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P12545 (PLMN_MACMU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Plasminogen
EC=3.4.21.7

Cleaved into the following 4 chains:

  1. Plasmin heavy chain A
  2. Activation peptide
  3. Plasmin heavy chain A, short form
  4. Plasmin light chain B
Gene names
Name:PLG
OrganismMacaca mulatta (Rhesus macaque)
Taxonomic identifier9544 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (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, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells By similarity.

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 structure

Interacts with CSPG4 and AMOT. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation By similarity.

Subcellular location

Secreted By similarity. Note: Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface By similarity.

Domain

Kringle domains mediate interaction with CSPG4 By similarity.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains 5 kringle domains.

Contains 1 PAN domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 810791Plasminogen
PRO_0000028059
Chain20 – 580561Plasmin heavy chain A
PRO_0000028060
Peptide20 – 9677Activation peptide
PRO_0000028061
Chain97 – 580484Plasmin heavy chain A, short form
PRO_0000028062
Chain581 – 810230Plasmin light chain B
PRO_0000028063

Regions

Domain20 – 9879PAN
Domain103 – 18179Kringle 1
Domain184 – 26279Kringle 2
Domain275 – 35278Kringle 3
Domain377 – 45478Kringle 4
Domain481 – 56080Kringle 5
Domain581 – 808228Peptidase S1

Sites

Active site6221Charge relay system By similarity
Active site6651Charge relay system By similarity
Active site7601Charge relay system By similarity
Binding site1341Fibrin By similarity
Binding site1361Fibrin By similarity
Binding site1361Omega-aminocarboxylic acids By similarity
Binding site1581Omega-aminocarboxylic acids By similarity
Binding site1721Omega-aminocarboxylic acids By similarity
Binding site4321Omega-aminocarboxylic acids By similarity
Binding site4451Omega-aminocarboxylic acids By similarity

Amino acid modifications

Glycosylation3651O-linked (GalNAc...) By similarity
Disulfide bond49 ↔ 73 By similarity
Disulfide bond53 ↔ 61 By similarity
Disulfide bond103 ↔ 181 By similarity
Disulfide bond124 ↔ 164 By similarity
Disulfide bond152 ↔ 176 By similarity
Disulfide bond185 ↔ 262 By similarity
Disulfide bond188 ↔ 316 By similarity
Disulfide bond206 ↔ 245 By similarity
Disulfide bond234 ↔ 257 By similarity
Disulfide bond275 ↔ 352 By similarity
Disulfide bond296 ↔ 335 By similarity
Disulfide bond324 ↔ 347 By similarity
Disulfide bond377 ↔ 454 By similarity
Disulfide bond398 ↔ 437 By similarity
Disulfide bond426 ↔ 449 By similarity
Disulfide bond481 ↔ 560 By similarity
Disulfide bond502 ↔ 543 By similarity
Disulfide bond531 ↔ 555 By similarity
Disulfide bond567 ↔ 685Interchain (between A and B chains) By similarity
Disulfide bond577 ↔ 585Interchain (between A and B chains) By similarity
Disulfide bond607 ↔ 623 By similarity
Disulfide bond699 ↔ 766 By similarity
Disulfide bond729 ↔ 745 By similarity
Disulfide bond756 ↔ 784 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12545 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: A75E1C51A1A0F24A

FASTA81090,255
        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

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References

[1]"Rhesus monkey apolipoprotein(a). Sequence, evolution, and sites of synthesis."
Tomlinson J.E., McLean J.W., Lawn R.M.
J. Biol. Chem. 264:5957-5965(1989) [PubMed: 2925643] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04697 mRNA. Translation: AAA36901.1.
PIRB30848. B32869.
RefSeqNP_001036540.1. NM_001043075.1.
UniGeneMmu.3024.

3D structure databases

ProteinModelPortalP12545.
SMRP12545. Positions 480-810.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12545.

Protein family/group databases

MEROPSS01.233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID703891.
KEGGmcc:703891.

Organism-specific databases

CTD5340.

Phylogenomic databases

eggNOGprNOG15519.
HOVERGENHBG004381.
InParanoidP12545.
OrthoDBEOG4RR6GQ.

Family and domain databases

InterProIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR023317. Pept_S1A_plasmin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 5 hits.
KOK01315.
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF57440. Kringle-like. 5 hits.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00021. KRINGLE_1. 5 hits.
PS50070. KRINGLE_2. 5 hits.
PS50948. PAN. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMN_MACMU
AccessionPrimary (citable) accession number: P12545
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 16, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents