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Reviewed, UniProtKB/Swiss-Prot Q5R8X6 (PLMN_PONAB)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Plasminogen
    EC=3.4.21.7
Cleaved into the following 4 chains:
    1- Recommended name:
            Plasmin heavy chain A
    2- Recommended name:
            Activation peptide
    3- Recommended name:
            Plasmin heavy chain A, short form
    4- Recommended name:
            Plasmin light chain B
Gene names
Name: PLG
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

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

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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 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 structure

Interacts with CSPG4 By similarity.

Subcellular location

Secreted.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 810791Plasminogen
PRO_0000285883
Chain20 – 580561Plasmin heavy chain A
PRO_0000285884
Peptide20 – 9677Activation peptide
PRO_0000285885
Chain97 – 580484Plasmin heavy chain A, short form
PRO_0000285886
Chain581 – 810230Plasmin light chain B
PRO_0000285887

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

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Sequences

Sequence LengthMass (Da)Tools
Q5R8X6-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 126D530C9942ADD4

FASTA81090,380
        10         20         30         40         50         60 
MEHKEVVLLL LLFLKSGQGE PLDDYVNTQG ASLFSVTKKQ LRAGSIEECA AKCEEEKEFT 

        70         80         90        100        110        120 
CRAFQYHSKE QQCVIMAENR KSSIIIRMRD VVLFEKKVYL SECKTGNGKN YRGTMSKTKN 

       130        140        150        160        170        180 
GITCQKWSST SPHRPRFSPA THPSEGLEEN YCRNPDNDAQ GPWCYTTDPE HRYDYCDIPE 

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

       250        260        270        280        290        300 
PRPWCFTTDP NKRWELCDIP RCTTPPPSSG PTYQCLKGTG ENYRGNVAVT VSGHTCQRWS 

       310        320        330        340        350        360 
AQTPQTHNRT PENFPCKNLD ENYCRNPDGE KAPWCYTTNS QVRWEYCKIP SCGSSPVSTE 

       370        380        390        400        410        420 
QLDPTAPPEL TPVVQDCYHG DGQSYRGTSS TTTTGKKCQS WSSMTPHWHQ KTPENYPDAG 

       430        440        450        460        470        480 
LTMNYCRNPD ADKGPWCFTT DPSVRWEYCN LKKCSGTEGS VVAPPPVVQL PNVETPSEED 

       490        500        510        520        530        540 
CMFGNGKGYR GKRATTVTGT PCQEWAAQEP HRHSIFTPQT NPRAGLEKNY CRNPDGDEGG 

       550        560        570        580        590        600 
PWCYTTNPRK HYDYCDVPQC ASSSFDCGKP QVEPKKCPGR VVGGCVANAH SWPWQVSLRT 

       610        620        630        640        650        660 
RFGTHFCGGT LISPEWVLTA AHCLEKSPRP SSYKVILGAH QEVNLEPHVQ EIEVSRLFLE 

       670        680        690        700        710        720 
PTRADIALLK LSSPAVITDK VIPACLPSPN YVVAGRTECF ITGWGETQGT FGAGLLKEAQ 

       730        740        750        760        770        780 
LPVIENKVCN RYEFLNGRVK STELCAGHLA GGTDSCQGDS GGPLVCFEKD KYILQGVTSW 

       790        800        810 
GLGCARPNKP GVYVRVSRFV TWIEGVMRNN

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

CR859622 mRNA. Translation: CAH91784.1.
RefSeqNP_001126035.1.
UniGenePab.5478

3D structure databases

SMRQ5R8X6. Positions 185-352, 564-810.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

Genome annotation databases

GeneID100172984.

Phylogenomic databases

HOVERGENQ5R8X6.

Enzyme and pathway databases

BRENDA3.4.21.7. 269192.

Family and domain databases

InterProIPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR003014. PAN-1_domain.
IPR003609. Pan_app.
IPR011358. Pept_S1A_Plasmin.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR003966. Peptidase_S1A_prothrombin.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 5 hits.
PfamPF00051. Kringle. 5 hits.
PF00024. PAN_1. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001150. Plasmin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00018. KRINGLE.
PR01505. PROTHROMBIN.
ProDomPD000395. Kringle. 5 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00130. KR. 5 hits.
SM00473. PAN_AP. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
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...

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Entry information

Entry namePLMN_PONAB
AccessionPrimary (citable) accession number: Q5R8X6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents