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P21692 (MMP1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interstitial collagenase
EC=3.4.24.7
Alternative name(s):
Matrix metalloproteinase-1
Short name=MMP-1

Cleaved into the following chain:

  1. 18 kDa interstitial collagenase
Gene names
Name:MMP1
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Binds 2 zinc ions per subunit.

Enzyme regulation

Can be activated without removal of the activation peptide.

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.

Post-translational modification

Undergoes autolytic cleavage to produce a N-terminal fragment having reduced collagenolytic activity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Propeptide20 – 9980Activation peptide
PRO_0000028707
Chain100 – 469370Interstitial collagenase
PRO_0000028708
Chain100 – 25815918 kDa interstitial collagenase
PRO_0000028709

Regions

Domain284 – 32643Hemopexin-like 1
Domain328 – 37245Hemopexin-like 2
Domain377 – 42448Hemopexin-like 3
Domain426 – 46641Hemopexin-like 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191 Ref.3
Metal binding921Zinc 2; in inhibited form By similarity
Metal binding1241Calcium 1
Metal binding1581Calcium 2
Metal binding1681Zinc 1
Metal binding1701Zinc 1
Metal binding1751Calcium 3
Metal binding1761Calcium 3; via carbonyl oxygen
Metal binding1781Calcium 3; via carbonyl oxygen
Metal binding1801Calcium 3; via carbonyl oxygen
Metal binding1831Zinc 1
Metal binding1901Calcium 2; via carbonyl oxygen
Metal binding1921Calcium 2; via carbonyl oxygen
Metal binding1941Calcium 2
Metal binding1961Zinc 1
Metal binding1981Calcium 3
Metal binding1991Calcium 1
Metal binding2011Calcium 3
Metal binding2181Zinc 2; catalytic
Metal binding2221Zinc 2; catalytic
Metal binding2281Zinc 2; catalytic
Metal binding2851Calcium 4; via carbonyl oxygen
Metal binding3291Calcium 4; via carbonyl oxygen
Metal binding3781Calcium 4; via carbonyl oxygen
Metal binding4271Calcium 4; via carbonyl oxygen
Site258 – 2592Cleavage; by autolysis

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Disulfide bond278 ↔ 466

Secondary structure

1 ................................................................. 469
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21692 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 7952D72B2753F682

FASTA46953,666
        10         20         30         40         50         60 
MFSLLLLLLL LCNTGSHGFP AATSETQEQD VEIVQKYLKN YYNLNSDGVP VEKKRNSGLV 

        70         80         90        100        110        120 
VEKLKQMQQF FGLKVTGKPD AETLNVMKQP RCGVPDVAEF VLTPGNPRWE NTHLTYRIEN 

       130        140        150        160        170        180 
YTPDLSREDV DRAIEKAFQL WSNVSPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN 

       190        200        210        220        230        240 
LAHAFQPGPG IGGDAHFDED ERWTKNFRDY NLYRVAAHEL GHSLGLSHST DIGALMYPNY 

       250        260        270        280        290        300 
IYTGDVQLSQ DDIDGIQAIY GPSENPVQPS GPQTPQVCDS KLTFDAITTL RGELMFFKDR 

       310        320        330        340        350        360 
FYMRTNSFYP EVELNFISVF WPQVPNGLQA AYEIADRDEV RFFKGNKYWA VRGQDVLYGY 

       370        380        390        400        410        420 
PKDIHRSFGF PSTVKNIDAA VFEEDTGKTY FFVAHECWRY DEYKQSMDTG YPKMIAEEFP 

       430        440        450        460 
GIGNKVDAVF QKDGFLYFFH GTRQYQFDFK TKRILTLQKA NSWFNCRKN

« Hide

References

[1]"Porcine collagenase from synovial fibroblasts: cDNA sequence and modulation of expression of RNA in vitro by various cytokines."
Richards C.D., Rafferty J.A., Reynolds J.J., Saklatvala J.
Matrix 11:161-167(1991) [PubMed: 1651440] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Nucleotide sequence of a cDNA for porcine type I collagenase, obtained by PCR."
Clarke N.J., O'Hare M.C., Cawston T.E., Harper G.P.
Nucleic Acids Res. 18:6703-6703(1990) [PubMed: 2174547] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-469.
Tissue: Synovial cell.
[3]"Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller."
Li J., Brick P., O'Hare M.C., Skarzynski T., Lloyd L.F., Curry V.A., Clark I.M., Bigg H.F., Hazleman B.L., Cawston T.E., Blow D.M.
Structure 3:541-549(1995) [PubMed: 8590015] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-469.
[4]"Recombinant porcine collagenase: purification and autolysis."
Clark I.M., Mitchell R.E., Powell L.K., Bigg H.F., Cawston T.E., O'Hare M.C.
Arch. Biochem. Biophys. 316:123-127(1995) [PubMed: 7840605] [Abstract]
Cited for: PROTEIN SEQUENCE OF 100-104 AND 248-282, AUTOCATALYTIC CLEAVAGE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X54724 mRNA. Translation: CAA38526.1.
PIRKCPGI. S15986.
RefSeqNP_001159701.1. NM_001166229.1.
UniGeneSsc.16013.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FBLX-ray2.50A100-469[»]
ProteinModelPortalP21692.
SMRP21692. Positions 31-466.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21692.

Protein family/group databases

MEROPSM10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397320.
KEGGssc:397320.

Organism-specific databases

CTD4312.

Phylogenomic databases

HOVERGENHBG052484.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016293. Pept_M10A_matrix_strom.
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.
G3DSA:2.110.10.10. Hemopexin. 1 hit.
KOK01388.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP21692.

Entry information

Entry nameMMP1_PIG
AccessionPrimary (citable) accession number: P21692
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: December 1, 1992
Last modified: November 16, 2011
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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