C331-363[»]
B/D364-622[»]
5JFDX-ray1.46H364-622[»]
L328-363[»]
5JZYX-ray1.27H364-622[»]
L328-363[»]
5L6NX-ray1.63H364-622[»]
L328-363[»]
5MJTX-ray1.40H364-622[»]
L328-363[»]
5MLSX-ray1.62H364-622[»]
L328-363[»]
5MM6X-ray1.29H364-622[»]
L328-363[»]
5NHUX-ray1.45A/C/H364-622[»]
B/D/L328-363[»]
5TO3X-ray2.34A318-363[»]
B364-621[»]
5Z5WNMR-A606-617[»]
5Z5XNMR-A605-622[»]
6C2WX-ray4.12A/B44-622[»]
6EO6X-ray1.69H364-622[»]
L328-363[»]
6EO7X-ray2.24H364-622[»]
L328-363[»]
6EO8X-ray1.94H364-622[»]
L328-363[»]
6EO9X-ray1.84H364-622[»]
L328-363[»]
7KMEX-ray2.10H364-622[»]
L328-363[»]
8KMEX-ray2.101328-359[»]
2364-620[»]
ProteinModelPortaliP00734
SMRiP00734
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00734

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 89GlaPROSITE-ProRule annotationAdd BLAST46
Domaini108 – 186Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini213 – 291Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini364 – 618Peptidase S1PROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni551 – 573High affinity receptor-binding region which is also known as the TP508 peptideAdd BLAST23

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IKPN Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000119133
HOVERGENiHBG108381
InParanoidiP00734
KOiK01313
OMAiHPVCLPD
OrthoDBiEOG091G0AH5
PhylomeDBiP00734
TreeFamiTF327329

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di2.40.20.10, 2 hits
4.10.140.10, 1 hit
InterProiView protein in InterPro
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR003966 Prothrombin/thrombin
IPR018992 Thrombin_light_chain
IPR037111 Thrombin_light_chain_sf
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PANTHERiPTHR24254:SF10 PTHR24254:SF10, 1 hit
PfamiView protein in Pfam
PF00594 Gla, 1 hit
PF00051 Kringle, 2 hits
PF09396 Thrombin_light, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001149 Thrombin, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
PR01505 PROTHROMBIN
SMARTiView protein in SMART
SM00069 GLA, 1 hit
SM00130 KR, 2 hits
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00011 GLA_1, 1 hit
PS50998 GLA_2, 1 hit
PS00021 KRINGLE_1, 2 hits
PS50070 KRINGLE_2, 2 hits
PS50240 TRYPSIN_DOM, 1 hit
PS00134 TRYPSIN_HIS, 1 hit
PS00135 TRYPSIN_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00734-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE
60 70 80 90 100
VRKGNLEREC VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL
110 120 130 140 150
AACLEGNCAE GLGTNYRGHV NITRSGIECQ LWRSRYPHKP EINSTTHPGA
160 170 180 190 200
DLQENFCRNP DSSTTGPWCY TTDPTVRRQE CSIPVCGQDQ VTVAMTPRSE
210 220 230 240 250
GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA QAKALSKHQD
260 270 280 290 300
FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG
310 320 330 340 350
DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK
360 370 380 390 400
TERELLESYI DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW
410 420 430 440 450
VLTAAHCLLY PPWDKNFTEN DLLVRIGKHS RTRYERNIEK ISMLEKIYIH
460 470 480 490 500
PRYNWRENLD RDIALMKLKK PVAFSDYIHP VCLPDRETAA SLLQAGYKGR
510 520 530 540 550
VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST RIRITDNMFC
560 570 580 590 600
AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY
610 620
GFYTHVFRLK KWIQKVIDQF GE
Length:622
Mass (Da):70,037
Last modified:January 1, 1990 - v2
Checksum:i8A25E1DA88208FCF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 25Missing in BAG64719 (PubMed:14702039).CuratedAdd BLAST17
Sequence conflicti66S → N in BAD96497 (Ref. 4) Curated1
Sequence conflicti119H → N AA sequence (PubMed:266717).Curated1
Sequence conflicti121N → S AA sequence (PubMed:266717).Curated1
Sequence conflicti164T → I AA sequence (PubMed:266717).Curated1
Sequence conflicti164T → N in CAA23842 (PubMed:6305407).Curated1
Sequence conflicti176V → A AA sequence (PubMed:266717).Curated1
Sequence conflicti183I → T AA sequence (PubMed:266717).Curated1
Sequence conflicti194 – 195AM → MV AA sequence (PubMed:266717).Curated2
Sequence conflicti308D → DEE AA sequence (PubMed:266717).Curated1
Sequence conflicti335D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti337G → R in BAD96495 (Ref. 4) Curated1
Sequence conflicti349D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti369D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti398D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti414D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti485D → N AA sequence (PubMed:873923).Curated1
Sequence conflicti494Q → G AA sequence (PubMed:873923).Curated1
Sequence conflicti504W → Y AA sequence (PubMed:873923).Curated1
Sequence conflicti509E → S AA sequence (PubMed:873923).Curated1
Sequence conflicti511W → V AA sequence (PubMed:873923).Curated1
Sequence conflicti514N → D AA sequence (PubMed:873923).Curated1
Sequence conflicti529 – 530PI → AL AA sequence (PubMed:873923).Curated2
Sequence conflicti590 – 592WGE → AGA in AAR08143 (Ref. 11) Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05523272E → G in FA2D; Shanghai. 1 Publication1
Natural variantiVAR_011781165T → M Polymorphism; confirmed at protein level. 4 PublicationsCorresponds to variant dbSNP:rs5896EnsemblClinVar.1
Natural variantiVAR_006711200E → K in FA2D; prothrombin type 3; variant confirmed at protein level. 2 PublicationsCorresponds to variant dbSNP:rs62623459EnsemblClinVar.1
Natural variantiVAR_006712314R → C in FA2D; Barcelona/Madrid. 1 PublicationCorresponds to variant dbSNP:rs121918477EnsemblClinVar.1
Natural variantiVAR_006713314R → H in FA2D; Padua-1. 1 PublicationCorresponds to variant dbSNP:rs754231232Ensembl.1
Natural variantiVAR_006714380M → T in FA2D; Himi-1. 1 PublicationCorresponds to variant dbSNP:rs121918481EnsemblClinVar.1
Natural variantiVAR_011782386P → T Polymorphism; confirmed at protein level. 2 PublicationsCorresponds to variant dbSNP:rs5897Ensembl.1
Natural variantiVAR_006715425R → C in FA2D; Quick-1. 1 PublicationCorresponds to variant dbSNP:rs121918479EnsemblClinVar.1
Natural variantiVAR_006716431R → H in FA2D; Himi-2. 1 PublicationCorresponds to variant dbSNP:rs121918482EnsemblClinVar.1
Natural variantiVAR_006717461R → W in FA2D; Tokushima. 3 PublicationsCorresponds to variant dbSNP:rs121918478EnsemblClinVar.1
Natural variantiVAR_006718509E → A in FA2D; Salakta/Frankfurt. 2 Publications