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Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99Zinc 2; in inhibited formBy similarity1
Metal bindingi131Calcium 1By similarity1
Metal bindingi165Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi175Zinc 1; structuralBy similarity1
Metal bindingi177Zinc 1; structuralBy similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi183Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi185Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi187Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi190Zinc 1; structuralBy similarity1
Metal bindingi197Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi201Calcium 2By similarity1
Metal bindingi203Zinc 1; structuralBy similarity1
Metal bindingi205Calcium 3By similarity1
Metal bindingi206Calcium 1By similarity1
Metal bindingi208Calcium 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi401Zinc 2; catalyticBy similarity1
Active sitei402PROSITE-ProRule annotation1
Metal bindingi405Zinc 2; catalyticBy similarity1
Metal bindingi411Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
PropeptideiPRO_000002875020 – 106Activation peptideAdd BLAST87
ChainiPRO_0000028751107 – 712Matrix metalloproteinase-9Add BLAST606

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Glycosylationi127N-linked (GlcNAc...)Sequence analysis1
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.
PeptideAtlasiP52176.
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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027556.

Structurei

3D structure databases

ProteinModelPortaliP52176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini342 – 390Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati523 – 568Hemopexin 1Add BLAST46
Repeati569 – 613Hemopexin 2Add BLAST45
Repeati615 – 662Hemopexin 3Add BLAST48
Repeati663 – 709Hemopexin 4Add BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi97 – 104Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP52176.
KOiK01403.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
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.
IPR033739. M10A_MMP.
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. 3 hits.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
X78324 mRNA. Translation: CAA55127.1.
BC142430 mRNA. Translation: AAI42431.1.
PIRiI46031.
RefSeqiNP_777169.1. NM_174744.2.
UniGeneiBt.4714.

3D structure databases

ProteinModelPortaliP52176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027556.

Chemistry databases

ChEMBLiCHEMBL5846.

Protein family/group databases

MEROPSiM10.004.

Proteomic databases

PaxDbiP52176.
PeptideAtlasiP52176.
PRIDEiP52176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282871.
KEGGibta:282871.

Organism-specific databases

CTDi4318.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP52176.
KOiK01403.

Miscellaneous databases

PROiP52176.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
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.
IPR033739. M10A_MMP.
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. 3 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 131 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.