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   16-JUN-2009, entry version 33.
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; Euteleostei;
OC   Protacanthopterygii; Salmoniformes; Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
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,
CC       converts fibrinogen to fibrin and activates factors V, VII, VIII,
CC       XIII, and, in complex with thrombomodulin, protein C. Functions in
CC       blood homeostasis, inflammation and wound healing (By similarity).
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in
CC       fibrinogen to form fibrin and release fibrinopeptides A and B.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
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
CC       are necessary for the calcium-dependent interaction with a
CC       negatively charged phospholipid surface, which is essential for
CC       the conversion of prothrombin to thrombin.
CC   -!- PTM: N-glycosylated (By similarity).
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
CC       the activation peptide and cleaves the remaining part into light
CC       and heavy chains. The activation process starts slowly because
CC       factor V itself has to be activated by the initial, small amounts
CC       of thrombin.
CC   -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
CC       (fragment 1) of the prothrombin, prior to its activation by factor
CC       Xa.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR   HOVERGEN; P84122; -.
DR   BRENDA; 3.4.21.5; 39345.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR012051; Peptidase_S1A_pr.
DR   PANTHER; PTHR19355:SF61; Peptidase_S1A_pr; 1.
DR   PROSITE; PS00011; GLA_1; PARTIAL.
DR   PROSITE; PS50998; GLA_2; PARTIAL.
DR   PROSITE; PS00021; KRINGLE_1; PARTIAL.
DR   PROSITE; PS50070; KRINGLE_2; PARTIAL.
DR   PROSITE; PS50240; TRYPSIN_DOM; PARTIAL.
DR   PROSITE; PS00134; TRYPSIN_HIS; PARTIAL.
DR   PROSITE; PS00135; TRYPSIN_SER; PARTIAL.
PE   1: Evidence at protein level;
KW   Blood coagulation; Calcium; Direct protein sequencing;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Serine protease.
FT   CHAIN         1     18       Thrombin light chain.
FT                                /FTId=PRO_0000028183.
FT   CHAIN        19     36       Thrombin heavy chain.
FT                                /FTId=PRO_0000028184.
FT   DOMAIN      <19    >36       Peptidase S1.
FT   NON_CONS     18     19
FT   NON_TER      36     36
SQ   SEQUENCE   36 AA;  3784 MW;  E451D38AE5FCA666 CRC64;
     SFGSGELVXG EXPXFEKIIV KGIDAEVASA PMQVML
//