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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1016/0958-6946(94)00033-L; AGRICOLA=IND20546772
Berglund L.,
Andersen M.D.,
Petersen T.E.;
"Cloning and characterization of the bovine plasminogen cDNA.";
Int. Dairy J. 5:593-603(1995).
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[2]
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PROTEIN SEQUENCE OF 27-812, AND GLYCOSYLATION AT ASN-315 AND SER-365.
PubMed=3846532 [NCBI, ExPASy, EBI, Israel, Japan]
Schaller J.,
Moser P.W.,
Dannegger-Muller G.A.K.,
Rosselet S.J.,
Kampfer U.,
Rickli E.E.;
"Complete amino acid sequence of bovine plasminogen. Comparison with human plasminogen.";
Eur. J. Biochem. 149:267-278(1985).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] OF 706-812.
DOI=10.1021/bi00313a035; PubMed=6148961 [NCBI, ExPASy, EBI, Israel, Japan]
Malinowski D.P.,
Sadler J.E.,
Davie E.W.;
"Characterization of a complementary deoxyribonucleic acid coding for human and bovine plasminogen.";
Biochemistry 23:4243-4250(1984).
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[4]
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STRUCTURE OF CARBOHYDRATES.
PubMed=3356193 [NCBI, ExPASy, EBI, Israel, Japan]
Marti T.,
Schaller J.,
Rickli E.E.,
Schmid K.,
Kamerling J.P.,
Gerwig G.J.,
van Halbeek H.,
Vliegenthart J.F.;
"The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen. Species specificity in relation to sialylation and fucosylation patterns.";
Eur. J. Biochem. 173:57-63(1988).
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- FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation; in ovulation it weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. It cleaves fibrin, fibronectin, thrombospondin, laminin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4.
- CATALYTIC ACTIVITY: Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
- ENZYME REGULATION: Converted into plasmin by plasminogen activators, both plasminogen and its activator being bound to fibrin. Cannot be activated with streptokinase.
- SUBUNIT: Interacts with CSPG4 (By similarity).
- SUBCELLULAR LOCATION: Secreted.
- DOMAIN: Kringle domains mediate interaction with CSPG4 (By similarity).
- PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity).
- PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-583, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity).
- MISCELLANEOUS: Plasmin is inactivated by alpha-2-antiplasmin immediately after dissociation from the clot.
- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily [view classification].
- SIMILARITY: Contains 5 kringle domains.
- SIMILARITY: Contains 1 PAN domain.
- SIMILARITY: Contains 1 peptidase S1 domain [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 812 AA [This is the length of the unprocessed precursor] |
Molecular weight: 91216 Da [This is the MW of the unprocessed precursor] |
CRC64: 38A6AA691E220946 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLPASPKMEH KAVVFLLLLF LKSGLGDLLD DYVNTQGASL LSLSRKNLAG RSVEDCAAKC
70 80 90 100 110 120
EEETDFVCRA FQYHSKEQQC VVMAENSKNT PVFRMRDVIL YEKRIYLLEC KTGNGQTYRG
130 140 150 160 170 180
TTAETKSGVT CQKWSATSPH VPKFSPEKFP LAGLEENYCR NPDNDENGPW CYTTDPDKRY
190 200 210 220 230 240
DYCDIPECED KCMHCSGENY EGKIAKTMSG RDCQAWDSQS PHAHGYIPSK FPNKNLKMNY
250 260 270 280 290 300
CRNPDGEPRP WCFTTDPQKR WEFCDIPRCT TPPPSSGPKY QCLKGTGKNY GGTVAVTESG
310 320 330 340 350 360
HTCQRWSEQT PHKHNRTPEN FPCKNLEENY CRNPNGEKAP WCYTTNSEVR WEYCTIPSCE
370 380 390 400 410 420
SSPLSTERMD VPVPPEQTPV PQDCYHGNGQ SYRGTSSTTI TGRKCQSWSS MTPHRHLKTP
430 440 450 460 470 480
ENYPNAGLTM NYCRNPDADK SPWCYTTDPR VRWEFCNLKK CSETPEQVPA APQAPGVENP
490 500 510 520 530 540
PEADCMIGTG KSYRGKKATT VAGVPCQEWA AQEPHQHSIF TPETNPQSGL ERNYCRNPDG
550 560 570 580 590 600
DVNGPWCYTM NPRKPFDYCD VPQCESSFDC GKPKVEPKKC SGRIVGGCVS KPHSWPWQVS
610 620 630 640 650 660
LRRSSRHFCG GTLISPKWVL TAAHCLDNIL ALSFYKVILG AHNEKVREQS VQEIPVSRLF
670 680 690 700 710 720
REPSQADIAL LKLSRPAIIT KEVIPACLPP PNYMVAARTE CYITGWGETQ GTFGEGLLKE
730 740 750 760 770 780
AHLPVIENKV CNRNEYLDGR VKPTELCAGH LIGGTDSCQG DSGGPLVCFE KDKYILQGVT
790 800 810
SWGLGCARPN KPGVYVRVSP YVPWIEETMR RN
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P06868 in FASTA format |
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