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P52176 (MMP9_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length712 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

Secretedextracellular spaceextracellular 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 repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 10687Activation peptide
PRO_0000028750
Chain107 – 712606Matrix metalloproteinase-9
PRO_0000028751

Regions

Domain225 – 27349Fibronectin type-II 1
Domain283 – 33149Fibronectin type-II 2
Domain342 – 39049Fibronectin type-II 3
Repeat523 – 56846Hemopexin 1
Repeat569 – 61345Hemopexin 2
Repeat615 – 66248Hemopexin 3
Repeat663 – 70947Hemopexin 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

Glycosylation381N-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 bond521 ↔ 709 By similarity

Sequences

Sequence LengthMass (Da)Tools
P52176 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E7FDA28372AEE0CE

FASTA71279,088
        10         20         30         40         50         60 
MSPLQPLVLA LLVLACCSAV PRRRQPTVVV FPGEPRTNLT NRQLAEEYLY RYGYTPGAEL 

        70         80         90        100        110        120 
SEDGQSLQRA LLRFQRRLSL PETGELDSTT LNAMRAPRCG VPDVGRFQTF EGELKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY GPEADIVIQF GVREHGDGYP 

       190        200        210        220        230        240 
FDGKNGLLAH AFPPGKGIQG DAHFDDEELW SLGKGVVIPT YFGNAKGAAC HFPFTFEGRS 

       250        260        270        280        290        300 
YSACTTDGRS DDMLWCSTTA DYDADRQFGF CPSERLYTQD GNADGKPCVF PFTFQGRTYS 

       310        320        330        340        350        360 
ACTSDGRSDG YRWCATTANY DQDKLYGFCP TRVDATVTGG NAAGELCVFP FTFLGKEYSA 

       370        380        390        400        410        420 
CTREGRNDGH LWCATTSNFD KDKKWGFCPD QGYSLFLVAA HEFGHALGLD HTSVPEALMY 

       430        440        450        460        470        480 
PMYRFTEEHP LHRDDVQGIQ HLYGPRPEPE PRPPTTTTTT TTEPQPTAPP TVCVTGPPTA 

       490        500        510        520        530        540 
RPSEGPTTGP TGPPAAGPTG PPTAGPSAAP TESPDPAEDV CNVDIFDAIA EIRNRLHFFK 

       550        560        570        580        590        600 
AGKYWRLSEG GGRRVQGPFL VKSKWPALPR KLDSAFEDPL TKKIFFFSGR QVWVYTGASL 

       610        620        630        640        650        660 
LGPRRLDKLG LGPEVAQVTG ALPRPEGKVL LFSGQSFWRF DVKTQKVDPQ SVTPVDQMFP 

       670        680        690        700        710 
GVPISTHDIF QYQEKAYFCQ DHFYWRVSSQ NEVNQVDYVG YVTFDLLKCP ED 

« Hide

References

« Hide 'large scale' references
[1]"Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes."
Baylis H.A., Megson A., Hall R.
Mol. Biochem. Parasitol. 69:211-222(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leukocyte.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78324 mRNA. Translation: CAA55127.1.
BC142430 mRNA. Translation: AAI42431.1.
PIRI46031.
RefSeqNP_777169.1. NM_174744.2.
UniGeneBt.4714.

3D structure databases

ProteinModelPortalP52176.
SMRP52176. Positions 29-444, 518-712.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL5846.

Protein family/group databases

MEROPSM10.004.

Proteomic databases

PaxDbP52176.
PRIDEP52176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282871.
KEGGbta:282871.

Organism-specific databases

CTD4318.

Phylogenomic databases

eggNOGNOG328372.
HOGENOMHOG000217926.
HOVERGENHBG052484.
InParanoidP52176.
KOK01403.

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.
IPR013806. Kringle-like.
IPR024079. MetalloPept_cat_dom.
IPR028688. MMP9.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR006970. PT.
[Graphical view]
PANTHERPTHR10201:SF30. PTHR10201:SF30. 1 hit.
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]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806399.

Entry information

Entry nameMMP9_BOVIN
AccessionPrimary (citable) accession number: P52176
Secondary accession number(s): A5PKB8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 116 of the entry and version 1 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