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UniProtKB/Swiss-Prot entry P12545


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PLMN_MACMU
Primary accession number P12545
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 83)
Name and origin of the protein
Protein name Plasminogen [Precursor]
Synonym EC 3.4.21.7
Contains Plasmin heavy chain A
Activation peptide
Plasmin heavy chain A, short form
Plasmin light chain B
Gene name
Name: PLG
From
Macaca mulatta (Rhesus macaque) [TaxID: 9544] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2925643 [NCBI, ExPASy, EBI, Israel, Japan]
Tomlinson J.E., McLean J.W., Lawn R.M.;
"Rhesus monkey apolipoprotein(a). Sequence, evolution, and sites of synthesis.";
J. Biol. Chem. 264:5957-5965(1989).
Comments
  • 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. Activated with catalytic amounts of streptokinase.
  • SUBUNIT: Interacts with CSPG4 (By similarity).
  • SUBCELLULAR LOCATION: Secreted.
  • DOMAIN: Kringle domains mediate interaction with CSPG4 (By similarity).
  • PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-580, 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.
  • MISCELLANEOUS: In the presence of the inhibitor, the activation involves only cleavage after Arg-580, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide.
  • 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].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04697; AAA36901.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B32869; B30848.
RefSeq NP_001036540.1; -.
UniGene Mmu.3024
3D structure databases
HSSP P00747; 1BUI. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
SMR P12545; 184-352, 564-810.
ModBase P12545.
Protein family/group databases
MEROPS S01.233; -.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0042730; Biological process: fibrinolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0048771; Biological process: tissue remodeling (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000001; Kringle.
IPR003014; PAN.
IPR003609; Pan_app.
IPR011358; Pept_S1A_Plasmin.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR003966; Peptidase_S1A_prothrombin.
Graphical view of domain structure.
Gene3D G3DSA:2.40.20.10; Kringle; 5.
Pfam PF00051; Kringle; 5.
PF00024; PAN_1; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001150; Plasmin; 1.
PRINTS PR00722; CHYMOTRYPSIN.
PR00018; KRINGLE.
PR01505; PROTHROMBIN.
ProDom PD000395; Kringle; 5.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00130; KR; 5.
SM00473; PAN_AP; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS00021; KRINGLE_1; 5.
PS50070; KRINGLE_2; 5.
PS50948; PAN; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P12545.
Genome annotation databases
Ensembl ENSMMUG00000016945; Macaca mulatta. [Contig view]
GeneID 703891; -.
KEGG mcc:703891; -.
Phylogenomic databases
HOVERGEN P12545; -.
Other
LinkHub P12545; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Blood coagulation; Fibrinolysis; Glycoprotein; Hydrolase; Kringle; Protease; Repeat; Secreted; Serine protease; Signal; Tissue remodeling; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     By similarity. 
CHAIN   20   810  791     Plasminogen. PRO_0000028059
CHAIN   20   580  561     Plasmin heavy chain A. PRO_0000028060
PEPTIDE   20    96  77     Activation peptide. PRO_0000028061
CHAIN   97   580  484     Plasmin heavy chain A, short form. PRO_0000028062
CHAIN   581   810  230     Plasmin light chain B. PRO_0000028063
DOMAIN   20    98  79     PAN. 
DOMAIN   103   181  79     Kringle 1. 
DOMAIN   184   262  79     Kringle 2. 
DOMAIN   275   352  78     Kringle 3. 
DOMAIN   377   454  78     Kringle 4. 
DOMAIN   481   560  80     Kringle 5. 
DOMAIN   581   808  228     Peptidase S1. 
ACT_SITE   622   622        Charge relay system (By similarity). 
ACT_SITE   665   665        Charge relay system (By similarity). 
ACT_SITE   760   760        Charge relay system (By similarity). 
BINDING   134   134        Fibrin (By similarity). 
BINDING   136   136        Fibrin (By similarity). 
BINDING   136   136        Omega-aminocarboxylic acids (By similarity). 
BINDING   158   158        Omega-aminocarboxylic acids (By similarity). 
BINDING   172   172        Omega-aminocarboxylic acids (By similarity). 
BINDING   432   432        Omega-aminocarboxylic acids (By similarity). 
BINDING   445   445        Omega-aminocarboxylic acids (By similarity). 
CARBOHYD   365   365        O-linked (GalNAc...) (By similarity). 
DISULFID   49    73        By similarity. 
DISULFID   53    61        By similarity. 
DISULFID   103   181        By similarity. 
DISULFID   124   164        By similarity. 
DISULFID   152   176        By similarity. 
DISULFID   185   262        By similarity. 
DISULFID   188   316        By similarity. 
DISULFID   206   245        By similarity. 
DISULFID   234   257        By similarity. 
DISULFID   275   352        By similarity. 
DISULFID   296   335        By similarity. 
DISULFID   324   347        By similarity. 
DISULFID   377   454        By similarity. 
DISULFID   398   437        By similarity. 
DISULFID   426   449        By similarity. 
DISULFID   481   560        By similarity. 
DISULFID   502   543        By similarity. 
DISULFID   531   555        By similarity. 
DISULFID   567   685        Interchain (between A and B chains) (By similarity). 
DISULFID   577   585        Interchain (between A and B chains) (By similarity). 
DISULFID   607   623        By similarity. 
DISULFID   699   766        By similarity. 
DISULFID   729   745        By similarity. 
DISULFID   756   784        By similarity. 
Sequence information
Length: 810 AA [This is the length of the unprocessed precursor] Molecular weight: 90255 Da [This is the MW of the unprocessed precursor] CRC64: A75E1C51A1A0F24A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEHKEVVLLL LLFLKSGQGE PLDDYVNTKG ASLFSITKKQ LGAGSIEECA AKCEEEEEFT 

        70         80         90        100        110        120 
CRSFQYHSKE QQCVIMAENR KSSIVFRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTRT 

       130        140        150        160        170        180 
GITCQKWSST SPHRPTFSPA THPSEGLEEN YCRNPDNDGQ GPWCYTTDPE ERFDYCDIPE 

       190        200        210        220        230        240 
CEDECMHCSG ENYDGKISKT MSGLECQAWD SQSPHAHGYI PSKFPNKNLK KNYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGDVAVT VSGHTCHGWS 

       310        320        330        340        350        360 
AQTPHTHNRT PENFPCKNLD ENYCRNPDGE KAPWCYTTNS QVRWEYCKIP SCESSPVSTE 

       370        380        390        400        410        420 
PLDPTAPPEL TPVVQECYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHWHE KTPENFPNAG 

       430        440        450        460        470        480 
LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEGS VAAPPPVAQL PDAETPSEED 

       490        500        510        520        530        540 
CMFGNGKGYR GKKATTVTGT PCQEWAAQEP HSHRIFTPET NPRAGLEKNY CRNPDGDVGG 

       550        560        570        580        590        600 
PWCYTTNPRK LFDYCDVPQC AASSFDCGKP QVEPKKCPGR VVGGCVAYPH SWPWQISLRT 

       610        620        630        640        650        660 
RLGMHFCGGT LISPEWVLTA AHCLEKSSRP SFYKVILGAH REVHLEPHVQ EIEVSKMFSE 

       670        680        690        700        710        720 
PARADIALLK LSSPAIITDK VIPACLPSPN YVVADRTECF ITGWGETQGT YGAGLLKEAR 

       730        740        750        760        770        780 
LPVIENKVCN RYEFLNGTVK TTELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW 

       790        800        810 
GLGCARPNKP GVYVRVSRFV TWIEGVMRNN 

P12545 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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