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Protein

Prothrombin

Gene

F2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei409 – 4091Charge relay system
Active sitei465 – 4651Charge relay system
Active sitei571 – 5711Charge relay system

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • fibrinogen binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: BHF-UCL
  • thrombospondin receptor activity Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Acute phase, Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BRENDAi3.4.21.5. 908.
ReactomeiR-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-BTA-202733. Cell surface interactions at the vascular wall.
R-BTA-375276. Peptide ligand-binding receptors.
R-BTA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-BTA-416476. G alpha (q) signalling events.
R-BTA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-BTA-76009. Platelet Aggregation (Plug Formation).

Protein family/group databases

MEROPSiS01.217.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei1245. Bos d Thrombin.

Chemistry

ChEMBLiCHEMBL4471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 43191 PublicationPRO_0000028153Add
BLAST
Chaini44 – 625582ProthrombinPRO_0000028154Add
BLAST
Peptidei44 – 199156Activation peptide fragment 1PRO_0000028155Add
BLAST
Peptidei200 – 317118Activation peptide fragment 2PRO_0000028156Add
BLAST
Chaini318 – 36649Thrombin light chainPRO_0000028157Add
BLAST
Chaini367 – 625259Thrombin heavy chainPRO_0000028158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 5014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei51 – 5114-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei58 – 5814-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi61 ↔ 66
Modified residuei63 – 6314-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei64 – 6414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei70 – 7014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi91 ↔ 104
Disulfide bondi109 ↔ 187
Glycosylationi120 – 1201N-linked (GlcNAc...)2 Publications
Disulfide bondi130 ↔ 170
Glycosylationi144 – 1441N-linked (GlcNAc...)2 Publications
Disulfide bondi158 ↔ 182
Disulfide bondi214 ↔ 292
Disulfide bondi235 ↔ 275
Disulfide bondi263 ↔ 287
Disulfide bondi339 ↔ 485Interchain (between light and heavy chains)
Disulfide bondi394 ↔ 410
Glycosylationi419 – 4191N-linked (GlcNAc...)1 Publication
Disulfide bondi539 ↔ 553
Disulfide bondi567 ↔ 597

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei199 – 2002Cleavage; by thrombin
Sitei317 – 3182Cleavage; by factor Xa
Sitei366 – 3672Cleavage; by factor Xa

Keywords - PTMi

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

Proteomic databases

PaxDbiP00735.
PeptideAtlasiP00735.
PRIDEiP00735.

PTM databases

UniCarbKBiP00735.

Miscellaneous databases

PMAP-CutDBP00735.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
coaQ4W8J92EBI-990806,EBI-990838From a different organism.

GO - Molecular functioni

  • fibrinogen binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-6099N.
IntActiP00735. 1 interaction.
MINTiMINT-1504393.
STRINGi9913.ENSBTAP00000009406.

Chemistry

BindingDBiP00735.

Structurei

Secondary structure

1
625
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 493Combined sources
Helixi50 – 523Combined sources
Helixi57 – 615Combined sources
Helixi68 – 747Combined sources
Helixi78 – 9013Combined sources
Turni91 – 933Combined sources
Helixi98 – 1069Combined sources
Beta strandi108 – 1103Combined sources
Turni112 – 1143Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi137 – 1393Combined sources
Turni145 – 1473Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi168 – 1747Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi192 – 1943Combined sources
Helixi217 – 2193Combined sources
Beta strandi238 – 2403Combined sources
Helixi243 – 2464Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi274 – 2763Combined sources
Beta strandi278 – 2803Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi310 – 3134Combined sources
Beta strandi321 – 3233Combined sources
Helixi329 – 3324Combined sources
Turni337 – 3404Combined sources
Turni343 – 3453Combined sources
Helixi346 – 3483Combined sources
Helixi355 – 3628Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi381 – 3866Combined sources
Turni387 – 3904Combined sources
Beta strandi391 – 40010Combined sources
Beta strandi403 – 4064Combined sources
Helixi408 – 4103Combined sources
Helixi414 – 4163Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi433 – 4364Combined sources
Turni439 – 4413Combined sources
Beta strandi443 – 4453Combined sources
Beta strandi447 – 4526Combined sources
Turni458 – 4614Combined sources
Beta strandi467 – 4737Combined sources
Helixi489 – 4957Combined sources
Beta strandi501 – 5066Combined sources
Beta strandi510 – 5134Combined sources
Beta strandi516 – 5183Combined sources
Beta strandi520 – 5223Combined sources
Beta strandi527 – 5337Combined sources
Helixi536 – 5416Combined sources
Beta strandi543 – 5453Combined sources
Beta strandi551 – 5544Combined sources
Helixi558 – 5603Combined sources
Turni568 – 5725Combined sources
Beta strandi574 – 5785Combined sources
Turni580 – 5823Combined sources
Beta strandi585 – 5917Combined sources
Beta strandi595 – 5984Combined sources
Beta strandi604 – 6085Combined sources
Turni609 – 6124Combined sources
Helixi613 – 6219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0HX-ray3.20A/D208-366[»]
B/E367-625[»]
1AVGX-ray2.60H367-625[»]
L326-366[»]
1BBRX-ray2.30E517-625[»]
H367-515[»]
J/L/M318-366[»]
K/N367-625[»]
1ETRX-ray2.20H367-625[»]
L318-366[»]
1ETSX-ray2.30H367-625[»]
L318-366[»]
1ETTX-ray2.50H367-625[»]
L318-366[»]
1HRTX-ray2.80H367-625[»]
L318-366[»]
1ID5X-ray2.50H367-622[»]
L318-366[»]
1MKWX-ray2.30H367-625[»]
K318-625[»]
L318-366[»]
1MKXX-ray2.20H367-625[»]
K318-625[»]
L318-366[»]
1NL1X-ray1.90A44-190[»]
1NL2X-ray2.30A44-189[»]
1TBQX-ray3.10H/K367-625[»]
J/L318-366[»]
1TBRX-ray2.60H/K367-625[»]
J/L318-366[»]
1TOCX-ray3.10A/C/E/G318-366[»]
B/D/F/H367-625[»]
1UCYX-ray2.20E517-625[»]
H367-516[»]
J/L/M318-366[»]
K/N367-625[»]
1UVTX-ray2.50H367-625[»]
L318-366[»]
1UVUX-ray2.80H367-625[»]
L318-366[»]
1VITX-ray3.20F367-516[»]
G517-625[»]
H367-625[»]
L/M318-366[»]
1YCPX-ray2.50H367-625[»]
J/L318-366[»]
K367-516[»]
M517-625[»]
2A1DX-ray3.50A/E326-366[»]
B/F367-625[»]
2HPPX-ray3.30P214-292[»]
2ODYX-ray2.35A/C318-366[»]
B/D367-625[»]
2PF1X-ray2.80A44-199[»]
2PF2X-ray2.20A44-199[»]
2SPTX-ray2.50A44-188[»]
3PMAX-ray2.20A/C336-364[»]
B/D367-625[»]
3PMBX-ray2.90A/C336-364[»]
B/D367-625[»]
ProteinModelPortaliP00735.
SMRiP00735. Positions 44-199, 208-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00735.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 9047GlaPROSITE-ProRule annotationAdd
BLAST
Domaini109 – 18779Kringle 1PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 29279Kringle 2PROSITE-ProRule annotationAdd
BLAST
Domaini367 – 621255Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni554 – 57623High affinity receptor-binding region which is also known as the TP508 peptideBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 2 kringle domains.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IKPN. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000251824.
HOVERGENiHBG108381.
InParanoidiP00735.
KOiK01313.
OMAiGIECQLW.
OrthoDBiEOG767394.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.140.10. 1 hit.
4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR003966. Prothrombin/thrombin.
IPR018992. Thrombin_light_chain.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24254:SF10. PTHR24254:SF10. 1 hit.
PfamiPF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001149. Thrombin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR01505. PROTHROMBIN.
SMARTiSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00011. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARVRGPRLP GCLALAALFS LVHSQHVFLA HQQASSLLQR ARRANKGFLE
60 70 80 90 100
EVRKGNLERE CLEEPCSREE AFEALESLSA TDAFWAKYTA CESARNPREK
110 120 130 140 150
LNECLEGNCA EGVGMNYRGN VSVTRSGIEC QLWRSRYPHK PEINSTTHPG
160 170 180 190 200
ADLRENFCRN PDGSITGPWC YTTSPTLRRE ECSVPVCGQD RVTVEVIPRS
210 220 230 240 250
GGSTTSQSPL LETCVPDRGR EYRGRLAVTT SGSRCLAWSS EQAKALSKDQ
260 270 280 290 300
DFNPAVPLAE NFCRNPDGDE EGAWCYVADQ PGDFEYCDLN YCEEPVDGDL
310 320 330 340 350
GDRLGEDPDP DAAIEGRTSE DHFQPFFNEK TFGAGEADCG LRPLFEKKQV
360 370 380 390 400
QDQTEKELFE SYIEGRIVEG QDAEVGLSPW QVMLFRKSPQ ELLCGASLIS
410 420 430 440 450
DRWVLTAAHC LLYPPWDKNF TVDDLLVRIG KHSRTRYERK VEKISMLDKI
460 470 480 490 500
YIHPRYNWKE NLDRDIALLK LKRPIELSDY IHPVCLPDKQ TAAKLLHAGF
510 520 530 540 550
KGRVTGWGNR RETWTTSVAE VQPSVLQVVN LPLVERPVCK ASTRIRITDN
560 570 580 590 600
MFCAGYKPGE GKRGDACEGD SGGPFVMKSP YNNRWYQMGI VSWGEGCDRD
610 620
GKYGFYTHVF RLKKWIQKVI DRLGS
Length:625
Mass (Da):70,506
Last modified:April 1, 1990 - v2
Checksum:i95AFF17C23AD78F9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311S → H in AAA30781 (PubMed:6326805).Curated
Sequence conflicti249 – 2491D → H in AAA30781 (PubMed:6326805).Curated
Sequence conflicti288 – 2881D → N AA sequence (Ref. 4) Curated
Sequence conflicti353 – 3531Q → E AA sequence (Ref. 4) Curated
Sequence conflicti355 – 3551E → Q AA sequence (Ref. 4) Curated
Sequence conflicti358 – 3581L → P in AAI05202 (Ref. 3) Curated
Sequence conflicti549 – 5502DN → ND AA sequence (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti600 – 6001D → N.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00135 mRNA. Translation: CAA23451.1.
J00041 mRNA. Translation: AAA30781.1.
BC105201 mRNA. Translation: AAI05202.1.
PIRiS02537. TBBO.
RefSeqiNP_776302.1. NM_173877.1.
XP_015330343.1. XM_015474857.1.
UniGeneiBt.29855.

Genome annotation databases

EnsembliENSBTAT00000009406; ENSBTAP00000009406; ENSBTAG00000007148.
GeneIDi280685.
KEGGibta:280685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00135 mRNA. Translation: CAA23451.1.
J00041 mRNA. Translation: AAA30781.1.
BC105201 mRNA. Translation: AAI05202.1.
PIRiS02537. TBBO.
RefSeqiNP_776302.1. NM_173877.1.
XP_015330343.1. XM_015474857.1.
UniGeneiBt.29855.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0HX-ray3.20A/D208-366[»]
B/E367-625[»]
1AVGX-ray2.60H367-625[»]
L326-366[»]
1BBRX-ray2.30E517-625[»]
H367-515[»]
J/L/M318-366[»]
K/N367-625[»]
1ETRX-ray2.20H367-625[»]
L318-366[»]
1ETSX-ray2.30H367-625[»]
L318-366[»]
1ETTX-ray2.50H367-625[»]
L318-366[»]
1HRTX-ray2.80H367-625[»]
L318-366[»]
1ID5X-ray2.50H367-622[»]
L318-366[»]
1MKWX-ray2.30H367-625[»]
K318-625[»]
L318-366[»]
1MKXX-ray2.20H367-625[»]
K318-625[»]
L318-366[»]
1NL1X-ray1.90A44-190[»]
1NL2X-ray2.30A44-189[»]
1TBQX-ray3.10H/K367-625[»]
J/L318-366[»]
1TBRX-ray2.60H/K367-625[»]
J/L318-366[»]
1TOCX-ray3.10A/C/E/G318-366[»]
B/D/F/H367-625[»]
1UCYX-ray2.20E517-625[»]
H367-516[»]
J/L/M318-366[»]
K/N367-625[»]
1UVTX-ray2.50H367-625[»]
L318-366[»]
1UVUX-ray2.80H367-625[»]
L318-366[»]
1VITX-ray3.20F367-516[»]
G517-625[»]
H367-625[»]
L/M318-366[»]
1YCPX-ray2.50H367-625[»]
J/L318-366[»]
K367-516[»]
M517-625[»]
2A1DX-ray3.50A/E326-366[»]
B/F367-625[»]
2HPPX-ray3.30P214-292[»]
2ODYX-ray2.35A/C318-366[»]
B/D367-625[»]
2PF1X-ray2.80A44-199[»]
2PF2X-ray2.20A44-199[»]
2SPTX-ray2.50A44-188[»]
3PMAX-ray2.20A/C336-364[»]
B/D367-625[»]
3PMBX-ray2.90A/C336-364[»]
B/D367-625[»]
ProteinModelPortaliP00735.
SMRiP00735. Positions 44-199, 208-621.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6099N.
IntActiP00735. 1 interaction.
MINTiMINT-1504393.
STRINGi9913.ENSBTAP00000009406.

Chemistry

BindingDBiP00735.
ChEMBLiCHEMBL4471.

Protein family/group databases

Allergomei1245. Bos d Thrombin.
MEROPSiS01.217.

PTM databases

UniCarbKBiP00735.

Proteomic databases

PaxDbiP00735.
PeptideAtlasiP00735.
PRIDEiP00735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009406; ENSBTAP00000009406; ENSBTAG00000007148.
GeneIDi280685.
KEGGibta:280685.

Organism-specific databases

CTDi2147.

Phylogenomic databases

eggNOGiENOG410IKPN. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000251824.
HOVERGENiHBG108381.
InParanoidiP00735.
KOiK01313.
OMAiGIECQLW.
OrthoDBiEOG767394.
TreeFamiTF327329.

Enzyme and pathway databases

BRENDAi3.4.21.5. 908.
ReactomeiR-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
R-BTA-202733. Cell surface interactions at the vascular wall.
R-BTA-375276. Peptide ligand-binding receptors.
R-BTA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-BTA-416476. G alpha (q) signalling events.
R-BTA-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-BTA-76009. Platelet Aggregation (Plug Formation).

Miscellaneous databases

EvolutionaryTraceiP00735.
PMAP-CutDBP00735.
PROiP00735.

Family and domain databases

Gene3Di4.10.140.10. 1 hit.
4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR003966. Prothrombin/thrombin.
IPR018992. Thrombin_light_chain.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24254:SF10. PTHR24254:SF10. 1 hit.
PfamiPF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001149. Thrombin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR01505. PROTHROMBIN.
SMARTiSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00011. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and evolution of the bovine prothrombin gene."
    Irwin D.M., Robertson K.A., Macgillivray R.T.A.
    J. Mol. Biol. 200:31-45(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization of bovine prothrombin mRNA and its translation product."
    McGillivray R.T.A., Davie E.W.
    Biochemistry 23:1626-1634(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal liver.
  4. Magnusson S., Sottrup-Jensen L., Petersen T.E., Claeys H.
    (In) Hemker H.C., Veltkamp J.J. (eds.); Boerhaave symposium on prothrombin and related coagulation factors, pp.25-46, Leiden University Press, Leiden (1975)
    Cited for: PROTEIN SEQUENCE OF 44-625, DISULFIDE BONDS, GAMMA-CARBOXYGLUTAMATION AT GLU-50; GLU-51; GLU-58; GLU-60; GLU-63; GLU-64; GLU-69; GLU-70; GLU-73 AND GLU-76, GLYCOSYLATION AT ASN-120; ASN-144 AND ASN-419.
  5. Cited for: GENE STRUCTURE.
  6. "Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1."
    Park C.H., Tulinsky A.
    Biochemistry 25:3977-3982(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
  7. "Structure of bovine prothrombin fragment 1 refined at 2.25-A resolution."
    Seshadri T.-P., Tulinsky A., Skrzypczak-Jankun E., Park C.H.
    J. Mol. Biol. 220:481-494(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF ACTIVATION PEPTIDE 1.
  8. "The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1."
    Soriano-Garcia M., Padmanabhan K., de Vos A.M., Tulinsky A.
    Biochemistry 31:2554-2566(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF ACTIVATION PEPTIDE 1 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-120 AND ASN-144.
  9. "The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution."
    Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.
    J. Biol. Chem. 267:7911-7920(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FIBRINOGEN.
  10. "The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution."
    Vitali J., Martin P.D., Malkowski M.G., Robertson W.D., Lazar J.B., Winant R.C., Johnson P.H., Edwards B.F.P.
    J. Biol. Chem. 267:17670-17678(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 318-625 IN COMPLEX WITH HIRUDIN.
  11. "Refined 2.3 A X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA. A starting point for improving antithrombotics."
    Brandstetter H., Turk D., Hoeffken H.W., Grosse D., Stuerzebecher J., Martin P.D., Edwards B.F.P., Bode W.
    J. Mol. Biol. 226:1085-1099(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  12. "The ornithodorin-thrombin crystal structure, a key to the TAP enigma?"
    van de Locht A., Stubbs M.T., Bode W., Friedrich T., Bollschweiler C., Hoffken W., Huber R.
    EMBO J. 15:6011-6017(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH ORNITHODORIN.
  13. "Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug."
    Fuentes-Prior P., Noeske-Jungblut C., Donner P., Schleuning W.-D., Huber R., Bode W.
    Proc. Natl. Acad. Sci. U.S.A. 94:11845-11850(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH TRIABIN.
  14. "Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins."
    Huang M., Rigby A.C., Morelli X., Grant M.A., Huang G., Furie B., Seaton B., Furie B.C.
    Nat. Struct. Biol. 10:751-756(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 44-190 IN COMPLEX WITH CALCIUM AND LYSOPHOSPHATIDYLSERINE.

Entry informationi

Entry nameiTHRB_BOVIN
AccessioniPrimary (citable) accession number: P00735
Secondary accession number(s): Q3MHK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: July 6, 2016
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.
Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.