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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Chen Y.,
Tan W.,
Cheng J.;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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[2]
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PROTEIN SEQUENCE OF 20-579.
Schaller J.,
Marti T.,
Roesselet S.J.,
Kaempfer U.,
Rickli E.E.;
"Amino acid sequence of the heavy chain of porcine plasmin. Comparison of the carbohydrate attachment sites with the human and bovine species.";
Fibrinolysis 1:91-102(1987).
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[3]
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PROTEIN SEQUENCE OF 469-809.
PubMed=3846533 [NCBI, ExPASy, EBI, Israel, Japan]
Marti T.,
Schaller J.,
Rickli E.E.;
"Determination of the complete amino-acid sequence of porcine miniplasminogen.";
Eur. J. Biochem. 149:279-285(1985).
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[4]
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GLYCOSYLATION AT ASN-308 AND THR-359, AND 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, sialic acid and is core fucosylated. 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-579, 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: 809 AA [This is the length of the unprocessed precursor] |
Molecular weight: 90615 Da [This is the MW of the unprocessed precursor] |
CRC64: 198261D2082A075D [This is a checksum on the sequence] |
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10 20 30 40 50 60
MDHKEVVLLL LLFLKSGLGD SLDDYVNTQG AFLFSLSRKQ VAARSVEECA AKCEAETNFI
70 80 90 100 110 120
CRAFQYHSKD QQCVVMAENS KTSPIARMRD VVLFEKRIYL SECKTGNGKN YRGTTSKTKS
130 140 150 160 170 180
GVICQKWSVS SPHIPKYSPE KFPLAGLEEN YCRNPDNDEK GPWCYTTDPE TRFDYCDIPE
190 200 210 220 230 240
CEDECMHCSG EHYEGKISKT MSGIECQSWG SQSPHAHGYL PSKFPNKNLK MNYCRNPDGE
250 260 270 280 290 300
PRPWCFTTDP NKRWEFCDIP RCTTPPPTSG PTYQCLKGRG ENYRGTVSVT ASGHTCQRWS
310 320 330 340 350 360
AQSPHKHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS EVRWDYCKIP SCGSSTTSTE
370 380 390 400 410 420
YLDAPVPPEQ TPVAQDCYRG NGESYRGTSS TTITGRKCQS WVSMTPHRHE KTPGNFPNAG
430 440 450 460 470 480
LTMNYCRNPD ADKSPWCYTT DPRVRWEYCN LKKCSETEQQ VTNFPAIAQV PSVEDLSEDC
490 500 510 520 530 540
MFGNGKRYRG KRATTVAGVP CQEWAAQEPH RHSIFTPETN PRAGLEKNYC RNPDGDDNGP
550 560 570 580 590 600
WCYTTNPQKL FDYCDVPQCV TSSFDCGKPK VEPKKCPARV VGGCVSIPHS WPWQISLRHR
610 620 630 640 650 660
YGGHFCGGTL ISPEWVLTAK HCLEKSSSPS SYKVILGAHE EYHLGEGVQE IDVSKLFKEP
670 680 690 700 710 720
SEADIALLKL SSPAIITDKV IPACLPTPNY VVADRTACYI TGWGETKGTY GAGLLKEARL
730 740 750 760 770 780
PVIENKVCNR YEYLGGKVSP NELCAGHLAG GIDSCQGDSG GPLVCFEKDK YILQGVTSWG
790 800
LGCALPNKPG VYVRVSRFVT WIEEIMRRN
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P06867 in FASTA format |
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ExPASy Home page
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