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O70138 (MMP8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutrophil collagenase

EC=3.4.24.34
Alternative name(s):
Collagenase 2
Matrix metalloproteinase-8
Short name=MMP-8
Gene names
Name:Mmp8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution.

Catalytic activity

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.

Cofactor

Binds 3 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

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

Subcellular location

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

Tissue specificity

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

Developmental stage

Expressed in late embryogenesis and in the involuting postpartum uterus.

Domain

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 similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 10080Activation peptide
PRO_0000028746
Chain101 – 465365Neutrophil collagenase
PRO_0000028747

Regions

Repeat276 – 32550Hemopexin 1
Repeat326 – 37247Hemopexin 2
Repeat374 – 42047Hemopexin 3
Repeat421 – 46444Hemopexin 4
Motif89 – 968Cysteine switch By similarity

Sites

Active site2181 By similarity
Metal binding911Zinc 2; in inhibited form By similarity
Metal binding1571Calcium 1 By similarity
Metal binding1671Zinc 1 By similarity
Metal binding1691Zinc 1 By similarity
Metal binding1741Calcium 2 By similarity
Metal binding1751Calcium 2; via carbonyl oxygen By similarity
Metal binding1771Calcium 2; via carbonyl oxygen By similarity
Metal binding1791Calcium 2; via carbonyl oxygen By similarity
Metal binding1821Zinc 1 By similarity
Metal binding1891Calcium 1; via carbonyl oxygen By similarity
Metal binding1911Calcium 1; via carbonyl oxygen By similarity
Metal binding1931Calcium 1 By similarity
Metal binding1951Zinc 1 By similarity
Metal binding1971Calcium 2 By similarity
Metal binding2001Calcium 2 By similarity
Metal binding2171Zinc 2; catalytic By similarity
Metal binding2211Zinc 2; catalytic By similarity
Metal binding2271Zinc 2; catalytic By similarity
Metal binding2861Calcium 3; via carbonyl oxygen By similarity
Metal binding3781Calcium 3; via carbonyl oxygen By similarity
Metal binding4251Calcium 3; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Disulfide bond279 ↔ 464 By similarity

Experimental info

Sequence conflict1161R → W in AAC12707. Ref.1
Sequence conflict3001D → E in AAC12707. Ref.1
Sequence conflict3241F → G in AAC12707. Ref.1
Sequence conflict4011Q → E in AAC12707. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O70138 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 448AEC59639E9237

FASTA46553,126
        10         20         30         40         50         60 
MFRLKTLPLL IFLHTQLANA FPVPEHLEEK NIKTAENYLR KFYNLPSNQF RSSRNATMVA 

        70         80         90        100        110        120 
EKLKEMQRFF SLAETGKLDA ATMGIMEMPR CGVPDSGDFL LTPGSPKWTH TNLTYRIINH 

       130        140        150        160        170        180 
TPQLSRAEVK TAIEKAFHVW SVASPLTFTE ILQGEADINI AFVSRDHGDN SPFDGPNGIL 

       190        200        210        220        230        240 
AHAFQPGQGI GGDAHFDSEE TWTQDSKNYN LFLVAAHEFG HSLGLSHSTD PGALMYPNYA 

       250        260        270        280        290        300 
YREPSTYSLP QDDINGIQTI YGPSDNPIQP TGPSTPKACD PHLRFDATTT LRGEIYFFKD 

       310        320        330        340        350        360 
KYFWRRHPQL RTVDLNFISL FWPFLPNGLQ AAYEDFDRDL VFLFKGRQYW ALSGYDLQQG 

       370        380        390        400        410        420 
YPRDISNYGF PRSVQAIDAA VSYNGKTYFF INNQCWRYDN QRRSMDPGYP KSIPSMFPGV 

       430        440        450        460 
NCRVDAVFLQ DSFFLFFSGP QYFAFNFVSH RVTRVARSNL WLNCS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22808.1.
RefSeqNP_032637.3. NM_008611.4.
UniGeneMm.16415.

3D structure databases

ProteinModelPortalO70138.
SMRO70138. Positions 32-464.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.002.

PTM databases

PhosphoSiteO70138.

Proteomic databases

PRIDEO70138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018765; ENSMUSP00000018765; ENSMUSG00000005800.
GeneID17394.
KEGGmmu:17394.
UCSCuc009ocr.2. mouse.

Organism-specific databases

CTD4317.
MGIMGI:1202395. Mmp8.

Phylogenomic databases

eggNOGNOG258253.
GeneTreeENSGT00730000110530.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ6GTR5.
KOK01402.
OMAYAFREPS.
OrthoDBEOG7XPZ57.
TreeFamTF315428.

Gene expression databases

BgeeO70138.
CleanExMM_MMP8.
GenevestigatorO70138.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201:SF137. PTHR10201:SF137. 1 hit.
PfamPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMMP8. mouse.
NextBio292028.
PROO70138.
SOURCESearch...

Entry information

Entry nameMMP8_MOUSE
AccessionPrimary (citable) accession number: O70138
Secondary accession number(s): O88733, Q6GTR5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot