Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9XSZ5 (MMP1_HORSE)

Last modified January 19, 2010. Version 74. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Interstitial collagenase
    EC=3.4.24.7
Alternative name(s):
    Matrix metalloproteinase-1
      Short name=MMP-1
Gene names
Name: MMP1
OrganismEquus caballus (Horse)
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Hide | Top

Protein attributes

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

Hide | Top

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.

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 4 hemopexin-like domains.

Hide | Top

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: InterPro

   Cellular componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Propeptide19 – 9981Activation peptide
PRO_0000028701
Chain100 – 469370Interstitial collagenase
PRO_0000028702

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 By similarity
Metal binding921Zinc 2; in inhibited form By similarity
Metal binding1241Calcium 1 By similarity
Metal binding1581Calcium 2 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1751Calcium 3 By similarity
Metal binding1761Calcium 3; via carbonyl oxygen By similarity
Metal binding1781Calcium 3; via carbonyl oxygen By similarity
Metal binding1801Calcium 3; via carbonyl oxygen By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1901Calcium 2; via carbonyl oxygen By similarity
Metal binding1921Calcium 2; via carbonyl oxygen By similarity
Metal binding1941Calcium 2 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding1981Calcium 3 By similarity
Metal binding1991Calcium 1 By similarity
Metal binding2011Calcium 3 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity
Metal binding2851Calcium 4; via carbonyl oxygen By similarity
Metal binding3291Calcium 4; via carbonyl oxygen By similarity
Metal binding3781Calcium 4; via carbonyl oxygen By similarity
Metal binding4271Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Disulfide bond278 ↔ 466 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9XSZ5-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: AEE6760AB2C529CA

FASTA46954,002
        10         20         30         40         50         60 
MLSLPLLLLL LWGMGSHSFP TVPSETREED VEMVQKYLEN YYNLKSDGEQ IEKQRHRSPV 

        70         80         90        100        110        120 
VEKLKQMQEF FGLKVTGKPD AETLNVMKQP RCGVPDVAEF VLTEGNPRWE NTHLTYRIEN 

       130        140        150        160        170        180 
YTPDLPRADV DQAIEKAFQL WSNVSPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN 

       190        200        210        220        230        240 
LAHAFQPGPR IGGDAHFDED ETWTSNFRNY NLYRVAAHEF GHSLGLSHST DIGALMYPNY 

       250        260        270        280        290        300 
FFTGDVQLSQ DDINGIQAIY GPSQNPIQPI GPQTPEVCDS KLTFDAITTI RGEVMFFKDR 

       310        320        330        340        350        360 
FYMRINPYYP EAELNFISIF WPQLPNGLQA AYEVSHRDEV RFFKGNKYWA VKGQDVLYGY 

       370        380        390        400        410        420 
PKDIHRSFGF PSTVKNIDAA VSEEDTGKTY FFVADKYWRY DEYKRSMDAG YPKMIADDFP 

       430        440        450        460 
GIGDKVDAVF QKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN

« Hide

Hide | Top

References

[1]"Cloning and expression of equine matrix metalloproteinase 1 (interstitial collagenase)."
Richardson D.W.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF148882 mRNA. Translation: AAD38030.1.
RefSeqNP_001075316.1.
UniGeneEca.13871

3D structure databases

SMRQ9XSZ5. Positions 31-465.
ModBaseSearch...

Protein family/group databases

MEROPSM10.001.

Genome annotation databases

EnsemblENSECAT00000025715; ENSECAP00000021406; ENSECAG00000023733; Equus caballus. [Genome view]
GeneID100033896.
KEGGecb:100033896.

Organism-specific databases

CTD100033896.

Phylogenomic databases

HOVERGENQ9XSZ5.
InParanoidQ9XSZ5.

Enzyme and pathway databases

BRENDA3.4.24.7. 1464.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR001818. Pept_M10A_M12B.
IPR016293. Pept_M10A_matrix.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 1 hit.
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]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameMMP1_HORSE
AccessionPrimary (citable) accession number: Q9XSZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 19, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

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