ID   THRB_SALSA              Reviewed;          36 AA.
AC   P84122;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Thrombin;
DE            EC=3.4.21.5;
DE   Contains:
DE     RecName: Full=Thrombin light chain;
DE   Contains:
DE     RecName: Full=Thrombin heavy chain;
DE   Flags: Fragments;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15236909; DOI=10.1016/j.jbbm.2004.04.016;
RA   Manseth E., Skjervold P.O., Flengsrud R.;
RT   "Sample displacement chromatography of Atlantic Salmon (Salmo salar)
RT   thrombin.";
RL   J. Biochem. Biophys. Methods 60:39-47(2004).
CC   -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts
CC       fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in
CC       complex with thrombomodulin, protein C. Functions in blood homeostasis,
CC       inflammation and wound healing (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
CC         fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
CC         Evidence={ECO:0000269|PubMed:15236909};
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterodimer with SERPINA5. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15236909}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC       {ECO:0000269|PubMed:15236909}.
CC   -!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions,
CC       result from the carboxylation of glutamyl residues by a microsomal
CC       enzyme, the vitamin K-dependent carboxylase. The modified residues are
CC       necessary for the calcium-dependent interaction with a negatively
CC       charged phospholipid surface, which is essential for the conversion of
CC       prothrombin to thrombin. {ECO:0000305}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Prothrombin is activated on the surface of a
CC       phospholipid membrane that binds the amino end of prothrombin and
CC       factors Va and Xa in Ca-dependent interactions; factor Xa removes the
CC       activation peptide and cleaves the remaining part into light and heavy
CC       chains. The activation process starts slowly because factor V itself
CC       has to be activated by the initial, small amounts of thrombin.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
CC       (fragment 1) of the prothrombin, prior to its activation by factor Xa.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   Proteomes; UP000087266; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Blood coagulation; Calcium; Direct protein sequencing;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease.
FT   CHAIN           1..18
FT                   /note="Thrombin light chain"
FT                   /evidence="ECO:0000303|PubMed:15236909"
FT                   /id="PRO_0000028183"
FT   CHAIN           19..36
FT                   /note="Thrombin heavy chain"
FT                   /evidence="ECO:0000303|PubMed:15236909"
FT                   /id="PRO_0000028184"
FT   DOMAIN          <19..>36
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000303|PubMed:15236909"
FT   NON_TER         36
FT                   /evidence="ECO:0000303|PubMed:15236909"
SQ   SEQUENCE   36 AA;  3784 MW;  E451D38AE5FCA666 CRC64;
     SFGSGELVXG EXPXFEKIIV KGIDAEVASA PMQVML