Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi92Zinc 2; in inhibited formBy similarity1
Metal bindingi158Calcium 1By similarity1
Metal bindingi168Zinc 1By similarity1
Metal bindingi170Zinc 1By similarity1
Metal bindingi175Calcium 2By similarity1
Metal bindingi176Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi180Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi190Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi194Calcium 1By similarity1
Metal bindingi196Zinc 1By similarity1
Metal bindingi198Calcium 2By similarity1
Metal bindingi201Calcium 2By similarity1
Metal bindingi218Zinc 2; catalyticBy similarity1
Active sitei219PROSITE-ProRule annotation1
Metal bindingi222Zinc 2; catalyticBy similarity1
Metal bindingi228Zinc 2; catalyticBy similarity1
Metal bindingi287Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi379Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi426Calcium 3; via carbonyl oxygenBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: RGD
  • serine-type endopeptidase activity Source: UniProtKB
  • zinc ion binding Source: RGD

GO - Biological processi

  • collagen catabolic process Source: UniProtKB-KW
  • ossification Source: RGD
  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil collagenase (EC:3.4.24.34)
Alternative name(s):
Matrix metalloproteinase-8
Short name:
MMP-8
Gene namesi
Name:Mmp8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi631408. Mmp8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
PropeptideiPRO_000002874821 – 101Activation peptideBy similarityAdd BLAST81
ChainiPRO_0000028749102 – 466Neutrophil collagenaseAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi56N-linked (GlcNAc...)Sequence analysis1
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi280 ↔ 465Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiO88766.
PRIDEiO88766.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013936.

Chemistry databases

BindingDBiO88766.

Structurei

3D structure databases

ProteinModelPortaliO88766.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati277 – 326Hemopexin 1Add BLAST50
Repeati327 – 373Hemopexin 2Add BLAST47
Repeati375 – 421Hemopexin 3Add BLAST47
Repeati422 – 465Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi90 – 97Cysteine switchBy similarity8

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO88766.
KOiK01402.
PhylomeDBiO88766.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028709. 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]
PANTHERiPTHR10201:SF137. PTHR10201:SF137. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHLKTLPFL FFFHTQLATA LPVPPEHLEE KNMKTAENYL RKFYHLPSNQ
60 70 80 90 100
FRSARNATMI AEKLKEMQRF FGLPETGKPD AATIEIMEKP RCGVPDSGDF
110 120 130 140 150
LLTPGSPKWT HTNLTYRIIN HTPQMSKAEV KTEIEKAFKI WSVPSTLTFT
160 170 180 190 200
ETLEGEADIN IAFVSRDHGD NSPFDGPNGI LAHAFQPGRG IGGDAHFDSE
210 220 230 240 250
ETWTQDSKNY NLFLVAAHEF GHSLGLSHST DPGALMYPNY AYREPSTYSL
260 270 280 290 300
PQDDINGIQT IYGPSDNPVQ PTGPSTPTAC DPHLRFDAAT TLRGEIYFFK
310 320 330 340 350
DKYFWRRHPQ LRTVDLNFIS LFWPFLPNGL QAAYEDFDRD LVFLFKGRQY
360 370 380 390 400
WALSAYDLQQ GYPRDISNYG FPRSVQAIDA AVSYNGKTYF FVNNQCWRYD
410 420 430 440 450
NQRRSMDPGY PTSIASVFPG INCRIDAVFQ QDSFFLFFSG PQYFAFNLVS
460
RRVTRVARSN LWLNCP
Length:466
Mass (Da):53,277
Last modified:November 1, 1998 - v1
Checksum:i8B9DE97576E76C90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007288 mRNA. Translation: CAA07432.1.
RefSeqiNP_071557.1. NM_022221.1.
UniGeneiRn.44474.

Genome annotation databases

GeneIDi63849.
KEGGirno:63849.
UCSCiRGD:631408. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ007288 mRNA. Translation: CAA07432.1.
RefSeqiNP_071557.1. NM_022221.1.
UniGeneiRn.44474.

3D structure databases

ProteinModelPortaliO88766.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013936.

Chemistry databases

BindingDBiO88766.
ChEMBLiCHEMBL2312.

Protein family/group databases

MEROPSiM10.002.

Proteomic databases

PaxDbiO88766.
PRIDEiO88766.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi63849.
KEGGirno:63849.
UCSCiRGD:631408. rat.

Organism-specific databases

CTDi4317.
RGDi631408. Mmp8.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO88766.
KOiK01402.
PhylomeDBiO88766.

Miscellaneous databases

PROiO88766.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028709. 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]
PANTHERiPTHR10201:SF137. PTHR10201:SF137. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP8_RAT
AccessioniPrimary (citable) accession number: O88766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.