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P50280 (MMP7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. 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:
Matrilysin
EC=3.4.24.23
Alternative name(s):
Matrin
Matrix metalloproteinase-7
Short name=MMP-7
Pump-1 protease
Uterine metalloproteinase
Gene names
Name:Mmp7
Synonyms:Mmp-7
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 length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase By similarity.

Catalytic activity

Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).

Cofactor

Binds 2 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix Probable.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Belongs to the peptidase M10A family.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 9777Activation peptide By similarity
PRO_0000028742
Chain98 – 267170Matrilysin
PRO_0000028743

Regions

Motif88 – 958Cysteine switch By similarity

Sites

Active site2181 By similarity
Metal binding901Zinc 2; in inhibited form By similarity
Metal binding1561Calcium 1 By similarity
Metal binding1661Zinc 1 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1731Calcium 2 By similarity
Metal binding1741Calcium 2; via carbonyl oxygen By similarity
Metal binding1761Calcium 2; via carbonyl oxygen By similarity
Metal binding1781Calcium 2; via carbonyl oxygen By similarity
Metal binding1811Zinc 1 By similarity
Metal binding1881Calcium 1; via carbonyl oxygen By similarity
Metal binding1901Calcium 1; via carbonyl oxygen By similarity
Metal binding1921Calcium 1 By similarity
Metal binding1941Zinc 1 By similarity
Metal binding1961Calcium 2 By similarity
Metal binding1991Calcium 2 By similarity
Metal binding2171Zinc 2; catalytic By similarity
Metal binding2211Zinc 2; catalytic By similarity
Metal binding2271Zinc 2; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P50280 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EBA3C3D9527A4C7B

FASTA26729,885
        10         20         30         40         50         60 
MAAMRLTLFR IVCLLPGCLA LPLSQEAGEV TALQWEQAQN YLRKFYLHDS KTKKATSAVD 

        70         80         90        100        110        120 
KLREMQKFFG LPETGKLSPR VMEIMQKPRC GVPDVAEFSL MPNSPKWHSR TVTYRIVSYT 

       130        140        150        160        170        180 
TDLPRFLVDQ IVKRALRMWS MQIPLNFKRV SWGTADIIIG FARGDHGDNF PFDGPGNTLG 

       190        200        210        220        230        240 
HAFAPGPGLG GDAHFDKDEY WTDGEDSGVN FLFVATHELG HSLGLGHSSV PSSVMYPTYQ 

       250        260 
GDHSEDFSLT KDDIAGIQKL YGKRNKL

« Hide

References

« Hide 'large scale' references
[1]"Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases."
Abramson S.R., Conner G.E., Nagase H., Neuhaus I., Woessner J.F.
J. Biol. Chem. 270:16016-16022(1995) [PubMed: 7608162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Uterus.
[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: Prostate.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L24374 mRNA. Translation: AAA99432.1.
BC064657 mRNA. Translation: AAH64657.1.
IPIIPI00196590.
PIRA57490.
RefSeqNP_036996.1. NM_012864.2.
UniGeneRn.10282.

3D structure databases

ProteinModelPortalP50280.
SMRP50280. Positions 98-264.
ModBaseSearch...

Protein-protein interaction databases

STRINGP50280.

Protein family/group databases

MEROPSM10.008.

Proteomic databases

PRIDEP50280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014041; ENSRNOP00000014041; ENSRNOG00000010507.
GeneID25335.
KEGGrno:25335.
UCSCNM_012864. rat.

Organism-specific databases

CTD4316.
RGD3100. Mmp7.

Phylogenomic databases

eggNOGmaNOG12555.
GeneTreeENSGT00570000079061.
HOVERGENHBG052484.
InParanoidP50280.
OMATEDYVIA.
OrthoDBEOG4H464B.
PhylomeDBP50280.

Enzyme and pathway databases

BRENDA3.4.24.23. 5301.

Gene expression databases

ArrayExpressP50280.
GenevestigatorP50280.
GermOnlineENSRNOG00000010507. Rattus norvegicus.

Family and domain databases

InterProIPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A_matrixin.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KOK01397.
PfamPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio606227.

Entry information

Entry nameMMP7_RAT
AccessionPrimary (citable) accession number: P50280
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 91 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

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