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P18292 (THRB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prothrombin

EC=3.4.21.5
Alternative name(s):
Coagulation factor II
Gene names
Name:F2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

Inhibited by SERPINA5 By similarity.

Subunit structure

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

Post-translational modification

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 By similarity.

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.

The peptide TP508 is able to accelerate repair of both soft and hard tissues.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 2 kringle domains.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4319
PRO_0000028177
Chain44 – 617574Prothrombin
PRO_0000028178
Peptide44 – 200157Activation peptide fragment 1
PRO_0000028179
Peptide201 – 323123Activation peptide fragment 2
PRO_0000028180
Chain324 – 35936Thrombin light chain
PRO_0000028181
Chain360 – 617258Thrombin heavy chain
PRO_0000028182

Regions

Domain44 – 9047Gla
Domain109 – 18779Kringle 1
Domain215 – 29278Kringle 2
Domain360 – 614255Peptidase S1
Region547 – 56923High affinity receptor-binding region which is also known as the TP508 peptide

Sites

Active site4021Charge relay system By similarity
Active site4581Charge relay system By similarity
Active site5641Charge relay system By similarity
Site200 – 2012Cleavage; by thrombin
Site323 – 3242Cleavage; by factor Xa
Site359 – 3602Cleavage; by factor Xa

Amino acid modifications

Modified residue5014-carboxyglutamate By similarity
Modified residue5114-carboxyglutamate By similarity
Modified residue5814-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6314-carboxyglutamate By similarity
Modified residue6414-carboxyglutamate By similarity
Modified residue6914-carboxyglutamate By similarity
Modified residue7014-carboxyglutamate By similarity
Modified residue7314-carboxyglutamate By similarity
Modified residue7614-carboxyglutamate By similarity
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 66 By similarity
Disulfide bond91 ↔ 104 By similarity
Disulfide bond109 ↔ 187 By similarity
Disulfide bond130 ↔ 170 By similarity
Disulfide bond158 ↔ 182 By similarity
Disulfide bond215 ↔ 292 By similarity
Disulfide bond236 ↔ 276 By similarity
Disulfide bond264 ↔ 287 By similarity
Disulfide bond332 ↔ 478Interchain (between light and heavy chains) By similarity
Disulfide bond387 ↔ 403 By similarity
Disulfide bond532 ↔ 546 By similarity
Disulfide bond560 ↔ 590 By similarity

Sequences

Sequence LengthMass (Da)Tools
P18292 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: AD27D1B71445DB1D

FASTA61770,412
        10         20         30         40         50         60 
MLHVRGLGLP GCLALAALAS LVHSQHVFLA PQQALSLLQR VRRANSGFLE ELRKGNLERE 

        70         80         90        100        110        120 
CVEEQCSYEE AFEALESPQD TDVFWAKYTV CDSVRKPRET FMDCLEGRCA MDLGLNYHGN 

       130        140        150        160        170        180 
VSVTHTGIEC QLWRSRYPHR PDINSTTHPG ADLKENFCRN PDSSTSGPWC YTTDPTVRRE 

       190        200        210        220        230        240 
ECSIPVCGQE GRTTVKMTPR SRGSKENLSP PLGECLLERG RLYQGNLAVT TLGSPCLAWD 

       250        260        270        280        290        300 
SLPTKTLSKY QNFDPEVKLV QNFCRNPDRD EEGAWCFVAQ QPGFEYCSLN YCDEAVGEEN 

       310        320        330        340        350        360 
HDGDESIAGR TTDAEFHTFF DERTFGLGEA DCGLRPLFEK KSLTDKTEKE LLDSYIDGRI 

       370        380        390        400        410        420 
VEGWDAEKGI APWQVMLFRK SPQELLCGAS LISDRWVLTA AHCILYPPWD KNFTENDLLV 

       430        440        450        460        470        480 
RIGKHSRTRY ERNVEKISML EKIYIHPRYN WRENLDRDIA LLKLKKPVPF SDYIHPVCLP 

       490        500        510        520        530        540 
DKQTVTSLLQ AGYKGRVTGW GNLRETWTTN INEIQPSVLQ VVNLPIVERP VCKASTRIRI 

       550        560        570        580        590        600 
TDNMFCAGFK VNDTKRGDAC EGDSGGPFVM KSPYNHRWYQ MGIVSWGEGC DRNGKYGFYT 

       610 
HVFRLKRWMQ KVIDQHR 

« Hide

References

[1]"cDNA sequence of rat prothrombin."
Dihanich M., Monard D.
Nucleic Acids Res. 18:4251-4251(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"Partial characterization of vertebrate prothrombin cDNAs: amplification and sequence analysis of the B chain of thrombin from nine different species."
Banfield D.K., Macgillivray R.T.
Proc. Natl. Acad. Sci. U.S.A. 89:2779-2783(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 383-617.
Tissue: Liver.
[3]"Enhancement of incisional wound healing and neovascularization in normal rats by thrombin and synthetic thrombin receptor-activating peptides."
Carney D.H., Mann R., Redin W.R., Pernia S.D., Berry D., Heggers J.P., Hayward P.G., Robson M.C., Christie J., Annable C., Fenton W.J. II, Glenn K.C.
J. Clin. Invest. 89:1469-1477(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE TP508 PEPTIDE.
[4]"Thrombin peptide (TP508) promotes fracture repair by up-regulating inflammatory mediators, early growth factors, and increasing angiogenesis."
Wang H., Li X., Tomin E., Doty S.B., Lane J.M., Carney D.H., Ryaby J.T.
J. Orthop. Res. 23:671-679(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE TP508 PEPTIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52835 Transcribed RNA. Translation: CAA37017.1.
M81397 mRNA. Translation: AAA42240.1.
PIRS10511.
UniGeneRn.54498.

3D structure databases

ProteinModelPortalP18292.
SMRP18292. Positions 44-190, 209-615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000022233.

Chemistry

BindingDBP18292.
ChEMBLCHEMBL3078.

Protein family/group databases

MEROPSS01.217.

PTM databases

PhosphoSiteP18292.

Proteomic databases

PaxDbP18292.
PRIDEP18292.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:61996. rat.

Organism-specific databases

RGD61996. F2.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251824.
HOVERGENHBG108381.
InParanoidP18292.
PhylomeDBP18292.

Gene expression databases

GenevestigatorP18292.

Family and domain databases

Gene3D2.40.20.10. 2 hits.
4.10.140.10. 1 hit.
4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR003966. Prothrombin/thrombin.
IPR018992. Thrombin_light_chain.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00594. Gla. 1 hit.
PF00051. Kringle. 2 hits.
PF09396. Thrombin_light. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001149. Thrombin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
PR01505. PROTHROMBIN.
SMARTSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEPS00011. 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]
ProtoNetSearch...

Other

PMAP-CutDBP18292.
PROP18292.

Entry information

Entry nameTHRB_RAT
AccessionPrimary (citable) accession number: P18292
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries