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Protein

Prothrombin

Gene

F2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. EC:3.4.21.5

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei409Charge relay system1
Active sitei465Charge relay system1
Active sitei571Charge relay system1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.5 908

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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)
R-BTA-977606 Regulation of Complement cascade

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S01.217

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Prothrombin (EC:3.4.21.5)
Alternative name(s):
Coagulation factor II
Cleaved into the following 4 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:F2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:28682 F2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
1245 Bos d Thrombin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4471

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002815325 – 431 PublicationAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002815444 – 625ProthrombinAdd BLAST582
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei504-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei514-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei584-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi120N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi130 ↔ 170
Glycosylationi144N-linked (GlcNAc...) asparagine2 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...) asparagine1 Publication1
Disulfide bondi539 ↔ 553
Disulfide bondi567 ↔ 597

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P00735

PeptideAtlas

More...
PeptideAtlasi
P00735

PRoteomics IDEntifications database

More...
PRIDEi
P00735

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
517

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00735

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P00735

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P00735

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000007148 Expressed in 10 organ(s), highest expression level in liver

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
coaQ4W8J92EBI-990806,EBI-990838From Staphylococcus aureus.

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-6099N

Protein interaction database and analysis system

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IntActi
P00735, 1 interactor

STRING: functional protein association networks

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STRINGi
9913.ENSBTAP00000009406

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P00735

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1625
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P00735

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P00735

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00735

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni554 – 576High affinity receptor-binding region which is also known as the TP508 peptideBy similarityAdd BLAST23

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IKPN Eukaryota
COG5640 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154234

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000251824

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG108381

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P00735

KEGG Orthology (KO)

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KOi
K01313

Identification of Orthologs from Complete Genome Data

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OMAi
GMNYRGN

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0AH5

TreeFam database of animal gene trees

More...
TreeFami
TF327329

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00108 KR, 2 hits
cd00190 Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.40.20.10, 2 hits
4.10.140.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

The PANTHER Classification System

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PANTHERi
PTHR24254:SF10 PTHR24254:SF10, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00594 Gla, 1 hit
PF00051 Kringle, 2 hits
PF09396 Thrombin_light, 1 hit
PF00089 Trypsin, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001149 Thrombin, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
PR01505 PROTHROMBIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00069 GLA, 1 hit
SM00130 KR, 2 hits
SM00020 Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits
SSF57630 SSF57630, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i95AFF17C23AD78F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti600D → N. 1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
V00135 mRNA Translation: CAA23451.1
J00041 mRNA Translation: AAA30781.1
BC105201 mRNA Translation: AAI05202.1

Protein sequence database of the Protein Information Resource

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PIRi
S02537 TBBO

NCBI Reference Sequences

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RefSeqi
NP_776302.1, NM_173877.1
XP_015330343.1, XM_015474857.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Bt.29855

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSBTAT00000009406; ENSBTAP00000009406; ENSBTAG00000007148

Database of genes from NCBI RefSeq genomes

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GeneIDi
280685

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
bta:280685

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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
STRINGi9913.ENSBTAP00000009406

Chemistry databases

BindingDBiP00735
ChEMBLiCHEMBL4471

Protein family/group databases

Allergomei1245 Bos d Thrombin
MEROPSiS01.217

PTM databases

GlyConnecti517
iPTMnetiP00735
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

Comparative Toxicogenomics Database

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CTDi
2147
VGNCiVGNC:28682 F2

Phylogenomic databases

eggNOGiENOG410IKPN Eukaryota
COG5640 LUCA
GeneTreeiENSGT00940000154234
HOGENOMiHOG000251824
HOVERGENiHBG108381
InParanoidiP00735
KOiK01313
OMAiGMNYRGN
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)
R-BTA-977606 Regulation of Complement cascade

Miscellaneous databases

EvolutionaryTraceiP00735
PMAP-CutDBiP00735

Protein Ontology

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PROi
PR:P00735

Gene expression databases

BgeeiENSBTAG00000007148 Expressed in 10 organ(s), highest expression level in liver

Family and domain databases

CDDicd00108 KR, 2 hits
cd00190 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTHRB_BOVIN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P00735
Secondary accession number(s): Q3MHK7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1990
Last modified: December 5, 2018
This is version 205 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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. SIMILARITY comments
    Index of protein domains and families
  3. Peptidase families
    Classification of peptidase families and list of entries
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