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Q11133 (MMP1_RANCA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. 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:
Interstitial collagenase
EC=3.4.24.7
Alternative name(s):
Matrix metalloproteinase-1
Short name=MMP-1
TC1
OrganismRana catesbeiana (American bullfrog) (Lithobates catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Raninae › Rana › Aquarana

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X.

Catalytic activity

Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Can be activated without removal of the activation peptide By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

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.

Contains 2 hemopexin-like domains.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Zymogen
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 – 2525 Potential
Propeptide26 – 8863Activation peptide Potential
PRO_0000028712
Chain89 – 384296Interstitial collagenase
PRO_0000028713

Regions

Domain276 – 32045Hemopexin-like 1
Domain346 – 38136Hemopexin-like 2
Motif79 – 868Cysteine switch By similarity

Sites

Active site1901 By similarity
Metal binding811Zinc 2; in inhibited form By similarity
Metal binding1131Calcium 1 By similarity
Metal binding1291Calcium 2 By similarity
Metal binding1391Zinc 1 By similarity
Metal binding1411Zinc 1 By similarity
Metal binding1461Calcium 3 By similarity
Metal binding1471Calcium 3; via carbonyl oxygen By similarity
Metal binding1491Calcium 3; via carbonyl oxygen By similarity
Metal binding1511Calcium 3; via carbonyl oxygen By similarity
Metal binding1541Zinc 1 By similarity
Metal binding1611Calcium 2; via carbonyl oxygen By similarity
Metal binding1631Calcium 2; via carbonyl oxygen By similarity
Metal binding1651Calcium 2 By similarity
Metal binding1671Zinc 1 By similarity
Metal binding1691Calcium 3 By similarity
Metal binding1701Calcium 1 By similarity
Metal binding1721Calcium 3 By similarity
Metal binding1891Zinc 2; catalytic By similarity
Metal binding1931Zinc 2; catalytic By similarity
Metal binding1991Zinc 2; catalytic By similarity
Metal binding2491Calcium 4; via carbonyl oxygen By similarity
Metal binding2771Calcium 4; via carbonyl oxygen By similarity
Metal binding3471Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond242 ↔ 381 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11133 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A5B5E2FB332239DF

FASTA38443,582
        10         20         30         40         50         60 
MLSGLWSSIL ALLGVFLQSV GEFRAETQEQ DVEIVQKYLK NYYNSDKRNS GLVVEILKQF 

        70         80         90        100        110        120 
FGLKVTGKPD AETLVMKQST CGVPDVGEYV LTPGNPRWEN THLTYRIENY TPDLVSPLTF 

       130        140        150        160        170        180 
TKVSEGQADI MISFVRGDHR DKYPFDGPGG NLAHASQPGP GIGGDAHFDE YERWTKNFQD 

       190        200        210        220        230        240 
YNLYRVAAHE LGHSLGLSHS TDIGALMYPT YLRGDVQLSQ DDIDGPSGNP VQPRGPQTPQ 

       250        260        270        280        290        300 
VCDSKLTFDA ITTVRGELMF FKMRTNRFYP EVELGLQAAY EMADRDEVRF FKGNKYWAVS 

       310        320        330        340        350        360 
GQDVLYGYPK DIHSSFGFPT GVAHECWSYD EYKQSMDTGY ADEFPGDAVF QKFFHGTRQY 

       370        380 
QFDLKTKRIL TLQKANSWFN CRKN

« Hide

References

[1]"Regionally and hormonally regulated expression of genes of collagen and collagenase in the anuran larval skin."
Oofusa K., Yomori S., Yoshizato K.
Int. J. Dev. Biol. 38:345-350(1994) [PubMed: 7981043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S75623 mRNA. Translation: AAB32661.1.
PIRI51267.

3D structure databases

ProteinModelPortalQ11133.
ModBaseSearch...

Protein family/group databases

MEROPSM10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052484.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018487. Hemopexin/matrixin_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A_matrixin.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
G3DSA:2.110.10.10. Hemopexin. 1 hit.
PfamPF00045. Hemopexin. 1 hit.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. False negative.
PS00024. HEMOPEXIN. False negative.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMP1_RANCA
AccessionPrimary (citable) accession number: Q11133
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 79 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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