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Reviewed, UniProtKB/Swiss-Prot P50282 (MMP9_RAT)

Last modified February 9, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Matrix metalloproteinase-9
      Short name=MMP-9
    EC=3.4.24.35
Alternative name(s):
    92 kDa type IV collagenase
    92 kDa gelatinase
    Gelatinase B
      Short name=GELB
Gene names
Name: Mmp9
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments By similarity.

Catalytic activity

Cleavage of gelatin types I and V and collagen types IV and V.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Binds 3 calcium ions per subunit By similarity.

Subunit structure

Exists as monomer or homodimer; disulfide-linked By similarity. Exists also as heterodimer with a 25 kDa protein By similarity. Interacts with ECM1 By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix Probable.

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.

Post-translational modification

N- and O-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 3 fibronectin type-II domains.

Contains 4 hemopexin-like domains.

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Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processcell growth

Inferred from expression pattern. Source: RGD

collagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

ossification

Inferred from expression pattern. Source: RGD

positive regulation of synaptic plasticity

Inferred from mutant phenotype. Source: RGD

proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from direct assay. Source: RGD

response to ethanol

Inferred from expression pattern. Source: RGD

response to heat

Inferred from expression pattern. Source: RGD

response to hypoxia

Inferred from expression pattern. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern. Source: RGD

response to mechanical stimulus

Inferred from expression pattern. Source: RGD

response to organic cyclic substance

Inferred from expression pattern. Source: RGD

response to oxidative stress

Inferred from direct assay. Source: RGD

response to radiation

Inferred from expression pattern. Source: RGD

response to vitamin A

Inferred from expression pattern. Source: RGD

tissue remodeling

Inferred from direct assay. Source: RGD

   Cellular componentextracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

fibronectin binding

Inferred from physical interaction. Source: RGD

metalloendopeptidase 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 10788Activation peptide By similarity
PRO_0000028762
Chain108 – 708601Matrix metalloproteinase-9
PRO_0000028763

Regions

Domain226 – 27449Fibronectin type-II 1
Domain284 – 33249Fibronectin type-II 2
Domain343 – 39149Fibronectin type-II 3
Domain524 – 56845Hemopexin-like 1
Domain570 – 61142Hemopexin-like 2
Domain616 – 66247Hemopexin-like 3
Domain667 – 70741Hemopexin-like 4
Motif98 – 1058Cysteine switch By similarity

Sites

Active site4031 By similarity
Metal binding1001Zinc 2; in inhibited form By similarity
Metal binding1321Calcium 1 By similarity
Metal binding1661Calcium 2; via carbonyl oxygen By similarity
Metal binding1761Zinc 1; structural By similarity
Metal binding1781Zinc 1; structural By similarity
Metal binding1831Calcium 3 By similarity
Metal binding1841Calcium 3; via carbonyl oxygen By similarity
Metal binding1861Calcium 3; via carbonyl oxygen By similarity
Metal binding1881Calcium 3; via carbonyl oxygen By similarity
Metal binding1911Zinc 1; structural By similarity
Metal binding1981Calcium 2; via carbonyl oxygen By similarity
Metal binding2001Calcium 2; via carbonyl oxygen By similarity
Metal binding2021Calcium 2 By similarity
Metal binding2041Zinc 1; structural By similarity
Metal binding2061Calcium 3 By similarity
Metal binding2071Calcium 1 By similarity
Metal binding2091Calcium 1 By similarity
Metal binding2091Calcium 3 By similarity
Metal binding4021Zinc 2; catalytic By similarity
Metal binding4061Zinc 2; catalytic By similarity
Metal binding4121Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Disulfide bond231 ↔ 257 By similarity
Disulfide bond245 ↔ 272 By similarity
Disulfide bond289 ↔ 315 By similarity
Disulfide bond303 ↔ 330 By similarity
Disulfide bond348 ↔ 374 By similarity
Disulfide bond362 ↔ 389 By similarity
Disulfide bond519 ↔ 707 By similarity

Experimental info

Sequence conflict21S → N in AAA90911. Ref.1
Sequence conflict1121D → E in AAA90911. Ref.1
Sequence conflict326 – 3272AD → LY in AAA90911. Ref.1
Sequence conflict3641S → G in AAA90911. Ref.1
Sequence conflict4411H → Q in AAA90911. Ref.1
Sequence conflict4721S → P in AAA90911. Ref.1
Sequence conflict5151D → V in AAA90911. Ref.1
Sequence conflict5511N → S in AAA90911. Ref.1
Sequence conflict5661F → L in AAA90911. Ref.1
Sequence conflict5681S → A in AAA90911. Ref.1
Sequence conflict5791P → S in AAA90911. Ref.1
Sequence conflict586 – 5894LWAQ → SGRK in AAA90911. Ref.1
Sequence conflict5971S → T in AAA90911. Ref.1
Sequence conflict6691Q → H in AAA90911. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P50282-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D57DC0D1B93A778C

FASTA70878,611
        10         20         30         40         50         60 
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL YRYGYTRAAQ 

        70         80         90        100        110        120 
MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC GVPDVGKFQT FDGDLKWHHH 

       130        140        150        160        170        180 
NITYWIQSYT EDLPRDVIDD SFARAFAVWS AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY 

       190        200        210        220        230        240 
PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR 

       250        260        270        280        290        300 
SYLSCTTDGR NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY 

       310        320        330        340        350        360 
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF PFVFLGKQYS 

       370        380        390        400        410        420 
TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM 

       430        440        450        460        470        480 
YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP DPRPPATTAA EPQPTAPPTM CSTAPPMAYP 

       490        500        510        520        530        540 
TGGPTVAPTG APSPGPTGPP TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG 

       550        560        570        580        590        600 
RYWKFSNHGG NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG 

       610        620        630        640        650        660 
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV TRLDNEFSGV 

       670        680        690        700 
PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV TYDLLQCP

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References

[1]"The cDNA cloning and expression of the gene encoding rat gelatinase B."
Okada A., Santavicca M., Basset P.
Gene 164:317-321(1995) [PubMed: 7590350] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
[2]"Cloning of rat 92-kDa type IV collagenase and expression of an active recombinant catalytic domain."
Xia Y., Garcia G., Chen S., Wilson C.B., Feng L.
FEBS Lett. 382:285-288(1996) [PubMed: 8605986] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer 344.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U24441 mRNA. Translation: AAA90911.1.
U36476 mRNA. Translation: AAB01721.1.
IPIIPI00196591.
PIRJC4364.
S62907.
RefSeqNP_112317.1.
UniGeneRn.10209

3D structure databases

SMRP50282. Positions 29-445.
ModBaseSearch...

Protein-protein interaction databases

STRINGP50282.

Protein family/group databases

MEROPSM10.004.

Genome annotation databases

EnsemblENSRNOT00000067236; ENSRNOP00000059757; ENSRNOG00000017539; Rattus norvegicus. [Genome view]
GeneID81687.
KEGGrno:81687.
UCSCNM_031055. rat.

Organism-specific databases

CTD81687.
RGD621320. Mmp9.

Phylogenomic databases

eggNOGroNOG07270.
HOVERGENP50282.
InParanoidP50282.

Enzyme and pathway databases

BRENDA3.4.24.35. 248.

Gene expression databases

ArrayExpressP50282.
GenevestigatorP50282.
GermOnlineENSRNOG00000017539. Rattus norvegicus.

Family and domain databases

InterProIPR000562. FN_type2_col_bd.
IPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR013806. Kringle-like.
IPR001818. Pept_M10A_M12B.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 1 hit.
PfamPF00040. fn2. 3 hits.
PF00045. Hemopexin. 1 hit.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSPR00013. FNTYPEII.
PR00138. MATRIXIN.
SMARTSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 2 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615324.

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Entry information

Entry nameMMP9_RAT
AccessionPrimary (citable) accession number: P50282
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 9, 2010
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

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) · Sequences · References · Cross-references · Entry information · Relevant documents