Reviewed, UniProtKB/Swiss-Prot P84122 (THRB_SALSA)

Names and origin

Protein names	Recommended name:     Thrombin     EC=3.4.21.5 Cleaved into the following 2 chains:     1- Recommended name:             Thrombin light chain     2- Recommended name:             Thrombin heavy chain
Organism	Salmo salar (Atlantic salmon)
Taxonomic identifier	8030 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonidae › Salmoninae › Salmo

Protein attributes

Sequence length	36 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. Ref.1
Subcellular location	Secreted. Ref.1
Tissue specificity	Expressed by the liver and secreted in plasma. Ref.1
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. N-glycosylated 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.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Gamma-carboxyglutamic acid Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 18	18	Thrombin light chain Ref.1		PRO_0000028183
	Chain	19 – 36	18	Thrombin heavy chain Ref.1		PRO_0000028184
Regions
	Domain	‹19 – ›36	›18	Peptidase S1
Experimental info
	Non-adjacent residues	18 – 19	2
	Non-terminal residue	36	1

Sequences

	Sequence		Length	Mass (Da)
	P84122-1 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: E451D38AE5FCA666	FASTA	36	3,784
	10 20 30 SFGSGELVXG EXPXFEKIIV KGIDAEVASA PMQVML

References

[1]	"Sample displacement chromatography of Atlantic Salmon (Salmo salar) thrombin." Manseth E., Skjervold P.O., Flengsrud R. J. Biochem. Biophys. Methods 60:39-47(2004) [PubMed: 15236909] [Abstract] Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P84122.
Enzyme and pathway databases
BRENDA	3.4.21.5. 39345.
Family and domain databases
InterPro	IPR000294. GLA_domain. IPR018056. Kringle_CS. IPR018114. Peptidase_S1/S6_AS. IPR012051. Peptidase_S1A_pr. [Graphical view]
PANTHER	PTHR19355:SF61. Peptidase_S1A_pr. 1 hit.
PROSITE	PS00011. GLA_1. Partial match. PS50998. GLA_2. Partial match. PS00021. KRINGLE_1. Partial match. PS50070. KRINGLE_2. Partial match. PS50240. TRYPSIN_DOM. Partial match. PS00134. TRYPSIN_HIS. Partial match. PS00135. TRYPSIN_SER. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THRB_SALSA

Accession

Primary (citable) accession number: P84122

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	August 31, 2004
Last modified:	June 16, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)