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Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Mus musculus (Mouse)
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. May play a role in the degradation of collagen fibers during uterine involution.

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. Activated by matrilysin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi91Zinc 2; in inhibited formBy similarity1
Metal bindingi157Calcium 1By similarity1
Metal bindingi167Zinc 1By similarity1
Metal bindingi169Zinc 1By similarity1
Metal bindingi174Calcium 2By similarity1
Metal bindingi175Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi177Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi179Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi182Zinc 1By similarity1
Metal bindingi189Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi193Calcium 1By similarity1
Metal bindingi195Zinc 1By similarity1
Metal bindingi197Calcium 2By similarity1
Metal bindingi200Calcium 2By similarity1
Metal bindingi217Zinc 2; catalyticBy similarity1
Active sitei218PROSITE-ProRule annotation1
Metal bindingi221Zinc 2; catalyticBy similarity1
Metal bindingi227Zinc 2; catalyticBy similarity1
Metal bindingi286Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi378Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi425Calcium 3; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1592389. Activation of Matrix Metalloproteinases.
R-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiM10.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutrophil collagenase (EC:3.4.24.34)
Alternative name(s):
Collagenase 2
Matrix metalloproteinase-8
Short name:
MMP-8
Gene namesi
Name:Mmp8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1202395. Mmp8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
PropeptideiPRO_000002874621 – 100Activation peptideAdd BLAST80
ChainiPRO_0000028747101 – 465Neutrophil collagenaseAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Glycosylationi112N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi279 ↔ 464By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO70138.
PaxDbiO70138.
PRIDEiO70138.

PTM databases

PhosphoSitePlusiO70138.

Expressioni

Tissue specificityi

Neutrophils. Expressed in uterus. Low levels in kidney and muscle.

Developmental stagei

Expressed in late embryogenesis and in the involuting postpartum uterus.

Gene expression databases

BgeeiENSMUSG00000005800.
CleanExiMM_MMP8.
GenevisibleiO70138. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018765.

Structurei

3D structure databases

ProteinModelPortaliO70138.
SMRiO70138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati276 – 325Hemopexin 1Add BLAST50
Repeati326 – 372Hemopexin 2Add BLAST47
Repeati374 – 420Hemopexin 3Add BLAST47
Repeati421 – 464Hemopexin 4Add BLAST44

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi89 – 96Cysteine 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.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO70138.
KOiK01402.
OMAiEETWTKT.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

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. 3 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.

O70138-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRLKTLPLL IFLHTQLANA FPVPEHLEEK NIKTAENYLR KFYNLPSNQF
60 70 80 90 100
RSSRNATMVA EKLKEMQRFF SLAETGKLDA ATMGIMEMPR CGVPDSGDFL
110 120 130 140 150
LTPGSPKWTH TNLTYRIINH TPQLSRAEVK TAIEKAFHVW SVASPLTFTE
160 170 180 190 200
ILQGEADINI AFVSRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDSEE
210 220 230 240 250
TWTQDSKNYN LFLVAAHEFG HSLGLSHSTD PGALMYPNYA YREPSTYSLP
260 270 280 290 300
QDDINGIQTI YGPSDNPIQP TGPSTPKACD PHLRFDATTT LRGEIYFFKD
310 320 330 340 350
KYFWRRHPQL RTVDLNFISL FWPFLPNGLQ AAYEDFDRDL VFLFKGRQYW
360 370 380 390 400
ALSGYDLQQG YPRDISNYGF PRSVQAIDAA VSYNGKTYFF INNQCWRYDN
410 420 430 440 450
QRRSMDPGYP KSIPSMFPGV NCRVDAVFLQ DSFFLFFSGP QYFAFNFVSH
460
RVTRVARSNL WLNCS
Length:465
Mass (Da):53,126
Last modified:July 27, 2011 - v2
Checksum:i448AEC59639E9237
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116R → W in AAC12707 (PubMed:9516153).Curated1
Sequence conflicti300D → E in AAC12707 (PubMed:9516153).Curated1
Sequence conflicti324F → G in AAC12707 (PubMed:9516153).Curated1
Sequence conflicti401Q → E in AAC12707 (PubMed:9516153).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96696 mRNA. Translation: AAC12707.1.
Y13342 mRNA. Translation: CAA73786.1.
AK089234 mRNA. Translation: BAC40805.1.
AK137468 mRNA. Translation: BAE23365.1.
AK154937 mRNA. Translation: BAE32938.1.
CH466522 Genomic DNA. Translation: EDL24937.1.
BC042742 mRNA. Translation: AAH42742.1.
CCDSiCCDS22808.1.
RefSeqiNP_032637.3. NM_008611.4.
UniGeneiMm.16415.

Genome annotation databases

EnsembliENSMUST00000018765; ENSMUSP00000018765; ENSMUSG00000005800.
GeneIDi17394.
KEGGimmu:17394.
UCSCiuc009ocr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96696 mRNA. Translation: AAC12707.1.
Y13342 mRNA. Translation: CAA73786.1.
AK089234 mRNA. Translation: BAC40805.1.
AK137468 mRNA. Translation: BAE23365.1.
AK154937 mRNA. Translation: BAE32938.1.
CH466522 Genomic DNA. Translation: EDL24937.1.
BC042742 mRNA. Translation: AAH42742.1.
CCDSiCCDS22808.1.
RefSeqiNP_032637.3. NM_008611.4.
UniGeneiMm.16415.

3D structure databases

ProteinModelPortaliO70138.
SMRiO70138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018765.

Protein family/group databases

MEROPSiM10.002.

PTM databases

PhosphoSitePlusiO70138.

Proteomic databases

MaxQBiO70138.
PaxDbiO70138.
PRIDEiO70138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018765; ENSMUSP00000018765; ENSMUSG00000005800.
GeneIDi17394.
KEGGimmu:17394.
UCSCiuc009ocr.2. mouse.

Organism-specific databases

CTDi4317.
MGIiMGI:1202395. Mmp8.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO70138.
KOiK01402.
OMAiEETWTKT.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1592389. Activation of Matrix Metalloproteinases.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiMmp8. mouse.
PROiO70138.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005800.
CleanExiMM_MMP8.
GenevisibleiO70138. MM.

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. 3 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_MOUSE
AccessioniPrimary (citable) accession number: O70138
Secondary accession number(s): O88733, Q6GTR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 144 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.