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Reviewed, UniProtKB/Swiss-Prot Q5R537 (THRB_PONAB)

Last modified January 19, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Prothrombin
    EC=3.4.21.5
Alternative name(s):
    Coagulation factor II
Cleaved into the following 4 chains:
    1- Recommended name:
            Activation peptide fragment 1
    2- Recommended name:
            Activation peptide fragment 2
    3- Recommended name:
            Thrombin light chain
    4- Recommended name:
            Thrombin heavy chain
Gene names
Name: F2
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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 By similarity.

Catalytic activity

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

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 By similarity.

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

Sequence similarities

Belongs to the peptidase S1 family.

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

Contains 2 kringle domains.

Contains 1 peptidase S1 domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4319 By similarity
PRO_0000028171
Chain44 – 623580Prothrombin
PRO_0000028172
Peptide44 – 199156Activation peptide fragment 1 By similarity
PRO_0000028173
Peptide200 – 328129Activation peptide fragment 2 By similarity
PRO_0000028174
Chain329 – 36436Thrombin light chain By similarity
PRO_0000028175
Chain365 – 622258Thrombin heavy chain By similarity
PRO_0000028176

Regions

Domain44 – 9047Gla
Domain108 – 18780Kringle 1
Domain213 – 29280Kringle 2
Domain365 – 619255Peptidase S1
Region552 – 57423High affinity receptor-binding region which also known as the TP508 peptide By similarity

Sites

Active site4071Charge relay system By similarity
Active site4631Charge relay system By similarity
Active site5691Charge relay system By similarity
Site199 – 2002Cleavage; by thrombin By similarity
Site328 – 3292Cleavage; by factor Xa By similarity
Site364 – 3652Cleavage; by factor Xa By similarity

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
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation4171N-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 bond214 ↔ 292 By similarity
Disulfide bond235 ↔ 275 By similarity
Disulfide bond263 ↔ 287 By similarity
Disulfide bond337 ↔ 483Interchain (between light and heavy chains) By similarity
Disulfide bond392 ↔ 408 By similarity
Disulfide bond537 ↔ 551 By similarity
Disulfide bond565 ↔ 595 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5R537-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6E89738B07AA8F87

FASTA62370,010
        10         20         30         40         50         60 
MAHVRGLQLP GCLALAALCT LVHSQHVFLA PQQALSLLQR VRRANSVFLE EVRKGNLERE 

        70         80         90        100        110        120 
CVEETCSYEE AFEALESSTA TDVFWAKYTA CETARTPRDK LAACLEGNCA EGLGTNYRGH 

       130        140        150        160        170        180 
LNITQSGIQC QLWRSRYPHK PEINSTTHPG ADLQENFCRN PDSSTTGPWC YTTDPTVRRQ 

       190        200        210        220        230        240 
ECSIPVCGQD QVTVAMTPRS EGSGVNLSPP SEQCVPDRGQ QYQGRLAVTT HGLPCLAWAS 

       250        260        270        280        290        300 
AQAKALSKHQ DFNSAVQLVE NFCRNPDGDE EGVWCYVAGK PGDFGYCDLN YCEEAMEEET 

       310        320        330        340        350        360 
GGGLDEDPDR AIEGRTATSE YQTFFDPRTF GSGEADCGLR PLFEKKSLED KTERELLESY 

       370        380        390        400        410        420 
IDGRIVEGSD AEIGMSPWQV MLFRKSPQEL LCGATLISDR WVLTAAHCLL YPPWDKNFTE 

       430        440        450        460        470        480 
NDLLVRIGKH SRTRYERNIE KISMLEKIYI HPRYNWRENL DRDIALMKLK KPVAFSDYIH 

       490        500        510        520        530        540 
PVCLPDRETA ASLLQAGYKG RVTGWGNLKE TWTANVGKVQ PSVLQVVNLP IVERPVCKDS 

       550        560        570        580        590        600 
TRIRITDNMF CAGYKPDEGK RGDACEGDSG GPFVMKSPFN NCWYQMGIVS WGEGCDRDGK 

       610        620 
YGFYTHVFRL KKWIQKVIDQ FGE

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR861038 mRNA. Translation: CAH93129.1.
RefSeqNP_001126851.1.
UniGenePab.147
Pab.18566

3D structure databases

SMRQ5R537. Positions 44-190, 79-199, 152-297, 208-364, 329-623.
ModBaseSearch...

Genome annotation databases

GeneID100173859.

Organism-specific databases

CTD100173859.

Phylogenomic databases

HOVERGENQ5R537.
InParanoidQ5R537.

Enzyme and pathway databases

BRENDA3.4.21.5. 269192.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla_dom.
IPR000294. GLA_domain.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR012051. Peptidase_S1A_pr.
IPR003966. Peptidase_S1A_prothrombin.
IPR009003. Ser/Cys_Pept_Trypsin-like.
IPR018992. Thrombin_light_chain.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 2 hits.
G3DSA:4.10.140.10. Thrombin_light_chain. 1 hit.
PANTHERPTHR19355:SF61. Peptidase_S1A_pr. 1 hit.
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.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.
SMARTSM00069. GLA. 1 hit.
SM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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...

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Entry information

Entry nameTHRB_PONAB
AccessionPrimary (citable) accession number: Q5R537
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: December 21, 2004
Last modified: January 19, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents