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Q01177 (PLMN_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 105. 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 5 chains:

  1. Plasmin heavy chain A
  2. Activation peptide
  3. Angiostatin
  4. Plasmin heavy chain A, short form
  5. Plasmin light chain B
Gene names
Name:Plg
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length812 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.

Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo 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. Cannot be activated with streptokinase.

Subunit structure

Interacts (both mature PLG and the angiostatin peptide) with AMOT and CSPG4. Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation. Interacts (the angiostatin peptide) with ATP5A1; the interaction inhibits most of the angiogenic effects of angiostatin 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-581, 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-581, resulting in 2 chains held together by 2 disulfide bonds. Without the inhibitor, the activation involves also removal of the activation peptide By similarity.

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 – 812793Plasminogen
PRO_0000028079
Chain20 – 581562Plasmin heavy chain A
PRO_0000028080
Peptide20 – 9778Activation peptide By similarity
PRO_0000028081
Chain98 – 581484Plasmin heavy chain A, short form
PRO_0000028082
Chain98 – ?436339Angiostatin
PRO_0000028083
Chain582 – 812231Plasmin light chain B
PRO_0000028084

Regions

Domain20 – 9879PAN
Domain102 – 18180Kringle 1
Domain184 – 26279Kringle 2
Domain274 – 35279Kringle 3
Domain375 – 45480Kringle 4
Domain480 – 56081Kringle 5
Domain582 – 810229Peptidase S1

Sites

Active site6241Charge relay system By similarity
Active site6671Charge relay system By similarity
Active site7621Charge relay system By similarity

Amino acid modifications

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 bond376 ↔ 454 By similarity
Disulfide bond397 ↔ 437 By similarity
Disulfide bond425 ↔ 449 By similarity
Disulfide bond481 ↔ 560 By similarity
Disulfide bond502 ↔ 543 By similarity
Disulfide bond531 ↔ 555 By similarity
Disulfide bond568 ↔ 687Interchain (between A and B chains) By similarity
Disulfide bond578 ↔ 586Interchain (between A and B chains) By similarity
Disulfide bond609 ↔ 625 By similarity
Disulfide bond701 ↔ 768 By similarity
Disulfide bond731 ↔ 747 By similarity
Disulfide bond758 ↔ 786 By similarity

Experimental info

Sequence conflict4181A → S in AAA41884. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q01177 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: 8C703C51410EBC9E

FASTA81290,536
        10         20         30         40         50         60 
MDHKEIILLF LLFLKPGQGD SLDGYVSTQG ASLHSLTKKQ LAAGSIADCL AKCEGETDFI 

        70         80         90        100        110        120 
CRSFQYHSKE QQCVIMAENS KTSSIIRMRD VILFEKRVYL SECKTGIGKG YRGTMSKTKT 

       130        140        150        160        170        180 
GVTCQKWSDT SPHVPKYSPS THPSEGLEEN YCRNPDNDEQ GPWCYTTDPD QRYEYCNIPE 

       190        200        210        220        230        240 
CEEECMYCSG EKYEGKISKT MSGLDCQSWD SQSPHAHGYI PAKFPSKNLK MNYCRNPDGE 

       250        260        270        280        290        300 
PRPWCFTTDP NKRWEYCDIP RCTTPPPPPG PTYQCLKGRG ENYRGTVSVT ASGKTCQRWS 

       310        320        330        340        350        360 
EQTPHRHNRT PENFPCKNLE ENYCRNPDGE TAPWCYTTDS QLRWEYCEIP SCGSSVSPDQ 

       370        380        390        400        410        420 
SDSSVLPEQT PVVQECYQGN GKSYRGTSST TNTGKKCQSW VSMTPHSHSK TPANFPDAGL 

       430        440        450        460        470        480 
EMNYCRNPDN DQRGPWCFTT DPSVRWEYCN LKRCSETGGG VAESAIVPQV PSAPGTSETD 

       490        500        510        520        530        540 
CMYGNGKEYR GKTAVTAAGT PCQEWAAQEP HSHRIFTPQT NPRAGLEKNY CRNPDGDVNG 

       550        560        570        580        590        600 
PWCYTMNPRK LYDYCNIPLC ASLSSFECGK PQVEPKKCPG RVVGGCVANP HSWPWQISLR 

       610        620        630        640        650        660 
TRFSGQHFCG GTLISPEWVL TAAHCLEKSS RPEFYKVILG AHEERILGSD VQQIAVTKLV 

       670        680        690        700        710        720 
LEPNDADIAL LKLSRPATIT DNVIPACLPS PNYVVADRTL CYITGWGETK GTPGAGRLKE 

       730        740        750        760        770        780 
AQLPVIENKV CNRAEYLNNR VKSTELCAGH LAGGIDSCQG DSGGPLVCFE KDKYILQGVT 

       790        800        810 
SWGLGCARPN KPGVYVRVSR YVNWIEREMR ND

« Hide

References

« Hide 'large scale' references
[1]"Rat plasminogen: cDNA and gene structure."
Bangert K., Johnsen A.H., Thorsen S.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]"Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen."
Kanalas J.J., Makker S.P.
J. Biol. Chem. 266:10825-10829(1991) [PubMed: 1645711] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-511.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ242649 mRNA. Translation: CAB46014.1.
BC091135 mRNA. Translation: AAH91135.1.
M62832 mRNA. Translation: AAA41884.1.
IPIIPI00206780.
PIRA40522.
RefSeqNP_445943.1. NM_053491.2.
UniGeneRn.20178.

3D structure databases

ProteinModelPortalQ01177.
SMRQ01177. Positions 565-812.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ01177.

Protein family/group databases

MEROPSS01.233.

Proteomic databases

PRIDEQ01177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023368; ENSRNOP00000023370; ENSRNOG00000017223.
GeneID85253.
KEGGrno:85253.
NMPDRfig|10116.3.peg.463.
UCSCBC091135. rat.

Organism-specific databases

CTD5340.
RGD619893. Plg.

Phylogenomic databases

eggNOGroNOG14223.
GeneTreeENSGT00600000084233.
HOVERGENHBG004381.
InParanoidQ01177.
OMAENKVCNR.
OrthoDBEOG4RR6GQ.
PhylomeDBQ01177.

Gene expression databases

ArrayExpressQ01177.
GenevestigatorQ01177.
GermOnlineENSRNOG00000017223. Rattus norvegicus.

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...

Other

NextBio617350.

Entry information

Entry namePLMN_RAT
AccessionPrimary (citable) accession number: Q01177
Secondary accession number(s): Q5BKB6, Q9R0W3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: August 31, 2004
Last modified: November 16, 2011
This is version 105 of the entry and version 2 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