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O88766 (MMP8_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutrophil collagenase

EC=3.4.24.34
Alternative name(s):
Matrix metalloproteinase-8
Short name=MMP-8
Gene names
Name:Mmp8
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Can degrade fibrillar type I, II, and III collagens.

Catalytic activity

Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.

Cofactor

Binds 3 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Cannot be activated without removal of the activation peptide By similarity.

Subcellular location

Cytoplasmic granule. Secretedextracellular spaceextracellular matrix By similarity. Note: Stored in intracellular granules.

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 repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 10181Activation peptide By similarity
PRO_0000028748
Chain102 – 466365Neutrophil collagenase
PRO_0000028749

Regions

Repeat277 – 32650Hemopexin 1
Repeat327 – 37347Hemopexin 2
Repeat375 – 42147Hemopexin 3
Repeat422 – 46544Hemopexin 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191 By similarity
Metal binding921Zinc 2; in inhibited form By similarity
Metal binding1581Calcium 1 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1751Calcium 2 By similarity
Metal binding1761Calcium 2; via carbonyl oxygen By similarity
Metal binding1781Calcium 2; via carbonyl oxygen By similarity
Metal binding1801Calcium 2; via carbonyl oxygen By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1901Calcium 1; via carbonyl oxygen By similarity
Metal binding1921Calcium 1; via carbonyl oxygen By similarity
Metal binding1941Calcium 1 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding1981Calcium 2 By similarity
Metal binding2011Calcium 2 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity
Metal binding2871Calcium 3; via carbonyl oxygen By similarity
Metal binding3791Calcium 3; via carbonyl oxygen By similarity
Metal binding4261Calcium 3; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond280 ↔ 465 Probable

Sequences

Sequence LengthMass (Da)Tools
O88766 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8B9DE97576E76C90

FASTA46653,277
        10         20         30         40         50         60 
MLHLKTLPFL FFFHTQLATA LPVPPEHLEE KNMKTAENYL RKFYHLPSNQ FRSARNATMI 

        70         80         90        100        110        120 
AEKLKEMQRF FGLPETGKPD AATIEIMEKP RCGVPDSGDF LLTPGSPKWT HTNLTYRIIN 

       130        140        150        160        170        180 
HTPQMSKAEV KTEIEKAFKI WSVPSTLTFT ETLEGEADIN IAFVSRDHGD NSPFDGPNGI 

       190        200        210        220        230        240 
LAHAFQPGRG IGGDAHFDSE ETWTQDSKNY NLFLVAAHEF GHSLGLSHST DPGALMYPNY 

       250        260        270        280        290        300 
AYREPSTYSL PQDDINGIQT IYGPSDNPVQ PTGPSTPTAC DPHLRFDAAT TLRGEIYFFK 

       310        320        330        340        350        360 
DKYFWRRHPQ LRTVDLNFIS LFWPFLPNGL QAAYEDFDRD LVFLFKGRQY WALSAYDLQQ 

       370        380        390        400        410        420 
GYPRDISNYG FPRSVQAIDA AVSYNGKTYF FVNNQCWRYD NQRRSMDPGY PTSIASVFPG 

       430        440        450        460 
INCRIDAVFQ QDSFFLFFSG PQYFAFNLVS RRVTRVARSN LWLNCP 

« Hide

References

[1]"Cloning, expression, characterization and activation properties of rat neutrophil collagenase (MMP-8)."
Overall C.M., Lowne D., Wells G., Burel S., Clements J.M.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Lewis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ007288 mRNA. Translation: CAA07432.1.
RefSeqNP_071557.1. NM_022221.1.
UniGeneRn.44474.

3D structure databases

ProteinModelPortalO88766.
SMRO88766. Positions 100-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000013936.

Chemistry

BindingDBO88766.
ChEMBLCHEMBL2312.

Protein family/group databases

MEROPSM10.002.

Proteomic databases

PaxDbO88766.
PRIDEO88766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID63849.
KEGGrno:63849.
UCSCRGD:631408. rat.

Organism-specific databases

CTD4317.
RGD631408. Mmp8.

Phylogenomic databases

eggNOGNOG258253.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidO88766.
KOK01402.
PhylomeDBO88766.

Gene expression databases

GenevestigatorO88766.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR028709. MMP1/MMP8.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF37. PTHR10201:SF37. 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]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612456.
PROO88766.

Entry information

Entry nameMMP8_RAT
AccessionPrimary (citable) accession number: O88766
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries