|
|
|
|
|
|
|
|
|
- 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.
- PTM: 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).
- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment (fragment 1) of the prothrombin, prior to its activation by factor Xa (By similarity).
- SIMILARITY: Belongs to the peptidase S1 family [view classification].
- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
- SIMILARITY: Contains 2 kringle domains.
- SIMILARITY: Contains 1 peptidase S1 domain [view classification].
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 623 AA [This is the length of the unprocessed precursor] |
Molecular weight: 70066 Da [This is the MW of the unprocessed precursor] |
CRC64: B7FEDC2231735D4E [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MAHVGGLWLH GCLALAVLVS LVHSQHVFMA PQQALSLLQR ARRANSGFFE EMRKGNLERE
70 80 90 100 110 120
CVEEQCSREE AYEALESPSE TDAFWAKYTA CESVRKSREK LVECLEGNCA EGLGMNYRGN
130 140 150 160 170 180
ISVTRSGIEC QLWRSRYPHK PEVNSTMYPG ADLRENFCRN PDGSITGPWC YTTSPTVRRE
190 200 210 220 230 240
ACSIPVCGQG RVTAELIPRS GGSTVNVSPP LETCVPERGR QYQGRLAVTS HGSPCLAWGS
250 260 270 280 290 300
SQAKALSKDQ DFNPAVPLVE NFCRNPDGDQ EGAWCYVAGQ PGDFEYCDLD YCEEPVDEEV
310 320 330 340 350 360
GDALGENADA AIEGRTTADD FQPFFNEKTF GAGEADCGLR PLFEKSSLED KTEKELFESY
370 380 390 400 410 420
IEGRIVEGSD AEIGLAPWQV MIFRKSPQEL LCGASLISDR WVLTAAHCLL YPPWDKNFTE
430 440 450 460 470 480
NDLLVRIGKH SRTRYERNIE KISMLEKIYI HPRYNWRENL DRDIALLKLR KPITFSDYIH
490 500 510 520 530 540
PVCLPDKETA TKLLRAGYKG RVTGWGNLKE TWTTSASEVQ PSVLQVVNLP IVERLVCKAS
550 560 570 580 590 600
TRIRITDNMF CAGYKPDEGK RGDACEGDSG GPFVMKSPFN NRWYQMGIVS WGEGCDRDGK
610 620
YGFYTHVFRL KKWMQKVIDR FGG
|
Q19AZ8 in FASTA format |
|
ExPASy Home page
SIB Switzerland
