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Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Zinc 2; in inhibited formBy similarity
Metal bindingi132 – 1321Calcium 1By similarity
Metal bindingi166 – 1661Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi176 – 1761Zinc 1; structuralBy similarity
Metal bindingi178 – 1781Zinc 1; structuralBy similarity
Metal bindingi183 – 1831Calcium 3By similarity
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi188 – 1881Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi191 – 1911Zinc 1; structuralBy similarity
Metal bindingi198 – 1981Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi200 – 2001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi202 – 2021Calcium 2By similarity
Metal bindingi204 – 2041Zinc 1; structuralBy similarity
Metal bindingi206 – 2061Calcium 3By similarity
Metal bindingi207 – 2071Calcium 1By similarity
Metal bindingi209 – 2091Calcium 1By similarity
Metal bindingi209 – 2091Calcium 3By similarity
Metal bindingi402 – 4021Zinc 2; catalyticBy similarity
Active sitei403 – 4031PROSITE-ProRule annotation
Metal bindingi406 – 4061Zinc 2; catalyticBy similarity
Metal bindingi412 – 4121Zinc 2; catalyticBy similarity

GO - Molecular functioni

  • fibronectin binding Source: RGD
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: RGD
  • peptidase activity Source: RGD
  • protein complex binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • cellular response to cell-matrix adhesion Source: RGD
  • cellular response to cytokine stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to iron(III) ion Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to low-density lipoprotein particle stimulus Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • collagen catabolic process Source: RGD
  • heart development Source: RGD
  • kidney development Source: RGD
  • leukocyte migration Source: InterPro
  • negative regulation of fibroblast proliferation Source: RGD
  • ossification Source: RGD
  • parturition Source: RGD
  • positive regulation of angiogenesis Source: RGD
  • positive regulation of leukocyte migration Source: RGD
  • positive regulation of synaptic plasticity Source: RGD
  • protein oligomerization Source: RGD
  • proteolysis Source: UniProtKB
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to heat Source: RGD
  • response to high light intensity Source: RGD
  • response to hyperoxia Source: RGD
  • response to hypoxia Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to nicotine Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to oxidative stress Source: RGD
  • response to radiation Source: RGD
  • response to retinoic acid Source: RGD
  • response to tumor necrosis factor Source: RGD
  • response to vitamin A Source: RGD
  • tissue remodeling Source: RGD
  • transformation of host cell by virus Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.35. 5301.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621320. Mmp9.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • protein complex Source: RGD
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 – 10788Activation peptideBy similarityPRO_0000028762Add
BLAST
Chaini108 – 708601Matrix metalloproteinase-9PRO_0000028763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi231 ↔ 257PROSITE-ProRule annotation
Disulfide bondi245 ↔ 272PROSITE-ProRule annotation
Disulfide bondi289 ↔ 315PROSITE-ProRule annotation
Disulfide bondi303 ↔ 330PROSITE-ProRule annotation
Disulfide bondi348 ↔ 374PROSITE-ProRule annotation
Disulfide bondi362 ↔ 389PROSITE-ProRule annotation
Disulfide bondi519 ↔ 707PROSITE-ProRule annotation

Post-translational modificationi

N- and O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP50282.
PRIDEiP50282.

Expressioni

Gene expression databases

GenevisibleiP50282. RN.

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

STRINGi10116.ENSRNOP00000023965.

Structurei

3D structure databases

ProteinModelPortaliP50282.
SMRiP50282. Positions 29-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini226 – 27449Fibronectin type-II 1PROSITE-ProRule annotationAdd
BLAST
Domaini284 – 33249Fibronectin type-II 2PROSITE-ProRule annotationAdd
BLAST
Domaini343 – 39149Fibronectin type-II 3PROSITE-ProRule annotationAdd
BLAST
Repeati521 – 56646Hemopexin 1Add
BLAST
Repeati567 – 61145Hemopexin 2Add
BLAST
Repeati613 – 66048Hemopexin 3Add
BLAST
Repeati661 – 70747Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi98 – 1058Cysteine 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.
InParanoidiP50282.
KOiK01403.
PhylomeDBiP50282.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.10.10.10. 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.
IPR018486. Hemopexin_CS.
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. 1 hit.
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. 2 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
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.

P50282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL
60 70 80 90 100
YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC
110 120 130 140 150
GVPDVGKFQT FDGDLKWHHH NITYWIQSYT EDLPRDVIDD SFARAFAVWS
160 170 180 190 200
AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ
210 220 230 240 250
GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR SYLSCTTDGR
260 270 280 290 300
NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY
310 320 330 340 350
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF
360 370 380 390 400
PFVFLGKQYS TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA
410 420 430 440 450
AHEFGHALGL DHSSVPEALM YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP
460 470 480 490 500
DPRPPATTAA EPQPTAPPTM CSTAPPMAYP TGGPTVAPTG APSPGPTGPP
510 520 530 540 550
TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG RYWKFSNHGG
560 570 580 590 600
NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG
610 620 630 640 650
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV
660 670 680 690 700
TRLDNEFSGV PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV

TYDLLQCP
Length:708
Mass (Da):78,611
Last modified:October 1, 1996 - v1
Checksum:iD57DC0D1B93A778C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → N in AAA90911 (PubMed:7590350).Curated
Sequence conflicti112 – 1121D → E in AAA90911 (PubMed:7590350).Curated
Sequence conflicti326 – 3272AD → LY in AAA90911 (PubMed:7590350).Curated
Sequence conflicti364 – 3641S → G in AAA90911 (PubMed:7590350).Curated
Sequence conflicti441 – 4411H → Q in AAA90911 (PubMed:7590350).Curated
Sequence conflicti472 – 4721S → P in AAA90911 (PubMed:7590350).Curated
Sequence conflicti515 – 5151D → V in AAA90911 (PubMed:7590350).Curated
Sequence conflicti551 – 5511N → S in AAA90911 (PubMed:7590350).Curated
Sequence conflicti566 – 5661F → L in AAA90911 (PubMed:7590350).Curated
Sequence conflicti568 – 5681S → A in AAA90911 (PubMed:7590350).Curated
Sequence conflicti579 – 5791P → S in AAA90911 (PubMed:7590350).Curated
Sequence conflicti586 – 5894LWAQ → SGRK in AAA90911 (PubMed:7590350).Curated
Sequence conflicti597 – 5971S → T in AAA90911 (PubMed:7590350).Curated
Sequence conflicti669 – 6691Q → H in AAA90911 (PubMed:7590350).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24441 mRNA. Translation: AAA90911.1.
U36476 mRNA. Translation: AAB01721.1.
PIRiJC4364.
S62907.
RefSeqiNP_112317.1. NM_031055.1.
UniGeneiRn.10209.

Genome annotation databases

GeneIDi81687.
KEGGirno:81687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24441 mRNA. Translation: AAA90911.1.
U36476 mRNA. Translation: AAB01721.1.
PIRiJC4364.
S62907.
RefSeqiNP_112317.1. NM_031055.1.
UniGeneiRn.10209.

3D structure databases

ProteinModelPortaliP50282.
SMRiP50282. Positions 29-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023965.

Chemistry

BindingDBiP50282.
ChEMBLiCHEMBL3870.

Protein family/group databases

MEROPSiM10.004.

Proteomic databases

PaxDbiP50282.
PRIDEiP50282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81687.
KEGGirno:81687.

Organism-specific databases

CTDi4318.
RGDi621320. Mmp9.

Phylogenomic databases

eggNOGiNOG328372.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP50282.
KOiK01403.
PhylomeDBiP50282.

Enzyme and pathway databases

BRENDAi3.4.24.35. 5301.

Miscellaneous databases

NextBioi615324.
PROiP50282.

Gene expression databases

GenevisibleiP50282. RN.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.10.10.10. 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.
IPR018486. Hemopexin_CS.
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. 1 hit.
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. 2 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.

Entry informationi

Entry nameiMMP9_RAT
AccessioniPrimary (citable) accession number: P50282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 137 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

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 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.