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P41246 (MMP9_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-9
Short name=MMP-9
EC=3.4.24.35
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name=GELB
Gene names
Name:MMP9
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Tissue specificity

Osteoclasts.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 10687Activation peptide By similarity
PRO_0000028760
Chain107 – 707601Matrix metalloproteinase-9
PRO_0000028761

Regions

Domain225 – 27349Fibronectin type-II 1
Domain283 – 33149Fibronectin type-II 2
Domain342 – 39049Fibronectin type-II 3
Domain521 – 56545Hemopexin-like 1
Domain567 – 60842Hemopexin-like 2
Domain613 – 65947Hemopexin-like 3
Domain661 – 70444Hemopexin-like 4
Motif97 – 1048Cysteine switch By similarity

Sites

Active site4021 By similarity
Metal binding991Zinc 2; in inhibited form By similarity
Metal binding1311Calcium 1 By similarity
Metal binding1651Calcium 2; via carbonyl oxygen By similarity
Metal binding1751Zinc 1; structural By similarity
Metal binding1771Zinc 1; structural By similarity
Metal binding1821Calcium 3 By similarity
Metal binding1831Calcium 3; via carbonyl oxygen By similarity
Metal binding1851Calcium 3; via carbonyl oxygen By similarity
Metal binding1871Calcium 3; via carbonyl oxygen By similarity
Metal binding1901Zinc 1; structural By similarity
Metal binding1971Calcium 2; via carbonyl oxygen By similarity
Metal binding1991Calcium 2; via carbonyl oxygen By similarity
Metal binding2011Calcium 2 By similarity
Metal binding2031Zinc 1; structural By similarity
Metal binding2051Calcium 3 By similarity
Metal binding2061Calcium 1 By similarity
Metal binding2081Calcium 1 By similarity
Metal binding2081Calcium 3 By similarity
Metal binding4011Zinc 2; catalytic By similarity
Metal binding4051Zinc 2; catalytic By similarity
Metal binding4111Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Disulfide bond230 ↔ 256 By similarity
Disulfide bond244 ↔ 271 By similarity
Disulfide bond288 ↔ 314 By similarity
Disulfide bond302 ↔ 329 By similarity
Disulfide bond347 ↔ 373 By similarity
Disulfide bond361 ↔ 388 By similarity
Disulfide bond516 ↔ 704 By similarity

Experimental info

Sequence conflict761K → P in AAA64358. Ref.2
Sequence conflict100 – 1023GVP → ASR in AAA64358. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P41246 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 053BCE8DC4D4758F

FASTA70778,308
        10         20         30         40         50         60 
MSPRQPLVLA LLVLGCCSAA PRRRQPTLVV FPGELRTRLT DRQLAEEYLF RYGYTRVASM 

        70         80         90        100        110        120 
HGDSQSLRLP LLLLQKHLSL PETGELDNAT LEAMRAPRCG VPDVGKFQTF EGDLKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRDVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGPGIQG DAHFDDEELW SLGKGVVVPT YFGNADGAPC HFPFTFEGRS 

       250        260        270        280        290        300 
YTACTTDGRS DGMAWCSTTA DYDTDRRFGF CPSERLYTQD GNADGKPCEF PFIFQGRTYS 

       310        320        330        340        350        360 
ACTTDGRSDG HRWCATTASY DKDKLYGFCP TRADSTVVGG NSAGELCVFP FVFLGKEYSS 

       370        380        390        400        410        420 
CTSEGRRDGR LWCATTSNFD SDKKWGFCPD KGYSLFLVAA HEFGHALGLD HSSVPERLMY 

       430        440        450        460        470        480 
PMYRYLEGSP LHEDDVRGIQ HLYGPNPNPQ PPATTTPEPQ PTAPPTACPT WPATVRPSEH 

       490        500        510        520        530        540 
PTTSPTGAPS AGPTGPPTAS PSAAPTASLD PAEDVCNVNV FDAIAEIGNK LHVFKDGRYW 

       550        560        570        580        590        600 
RFSEGSGRRP QGPFLIADTW PALPAKLDSA FEEPLTKKLF FFSGRQVWVY TGASVLGPRR 

       610        620        630        640        650        660 
LDKLGLGPEV PHVTGALPRA GGKVLLFGAQ RFWRFDVKTQ TVDSRSGAPV DQMFPGVPLN 

       670        680        690        700 
THDVFQYREK AYFCQDRFFW RVSTRNEVNL VDQVGYVSFD ILHCPED

« Hide

References

[1]"Identification of matrix metalloproteinase 9 in rabbit osteoclasts."
Tezuka K.I., Nemoto K., Tezuka Y., Sato T., Ikeda Y., Kobori M., Kawashima H., Eguchi H., Hakeda Y., Kumegawa M.
J. Biol. Chem. 269:15006-15009(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Japanese white.
Tissue: Bone.
[2]"The rabbit gene for 92-kDa matrix metalloproteinase. Role of AP1 and AP2 in cell type-specific transcription."
Fini M.E., Bartlett J.D., Matsubara M., Rinehart W.B., Mody M.K., Girard M.T., Rainville M.
J. Biol. Chem. 269:28620-28628(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
Strain: New Zealand white.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D26514 mRNA. Translation: BAA05520.1.
L36050 Genomic DNA. Translation: AAA64358.1.
PIRA53796.
RefSeqNP_001075672.1. NM_001082203.1.
UniGeneOcu.1773.

3D structure databases

ProteinModelPortalP41246.
SMRP41246. Positions 29-444, 513-707.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000025066.

Protein family/group databases

MEROPSM10.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008993.

Organism-specific databases

CTD4318.

Phylogenomic databases

eggNOGNOG328372.
HOGENOMHOG000217926.
HOVERGENHBG052484.
OrthoDBEOG4H9XJZ.

Family and domain databases

Gene3D2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProIPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR006970. PT.
[Graphical view]
PfamPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF57440. Kringle-like. 3 hits.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMP9_RABIT
AccessionPrimary (citable) accession number: P41246
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents