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P41246

- MMP9_RABIT

UniProt

P41246 - MMP9_RABIT

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Protein
Matrix metalloproteinase-9
Gene
MMP9
Organism
Oryctolagus cuniculus (Rabbit)
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 bindingi99 – 991Zinc 2; in inhibited form By similarity
Metal bindingi131 – 1311Calcium 1 By similarity
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygen By similarity
Metal bindingi175 – 1751Zinc 1; structural By similarity
Metal bindingi177 – 1771Zinc 1; structural By similarity
Metal bindingi182 – 1821Calcium 3 By similarity
Metal bindingi183 – 1831Calcium 3; via carbonyl oxygen By similarity
Metal bindingi185 – 1851Calcium 3; via carbonyl oxygen By similarity
Metal bindingi187 – 1871Calcium 3; via carbonyl oxygen By similarity
Metal bindingi190 – 1901Zinc 1; structural By similarity
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygen By similarity
Metal bindingi199 – 1991Calcium 2; via carbonyl oxygen By similarity
Metal bindingi201 – 2011Calcium 2 By similarity
Metal bindingi203 – 2031Zinc 1; structural By similarity
Metal bindingi205 – 2051Calcium 3 By similarity
Metal bindingi206 – 2061Calcium 1 By similarity
Metal bindingi208 – 2081Calcium 1 By similarity
Metal bindingi208 – 2081Calcium 3 By similarity
Metal bindingi401 – 4011Zinc 2; catalytic By similarity
Active sitei402 – 4021 By similarity
Metal bindingi405 – 4051Zinc 2; catalytic By similarity
Metal bindingi411 – 4111Zinc 2; catalytic By 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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. 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 – 10687Activation peptide By similarity
PRO_0000028760Add
BLAST
Chaini107 – 707601Matrix metalloproteinase-9
PRO_0000028761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi230 ↔ 256 By similarity
Disulfide bondi244 ↔ 271 By similarity
Disulfide bondi288 ↔ 314 By similarity
Disulfide bondi302 ↔ 329 By similarity
Disulfide bondi347 ↔ 373 By similarity
Disulfide bondi361 ↔ 388 By similarity
Disulfide bondi516 ↔ 704 By similarity

Post-translational modificationi

N- and O-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Osteoclasts.

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

STRINGi9986.ENSOCUP00000025066.

Structurei

3D structure databases

ProteinModelPortaliP41246.
SMRiP41246. Positions 29-444, 513-707.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 27349Fibronectin type-II 1
Add
BLAST
Domaini283 – 33149Fibronectin type-II 2
Add
BLAST
Domaini342 – 39049Fibronectin type-II 3
Add
BLAST
Repeati518 – 56346Hemopexin 1
Add
BLAST
Repeati564 – 60845Hemopexin 2
Add
BLAST
Repeati610 – 65748Hemopexin 3
Add
BLAST
Repeati658 – 70447Hemopexin 4
Add
BLAST

Motif

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

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.
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. 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.
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.

P41246-1 [UniParc]FASTAAdd to Basket

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MSPRQPLVLA LLVLGCCSAA PRRRQPTLVV FPGELRTRLT DRQLAEEYLF    50
RYGYTRVASM HGDSQSLRLP LLLLQKHLSL PETGELDNAT LEAMRAPRCG 100
VPDVGKFQTF EGDLKWHHHN ITYWIQNYSE DLPRDVIDDA FARAFALWSA 150
VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG 200
DAHFDDEELW SLGKGVVVPT YFGNADGAPC HFPFTFEGRS YTACTTDGRS 250
DGMAWCSTTA DYDTDRRFGF CPSERLYTQD GNADGKPCEF PFIFQGRTYS 300
ACTTDGRSDG HRWCATTASY DKDKLYGFCP TRADSTVVGG NSAGELCVFP 350
FVFLGKEYSS CTSEGRRDGR LWCATTSNFD SDKKWGFCPD KGYSLFLVAA 400
HEFGHALGLD HSSVPERLMY PMYRYLEGSP LHEDDVRGIQ HLYGPNPNPQ 450
PPATTTPEPQ PTAPPTACPT WPATVRPSEH PTTSPTGAPS AGPTGPPTAS 500
PSAAPTASLD PAEDVCNVNV FDAIAEIGNK LHVFKDGRYW RFSEGSGRRP 550
QGPFLIADTW PALPAKLDSA FEEPLTKKLF FFSGRQVWVY TGASVLGPRR 600
LDKLGLGPEV PHVTGALPRA GGKVLLFGAQ RFWRFDVKTQ TVDSRSGAPV 650
DQMFPGVPLN THDVFQYREK AYFCQDRFFW RVSTRNEVNL VDQVGYVSFD 700
ILHCPED 707
Length:707
Mass (Da):78,308
Last modified:February 1, 1995 - v1
Checksum:i053BCE8DC4D4758F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761K → P in AAA64358. 1 Publication
Sequence conflicti100 – 1023GVP → ASR in AAA64358. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26514 mRNA. Translation: BAA05520.1.
L36050 Genomic DNA. Translation: AAA64358.1.
PIRiA53796.
RefSeqiNP_001075672.1. NM_001082203.1.
UniGeneiOcu.1773.

Genome annotation databases

GeneIDi100008993.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26514 mRNA. Translation: BAA05520.1 .
L36050 Genomic DNA. Translation: AAA64358.1 .
PIRi A53796.
RefSeqi NP_001075672.1. NM_001082203.1.
UniGenei Ocu.1773.

3D structure databases

ProteinModelPortali P41246.
SMRi P41246. Positions 29-444, 513-707.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000025066.

Protein family/group databases

MEROPSi M10.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008993.

Organism-specific databases

CTDi 4318.

Phylogenomic databases

eggNOGi NOG328372.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.

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.
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. 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.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification of matrix metalloproteinase 9 in rabbit osteoclasts."
    Tezuka K.I., Nemoto K., Tezuka Y., Sato T., Ikeda Y., Kobori M., Kawashima H., Eguchi H., Hakeda Y., Kumegawa M.
    J. Biol. Chem. 269:15006-15009(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Japanese white.
    Tissue: Bone.
  2. "The rabbit gene for 92-kDa matrix metalloproteinase. Role of AP1 and AP2 in cell type-specific transcription."
    Fini M.E., Bartlett J.D., Matsubara M., Rinehart W.B., Mody M.K., Girard M.T., Rainville M.
    J. Biol. Chem. 269:28620-28628(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
    Strain: New Zealand white.
    Tissue: Liver.

Entry informationi

Entry nameiMMP9_RABIT
AccessioniPrimary (citable) accession number: P41246
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 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

Similar proteinsi