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O70138

- MMP8_MOUSE

UniProt

O70138 - MMP8_MOUSE

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Protein

Neutrophil collagenase

Gene
Mmp8
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Binds 3 calcium ions per subunit By similarity.
Binds 2 zinc ions per subunit By similarity.

Enzyme regulationi

Cannot be activated without removal of the activation peptide. Activated by matrilysin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc 2; in inhibited form By similarity
Metal bindingi157 – 1571Calcium 1 By similarity
Metal bindingi167 – 1671Zinc 1 By similarity
Metal bindingi169 – 1691Zinc 1 By similarity
Metal bindingi174 – 1741Calcium 2 By similarity
Metal bindingi175 – 1751Calcium 2; via carbonyl oxygen By similarity
Metal bindingi177 – 1771Calcium 2; via carbonyl oxygen By similarity
Metal bindingi179 – 1791Calcium 2; via carbonyl oxygen By similarity
Metal bindingi182 – 1821Zinc 1 By similarity
Metal bindingi189 – 1891Calcium 1; via carbonyl oxygen By similarity
Metal bindingi191 – 1911Calcium 1; via carbonyl oxygen By similarity
Metal bindingi193 – 1931Calcium 1 By similarity
Metal bindingi195 – 1951Zinc 1 By similarity
Metal bindingi197 – 1971Calcium 2 By similarity
Metal bindingi200 – 2001Calcium 2 By similarity
Metal bindingi217 – 2171Zinc 2; catalytic By similarity
Active sitei218 – 2181 By similarity
Metal bindingi221 – 2211Zinc 2; catalytic By similarity
Metal bindingi227 – 2271Zinc 2; catalytic By similarity
Metal bindingi286 – 2861Calcium 3; via carbonyl oxygen By similarity
Metal bindingi378 – 3781Calcium 3; via carbonyl oxygen By similarity
Metal bindingi425 – 4251Calcium 3; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. serine-type endopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

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
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1202395. Mmp8.

Subcellular locationi

Cytoplasmic granule. Secretedextracellular spaceextracellular matrix
Note: Stored in intracellular granules and released during inflammatory conditions.

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 By similarityAdd
BLAST
Propeptidei21 – 10080Activation peptidePRO_0000028746Add
BLAST
Chaini101 – 465365Neutrophil collagenasePRO_0000028747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi112 – 1121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi279 ↔ 464 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiO70138.

PTM databases

PhosphoSiteiO70138.

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

BgeeiO70138.
CleanExiMM_MMP8.
GenevestigatoriO70138.

Structurei

3D structure databases

ProteinModelPortaliO70138.
SMRiO70138. Positions 32-464.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati276 – 32550Hemopexin 1Add
BLAST
Repeati326 – 37247Hemopexin 2Add
BLAST
Repeati374 – 42047Hemopexin 3Add
BLAST
Repeati421 – 46444Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 968Cysteine switch By similarity

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.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG258253.
GeneTreeiENSGT00730000110530.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ6GTR5.
KOiK01402.
OMAiYAFREPS.
OrthoDBiEOG7XPZ57.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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

MFRLKTLPLL IFLHTQLANA FPVPEHLEEK NIKTAENYLR KFYNLPSNQF    50
RSSRNATMVA EKLKEMQRFF SLAETGKLDA ATMGIMEMPR CGVPDSGDFL 100
LTPGSPKWTH TNLTYRIINH TPQLSRAEVK TAIEKAFHVW SVASPLTFTE 150
ILQGEADINI AFVSRDHGDN SPFDGPNGIL AHAFQPGQGI GGDAHFDSEE 200
TWTQDSKNYN LFLVAAHEFG HSLGLSHSTD PGALMYPNYA YREPSTYSLP 250
QDDINGIQTI YGPSDNPIQP TGPSTPKACD PHLRFDATTT LRGEIYFFKD 300
KYFWRRHPQL RTVDLNFISL FWPFLPNGLQ AAYEDFDRDL VFLFKGRQYW 350
ALSGYDLQQG YPRDISNYGF PRSVQAIDAA VSYNGKTYFF INNQCWRYDN 400
QRRSMDPGYP KSIPSMFPGV NCRVDAVFLQ DSFFLFFSGP QYFAFNFVSH 450
RVTRVARSNL WLNCS 465
Length:465
Mass (Da):53,126
Last modified:July 27, 2011 - v2
Checksum:i448AEC59639E9237
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161R → W in AAC12707. 1 Publication
Sequence conflicti300 – 3001D → E in AAC12707. 1 Publication
Sequence conflicti324 – 3241F → G in AAC12707. 1 Publication
Sequence conflicti401 – 4011Q → E in AAC12707. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22808.1.
RefSeqi NP_032637.3. NM_008611.4.
UniGenei Mm.16415.

3D structure databases

ProteinModelPortali O70138.
SMRi O70138. Positions 32-464.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.002.

PTM databases

PhosphoSitei O70138.

Proteomic databases

PRIDEi O70138.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018765 ; ENSMUSP00000018765 ; ENSMUSG00000005800 .
GeneIDi 17394.
KEGGi mmu:17394.
UCSCi uc009ocr.2. mouse.

Organism-specific databases

CTDi 4317.
MGIi MGI:1202395. Mmp8.

Phylogenomic databases

eggNOGi NOG258253.
GeneTreei ENSGT00730000110530.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi Q6GTR5.
KOi K01402.
OMAi YAFREPS.
OrthoDBi EOG7XPZ57.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP8. mouse.
NextBioi 292028.
PROi O70138.
SOURCEi Search...

Gene expression databases

Bgeei O70138.
CleanExi MM_MMP8.
Genevestigatori O70138.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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 ]
PANTHERi PTHR10201:SF137. PTHR10201:SF137. 1 hit.
Pfami PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the cDNA for mouse neutrophil collagenase: demonstration of shared negative regulatory pathways for neutrophil secondary granule protein gene expression."
    Lawson N.D., Khanna-Gupta A., Berliner N.
    Blood 91:2517-2524(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Collagenase 2 (MMP-8) expression in murine tissue-remodelling processes. Analysis of its potential role in postpartum involution of the uterus."
    Balbin M., Fueyo A., Knaeuper V., Pendas A.M., Lopez J.M., Jimenez M.G., Murphy G., Lopez-Otin C.
    J. Biol. Chem. 273:23959-23968(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/Sv.
    Tissue: Embryo.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone and Dendritic cell.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129.
    Tissue: Mammary tumor.

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: September 3, 2014
This is version 129 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

External Data

Dasty 3

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