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P52176

- MMP9_BOVIN

UniProt

P52176 - MMP9_BOVIN

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Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit.By similarity
Binds 3 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Zinc 2; in inhibited formBy similarity
Metal bindingi131 – 1311Calcium 1By similarity
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi175 – 1751Zinc 1; structuralBy similarity
Metal bindingi177 – 1771Zinc 1; structuralBy similarity
Metal bindingi182 – 1821Calcium 3By similarity
Metal bindingi183 – 1831Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi185 – 1851Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi190 – 1901Zinc 1; structuralBy similarity
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi199 – 1991Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi201 – 2011Calcium 2By similarity
Metal bindingi203 – 2031Zinc 1; structuralBy similarity
Metal bindingi205 – 2051Calcium 3By similarity
Metal bindingi206 – 2061Calcium 1By similarity
Metal bindingi208 – 2081Calcium 1By similarity
Metal bindingi208 – 2081Calcium 3By similarity
Metal bindingi401 – 4011Zinc 2; catalyticBy similarity
Active sitei402 – 4021PROSITE-ProRule annotation
Metal bindingi405 – 4051Zinc 2; catalyticBy similarity
Metal bindingi411 – 4111Zinc 2; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
  2. leukocyte migration Source: InterPro
  3. ossification Source: InterPro
  4. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-9 (EC:3.4.24.35)
Short name:
MMP-9
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name:
GELB
Gene namesi
Name:MMP9
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Propeptidei20 – 10687Activation peptidePRO_0000028750Add
BLAST
Chaini107 – 712606Matrix metalloproteinase-9PRO_0000028751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
Disulfide bondi521 ↔ 709PROSITE-ProRule annotation

Post-translational modificationi

N- and O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP52176.
PRIDEiP52176.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP52176.
SMRiP52176. Positions 29-444, 518-712.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 27349Fibronectin type-II 1PROSITE-ProRule annotationAdd
BLAST
Domaini283 – 33149Fibronectin type-II 2PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 39049Fibronectin type-II 3PROSITE-ProRule annotationAdd
BLAST
Repeati523 – 56846Hemopexin 1Add
BLAST
Repeati569 – 61345Hemopexin 2Add
BLAST
Repeati615 – 66248Hemopexin 3Add
BLAST
Repeati663 – 70947Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi97 – 1048Cysteine switchBy similarity

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG328372.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP52176.
KOiK01403.

Family and domain databases

Gene3Di2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR000562. 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]
PANTHERiPTHR10201:SF30. PTHR10201:SF30. 1 hit.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52176-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPLQPLVLA LLVLACCSAV PRRRQPTVVV FPGEPRTNLT NRQLAEEYLY
60 70 80 90 100
RYGYTPGAEL SEDGQSLQRA LLRFQRRLSL PETGELDSTT LNAMRAPRCG
110 120 130 140 150
VPDVGRFQTF EGELKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA
160 170 180 190 200
VTPLTFTRVY GPEADIVIQF GVREHGDGYP FDGKNGLLAH AFPPGKGIQG
210 220 230 240 250
DAHFDDEELW SLGKGVVIPT YFGNAKGAAC HFPFTFEGRS YSACTTDGRS
260 270 280 290 300
DDMLWCSTTA DYDADRQFGF CPSERLYTQD GNADGKPCVF PFTFQGRTYS
310 320 330 340 350
ACTSDGRSDG YRWCATTANY DQDKLYGFCP TRVDATVTGG NAAGELCVFP
360 370 380 390 400
FTFLGKEYSA CTREGRNDGH LWCATTSNFD KDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HTSVPEALMY PMYRFTEEHP LHRDDVQGIQ HLYGPRPEPE
460 470 480 490 500
PRPPTTTTTT TTEPQPTAPP TVCVTGPPTA RPSEGPTTGP TGPPAAGPTG
510 520 530 540 550
PPTAGPSAAP TESPDPAEDV CNVDIFDAIA EIRNRLHFFK AGKYWRLSEG
560 570 580 590 600
GGRRVQGPFL VKSKWPALPR KLDSAFEDPL TKKIFFFSGR QVWVYTGASL
610 620 630 640 650
LGPRRLDKLG LGPEVAQVTG ALPRPEGKVL LFSGQSFWRF DVKTQKVDPQ
660 670 680 690 700
SVTPVDQMFP GVPISTHDIF QYQEKAYFCQ DHFYWRVSSQ NEVNQVDYVG
710
YVTFDLLKCP ED
Length:712
Mass (Da):79,088
Last modified:October 1, 1996 - v1
Checksum:iE7FDA28372AEE0CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78324 mRNA. Translation: CAA55127.1.
BC142430 mRNA. Translation: AAI42431.1.
PIRiI46031.
RefSeqiNP_777169.1. NM_174744.2.
UniGeneiBt.4714.

Genome annotation databases

GeneIDi282871.
KEGGibta:282871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78324 mRNA. Translation: CAA55127.1 .
BC142430 mRNA. Translation: AAI42431.1 .
PIRi I46031.
RefSeqi NP_777169.1. NM_174744.2.
UniGenei Bt.4714.

3D structure databases

ProteinModelPortali P52176.
SMRi P52176. Positions 29-444, 518-712.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL5846.

Protein family/group databases

MEROPSi M10.004.

Proteomic databases

PaxDbi P52176.
PRIDEi P52176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 282871.
KEGGi bta:282871.

Organism-specific databases

CTDi 4318.

Phylogenomic databases

eggNOGi NOG328372.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.
InParanoidi P52176.
KOi K01403.

Miscellaneous databases

NextBioi 20806399.

Family and domain databases

Gene3Di 2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProi IPR000562. 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 ]
PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
Pfami PF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view ]
PRINTSi PR00138. MATRIXIN.
SMARTi SM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEi PS00546. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMMP9_BOVIN
AccessioniPrimary (citable) accession number: P52176
Secondary accession number(s): A5PKB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3