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Protein

Neutrophil collagenase

Gene

Mmp8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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: RGD

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi631408 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

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...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence 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
SMRiO88766
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

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
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 2 hits
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
IPR036366 PGBDSf
PANTHERiPTHR10201:SF137 PTHR10201:SF137, 1 hit
PfamiView protein in Pfam
PF00045 Hemopexin, 4 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.

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

Similar proteinsi

Entry informationi

Entry nameiMMP8_RAT
AccessioniPrimary (citable) accession number: O88766
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health