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P50282

- MMP9_RAT

UniProt

P50282 - MMP9_RAT

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Protein
Matrix metalloproteinase-9
Gene
Mmp9
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

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 bindingi100 – 1001Zinc 2; in inhibited form By similarity
Metal bindingi132 – 1321Calcium 1 By similarity
Metal bindingi166 – 1661Calcium 2; via carbonyl oxygen By similarity
Metal bindingi176 – 1761Zinc 1; structural By similarity
Metal bindingi178 – 1781Zinc 1; structural By similarity
Metal bindingi183 – 1831Calcium 3 By similarity
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygen By similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygen By similarity
Metal bindingi188 – 1881Calcium 3; via carbonyl oxygen By similarity
Metal bindingi191 – 1911Zinc 1; structural By similarity
Metal bindingi198 – 1981Calcium 2; via carbonyl oxygen By similarity
Metal bindingi200 – 2001Calcium 2; via carbonyl oxygen By similarity
Metal bindingi202 – 2021Calcium 2 By similarity
Metal bindingi204 – 2041Zinc 1; structural By similarity
Metal bindingi206 – 2061Calcium 3 By similarity
Metal bindingi207 – 2071Calcium 1 By similarity
Metal bindingi209 – 2091Calcium 1 By similarity
Metal bindingi209 – 2091Calcium 3 By similarity
Metal bindingi402 – 4021Zinc 2; catalytic By similarity
Active sitei403 – 4031 By similarity
Metal bindingi406 – 4061Zinc 2; catalytic By similarity
Metal bindingi412 – 4121Zinc 2; catalytic By similarity

GO - Molecular functioni

  1. fibronectin binding Source: RGD
  2. metalloendopeptidase activity Source: UniProtKB
  3. metallopeptidase activity Source: RGD
  4. peptidase activity Source: RGD
  5. protein binding Source: RGD
  6. protein complex binding Source: RGD
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. anatomical structure regression Source: RGD
  2. cellular response to cell-matrix adhesion Source: RGD
  3. cellular response to cytokine stimulus Source: RGD
  4. cellular response to interleukin-1 Source: RGD
  5. cellular response to iron(III) ion Source: RGD
  6. cellular response to lipopolysaccharide Source: RGD
  7. cellular response to low-density lipoprotein particle stimulus Source: RGD
  8. cellular response to tumor necrosis factor Source: RGD
  9. collagen catabolic process Source: RGD
  10. kidney development Source: RGD
  11. leukocyte migration Source: InterPro
  12. negative regulation of fibroblast proliferation Source: RGD
  13. ossification Source: RGD
  14. parturition Source: RGD
  15. positive regulation of angiogenesis Source: RGD
  16. positive regulation of synaptic plasticity Source: RGD
  17. protein oligomerization Source: RGD
  18. proteolysis Source: UniProtKB
  19. response to drug Source: RGD
  20. response to estradiol Source: RGD
  21. response to ethanol Source: RGD
  22. response to heat Source: RGD
  23. response to high light intensity Source: RGD
  24. response to hyperoxia Source: RGD
  25. response to hypoxia Source: RGD
  26. response to lipopolysaccharide Source: RGD
  27. response to mechanical stimulus Source: RGD
  28. response to nicotine Source: RGD
  29. response to nutrient Source: RGD
  30. response to organic cyclic compound Source: RGD
  31. response to organic substance Source: RGD
  32. response to oxidative stress Source: RGD
  33. response to radiation Source: RGD
  34. response to retinoic acid Source: RGD
  35. response to tumor necrosis factor Source: RGD
  36. response to vitamin A Source: RGD
  37. tissue remodeling Source: RGD
  38. 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

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: Unplaced

Organism-specific databases

RGDi621320. Mmp9.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. protein complex Source: RGD
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarity
Add
BLAST
Propeptidei20 – 10788Activation peptide By similarity
PRO_0000028762Add
BLAST
Chaini108 – 708601Matrix metalloproteinase-9
PRO_0000028763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi121 – 1211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi231 ↔ 257 By similarity
Disulfide bondi245 ↔ 272 By similarity
Disulfide bondi289 ↔ 315 By similarity
Disulfide bondi303 ↔ 330 By similarity
Disulfide bondi348 ↔ 374 By similarity
Disulfide bondi362 ↔ 389 By similarity
Disulfide bondi519 ↔ 707 By similarity

Post-translational modificationi

N- and O-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP50282.
PRIDEiP50282.

Expressioni

Gene expression databases

GenevestigatoriP50282.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023965.

Structurei

3D structure databases

ProteinModelPortaliP50282.
SMRiP50282. Positions 29-445.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi98 – 1058Cysteine switch By 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.
Contains 4 hemopexin repeats.

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

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MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL    50
YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC 100
GVPDVGKFQT FDGDLKWHHH NITYWIQSYT EDLPRDVIDD SFARAFAVWS 150
AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ 200
GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR SYLSCTTDGR 250
NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY 300
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF 350
PFVFLGKQYS TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA 400
AHEFGHALGL DHSSVPEALM YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP 450
DPRPPATTAA EPQPTAPPTM CSTAPPMAYP TGGPTVAPTG APSPGPTGPP 500
TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG RYWKFSNHGG 550
NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG 600
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV 650
TRLDNEFSGV PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV 700
TYDLLQCP 708
Length:708
Mass (Da):78,611
Last modified:October 1, 1996 - v1
Checksum:iD57DC0D1B93A778C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → N in AAA90911. 1 Publication
Sequence conflicti112 – 1121D → E in AAA90911. 1 Publication
Sequence conflicti326 – 3272AD → LY in AAA90911. 1 Publication
Sequence conflicti364 – 3641S → G in AAA90911. 1 Publication
Sequence conflicti441 – 4411H → Q in AAA90911. 1 Publication
Sequence conflicti472 – 4721S → P in AAA90911. 1 Publication
Sequence conflicti515 – 5151D → V in AAA90911. 1 Publication
Sequence conflicti551 – 5511N → S in AAA90911. 1 Publication
Sequence conflicti566 – 5661F → L in AAA90911. 1 Publication
Sequence conflicti568 – 5681S → A in AAA90911. 1 Publication
Sequence conflicti579 – 5791P → S in AAA90911. 1 Publication
Sequence conflicti586 – 5894LWAQ → SGRK in AAA90911. 1 Publication
Sequence conflicti597 – 5971S → T in AAA90911. 1 Publication
Sequence conflicti669 – 6691Q → H in AAA90911. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U24441 mRNA. Translation: AAA90911.1 .
U36476 mRNA. Translation: AAB01721.1 .
PIRi JC4364.
S62907.
RefSeqi NP_112317.1. NM_031055.1.
UniGenei Rn.10209.

3D structure databases

ProteinModelPortali P50282.
SMRi P50282. Positions 29-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000023965.

Chemistry

BindingDBi P50282.
ChEMBLi CHEMBL3870.

Protein family/group databases

MEROPSi M10.004.

Proteomic databases

PaxDbi P50282.
PRIDEi P50282.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81687.
KEGGi rno:81687.

Organism-specific databases

CTDi 4318.
RGDi 621320. Mmp9.

Phylogenomic databases

eggNOGi NOG328372.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.
InParanoidi P50282.
KOi K01403.
PhylomeDBi P50282.

Miscellaneous databases

NextBioi 615324.
PROi P50282.

Gene expression databases

Genevestigatori P50282.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
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.
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 ]
PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
Pfami PF00040. fn2. 3 hits.
PF00045. Hemopexin. 1 hit.
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. 2 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 130 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

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