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Reviewed, UniProtKB/Swiss-Prot P33574 (PLMN_PETMA)

Last modified June 16, 2009. Version 62. 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

Names and origin

Protein namesRecommended name:
    Plasminogen
    EC=3.4.21.7
OrganismPetromyzon marinus (Sea lamprey)
Taxonomic identifier7757 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataHyperoartiaPetromyzontiformesPetromyzontidaePetromyzon

Protein attributes

Sequence length325 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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.

Catalytic activity

Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S1 family. Plasminogen subfamily.

Contains at least 2 kringle domains.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Tissue remodeling
   Cellular componentSecreted
   DomainKringle
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›325›325Plasminogen
PRO_0000088706

Amino acid modifications

Disulfide bond81 ↔ 146 By similarity
Disulfide bond102 ↔ 135 By similarity
Disulfide bond124 ↔ 141 By similarity
Disulfide bond188 ↔ 212 By similarity

Experimental info

Non-adjacent residues15 – 162
Non-adjacent residues34 – 352
Non-adjacent residues44 – 452
Non-adjacent residues76 – 772
Non-adjacent residues111 – 1122
Non-adjacent residues138 – 1392
Non-adjacent residues158 – 1592
Non-adjacent residues178 – 1792
Non-adjacent residues216 – 2172
Non-adjacent residues236 – 2372
Non-adjacent residues267 – 2682
Non-adjacent residues282 – 2832
Non-adjacent residues295 – 2962
Non-adjacent residues307 – 3082
Non-adjacent residues315 – 3162
Non-terminal residue3251

Sequences

Sequence LengthMass (Da)Tools
P33574-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 1B5F0B539AC6ED3C

FASTA32535,206
        10         20         30         40         50         60 
APIKGYSVTV XLYIFDCQKW SSNYPHKPNF SDATDPKGPW CYTTDYXGAA SVTRSGLRGD 

        70         80         90        100        110        120 
EQTPHRHTFS PQSFAGLTTA CVKGTGEGYR GTAALTVSGK ACQAWASQTP GDVYSCQGLV 

       130        140        150        160        170        180 
SNYCRNPDGE KLPWCYTTEY CNVPSCTGGP TGSEYHEILT PAQDXYTGIV EDYRGKMSPD 

       190        200        210        220        230        240 
AGLEENFCRN PDQDPQGPWC YTXNPEAXPR YCDVLSVVGG XEAQRNSXPR QISLQYGWQT 

       250        260        270        280        290        300 
VHVQSIHAEP RGVDIALVKI APPAQLTACV ITXWGETQGT GEDVQFCAGY PEGGTDPVSL 

       310        320 
VCLEPCVLAP VLVGVVILPX NDRXQ 

« Hide

References

[1]"Isolation, characterization and partial amino acid sequence of lamprey plasminogen."
Affolter M., Schaller J., Rickli E.E.
Protein Seq. Data Anal. 5:207-211(1993)
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRS33879.

3D structure databases

HSSPHSSP built from PDB template 5HPG based on UniProtKB P00747.
ModBaseSearch...

Protein family/group databases

MEROPSS01.233.

Phylogenomic databases

HOVERGENP33574.

Enzyme and pathway databases

BRENDA3.4.21.7. 276373.

Family and domain databases

InterProIPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 2 hits.
PfamPF00051. Kringle. 2 hits.
[Graphical view]
PRINTSPR00018. KRINGLE.
ProDomPD000395. Kringle. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00130. KR. 2 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00021. KRINGLE_1. 2 hits.
PS50070. KRINGLE_2. 2 hits.
PS50240. TRYPSIN_DOM. Partial match.
PS00134. TRYPSIN_HIS. Partial match.
PS00135. TRYPSIN_SER. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePLMN_PETMA
AccessionPrimary (citable) accession number: P33574
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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