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Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Activity 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

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1202395 Mmp8

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagineSequence analysis1
Glycosylationi112N-linked (GlcNAc...) asparagineSequence 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 Expressed in 50 organ(s), highest expression level in bone marrow
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

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
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028709 MMP8
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
PANTHERiPTHR10201:SF137 PTHR10201:SF137, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

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

Similar proteinsi

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
PROiPR:O70138
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005800 Expressed in 50 organ(s), highest expression level in bone marrow
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
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028709 MMP8
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
PANTHERiPTHR10201:SF137 PTHR10201:SF137, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMMP8_MOUSE
AccessioniPrimary (citable) accession number: O70138
Secondary accession number(s): O88733, Q6GTR5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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