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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)DescriptionActionsGraphical viewLength
Active sitei409Charge relay system1
Active sitei465Charge relay system1
Active sitei571Charge relay system1

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 databases

ChEMBLiCHEMBL4471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002815325 – 431 PublicationAdd BLAST19
ChainiPRO_000002815444 – 625ProthrombinAdd BLAST582
PeptideiPRO_000002815544 – 199Activation peptide fragment 1Add BLAST156
PeptideiPRO_0000028156200 – 317Activation peptide fragment 2Add BLAST118
ChainiPRO_0000028157318 – 366Thrombin light chainAdd BLAST49
ChainiPRO_0000028158367 – 625Thrombin heavy chainAdd BLAST259

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei504-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei514-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei584-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi61 ↔ 66
Modified residuei634-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei644-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei704-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei734-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi91 ↔ 104
Disulfide bondi109 ↔ 187
Glycosylationi120N-linked (GlcNAc...)2 Publications1
Disulfide bondi130 ↔ 170
Glycosylationi144N-linked (GlcNAc...)2 Publications1
Disulfide bondi158 ↔ 182
Disulfide bondi214 ↔ 292
Disulfide bondi235 ↔ 275
Disulfide bondi263 ↔ 287
Disulfide bondi339 ↔ 485Interchain (between light and heavy chains)
Disulfide bondi394 ↔ 410
Glycosylationi419N-linked (GlcNAc...)1 Publication1
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)DescriptionActionsGraphical viewLength
Sitei199 – 200Cleavage; by thrombin2
Sitei317 – 318Cleavage; by factor Xa2
Sitei366 – 367Cleavage; by factor Xa2

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.

Gene expression databases

BgeeiENSBTAG00000007148.

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 interactor.
MINTiMINT-1504393.
STRINGi9913.ENSBTAP00000009406.

Chemistry databases

BindingDBiP00735.

Structurei

Secondary structure

1625
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 49Combined sources3
Helixi50 – 52Combined sources3
Helixi57 – 61Combined sources5
Helixi68 – 74Combined sources7
Helixi78 – 90Combined sources13
Turni91 – 93Combined sources3
Helixi98 – 106Combined sources9
Beta strandi108 – 110Combined sources3
Turni112 – 114Combined sources3
Beta strandi125 – 127Combined sources3
Beta strandi137 – 139Combined sources3
Turni145 – 147Combined sources3
Beta strandi149 – 151Combined sources3
Beta strandi168 – 174Combined sources7
Beta strandi179 – 181Combined sources3
Beta strandi185 – 189Combined sources5
Beta strandi192 – 194Combined sources3
Helixi217 – 219Combined sources3
Beta strandi238 – 240Combined sources3
Helixi243 – 246Combined sources4
Beta strandi248 – 250Combined sources3
Beta strandi254 – 256Combined sources3
Beta strandi274 – 276Combined sources3
Beta strandi278 – 280Combined sources3
Beta strandi284 – 286Combined sources3
Beta strandi291 – 293Combined sources3
Beta strandi310 – 313Combined sources4
Beta strandi321 – 323Combined sources3
Helixi329 – 332Combined sources4
Turni337 – 340Combined sources4
Turni343 – 345Combined sources3
Helixi346 – 348Combined sources3
Helixi355 – 362Combined sources8
Beta strandi370 – 372Combined sources3
Beta strandi375 – 377Combined sources3
Beta strandi381 – 386Combined sources6
Turni387 – 390Combined sources4
Beta strandi391 – 400Combined sources10
Beta strandi403 – 406Combined sources4
Helixi408 – 410Combined sources3
Helixi414 – 416Combined sources3
Beta strandi424 – 430Combined sources7
Beta strandi433 – 436Combined sources4
Turni439 – 441Combined sources3
Beta strandi443 – 445Combined sources3
Beta strandi447 – 452Combined sources6
Turni458 – 461Combined sources4
Beta strandi467 – 473Combined sources7
Helixi489 – 495Combined sources7
Beta strandi501 – 506Combined sources6
Beta strandi510 – 513Combined sources4
Beta strandi516 – 518Combined sources3
Beta strandi520 – 522Combined sources3
Beta strandi527 – 533Combined sources7
Helixi536 – 541Combined sources6
Beta strandi543 – 545Combined sources3
Beta strandi551 – 554Combined sources4
Helixi558 – 560Combined sources3
Turni568 – 572Combined sources5
Beta strandi574 – 578Combined sources5
Turni580 – 582Combined sources3
Beta strandi585 – 591Combined sources7
Beta strandi595 – 598Combined sources4
Beta strandi604 – 608Combined sources5
Turni609 – 612Combined sources4
Helixi613 – 621Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00735.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 90GlaPROSITE-ProRule annotationAdd BLAST47
Domaini109 – 187Kringle 1PROSITE-ProRule annotationAdd BLAST79
Domaini214 – 292Kringle 2PROSITE-ProRule annotationAdd BLAST79
Domaini367 – 621Peptidase S1PROSITE-ProRule annotationAdd BLAST255

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni554 – 576High affinity receptor-binding region which is also known as the TP508 peptideBy similarityAdd BLAST23

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.
OrthoDBiEOG091G0AH5.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti231S → H in AAA30781 (PubMed:6326805).Curated1
Sequence conflicti249D → H in AAA30781 (PubMed:6326805).Curated1
Sequence conflicti288D → N AA sequence (Ref. 4) Curated1
Sequence conflicti353Q → E AA sequence (Ref. 4) Curated1
Sequence conflicti355E → Q AA sequence (Ref. 4) Curated1
Sequence conflicti358L → P in AAI05202 (Ref. 3) Curated1
Sequence conflicti549 – 550DN → ND AA sequence (Ref. 4) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti600D → N.1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

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.
OrthoDBiEOG091G0AH5.
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.

Gene expression databases

BgeeiENSBTAG00000007148.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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.
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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: November 2, 2016
This is version 191 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.