Neutrophil collagenase precursor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot O70138 (MMP8_MOUSE)

Last modified October 13, 2009. Version 88. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Neutrophil collagenase
    EC=3.4.24.34
Alternative name(s):
    Matrix metalloproteinase-8
      Short name=MMP-8
    Collagenase 2

Gene names

Name:

Mmp8

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	465 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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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. Secreted › extracellular space › extracellular 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-like domains.

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Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

By similarity

Propeptide

21 – 100

Activation peptide

PRO_0000028746

Chain

101 – 465

365

Neutrophil collagenase

PRO_0000028747

Regions

Domain

285 – 327

Hemopexin-like 1

Domain

329 – 372

Hemopexin-like 2

Domain

377 – 422

Hemopexin-like 3

Domain

424 – 464

Hemopexin-like 4

Motif

89 – 96

Cysteine switch By similarity

Sites

Active site

218

By similarity

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

157

Calcium 1 By similarity

Metal binding

167

Zinc 1 By similarity

Metal binding

169

Zinc 1 By similarity

Metal binding

174

Calcium 2 By similarity

Metal binding

175

Calcium 2; via carbonyl oxygen By similarity

Metal binding

177

Calcium 2; via carbonyl oxygen By similarity

Metal binding

179

Calcium 2; via carbonyl oxygen By similarity

Metal binding

182

Zinc 1 By similarity

Metal binding

189

Calcium 1; via carbonyl oxygen By similarity

Metal binding

191

Calcium 1; via carbonyl oxygen By similarity

Metal binding

193

Calcium 1 By similarity

Metal binding

195

Zinc 1 By similarity

Metal binding

197

Calcium 2 By similarity

Metal binding

200

Calcium 2 By similarity

Metal binding

217

Zinc 2; catalytic By similarity

Metal binding

221

Zinc 2; catalytic By similarity

Metal binding

227

Zinc 2; catalytic By similarity

Metal binding

286

Calcium 3; via carbonyl oxygen By similarity

Metal binding

378

Calcium 3; via carbonyl oxygen By similarity

Metal binding

425

Calcium 3; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

112

N-linked (GlcNAc...) Potential

Disulfide bond

279 ↔ 464

By similarity

Experimental info

Sequence conflict

116

W → R in CAA73786. Ref.2

Sequence conflict

300

E → D in CAA73786. Ref.2

Sequence conflict

324

G → F in CAA73786. Ref.2

Sequence conflict

401

E → Q in CAA73786. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O70138-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 7C67851D3AFB9448
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FASTA

465

53,081

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

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

       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 LRGEIYFFKE 

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

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

       430        440        450        460 
NCRVDAVFLQ DSFFLFFSGP QYFAFNFVSH RVTRVARSNL WLNCS

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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: 9516153] [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: 9727011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Sv. Tissue: Embryo.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U96696 mRNA. Translation: AAC12707.1. Y13342 mRNA. Translation: CAA73786.1.
IPI	IPI00115635.
RefSeq	NP_032637.3.
UniGene	Mm.16415
3D structure databases
HSSP	HSSP built from PDB template 1BZS based on UniProtKB P22894.
ModBase	Search...
Protein-protein interaction databases
STRING	O70138.
Protein family/group databases
MEROPS	M10.002.
Proteomic databases
PRIDE	O70138.
Genome annotation databases
Ensembl	ENSMUST00000018765; ENSMUSP00000018765; ENSMUSG00000005800; Mus musculus. [Genome view]
GeneID	17394.
KEGG	mmu:17394.
Organism-specific databases
MGI	MGI:1202395. Mmp8.
Phylogenomic databases
HOGENOM	O70138.
HOVERGEN	O70138.
Enzyme and pathway databases
BRENDA	3.4.24.34. 244.
Gene expression databases
ArrayExpress	O70138.
Bgee	O70138.
CleanEx	MM_MMP8.
Genevestigator	O70138.
GermOnline	ENSMUSG00000005800. Mus musculus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

MMP8_MOUSE

Accession

Primary (citable) accession number: O70138
Secondary accession number(s): O88733

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	October 13, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents