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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).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
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-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 peptideBy similarityPRO_0000028760Add
BLAST
Chaini107 – 707601Matrix metalloproteinase-9PRO_0000028761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-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 bondi516 ↔ 704PROSITE-ProRule annotation

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. Exists also as heterodimer with a 25 kDa protein. Interacts with ECM1.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000025066.

Structurei

3D structure databases

ProteinModelPortaliP41246.
SMRiP41246. Positions 29-444, 513-707.
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
Repeati518 – 56346Hemopexin 1Add
BLAST
Repeati564 – 60845Hemopexin 2Add
BLAST
Repeati610 – 65748Hemopexin 3Add
BLAST
Repeati658 – 70447Hemopexin 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.
InParanoidiP41246.

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

« Hide

        10         20         30         40         50
MSPRQPLVLA LLVLGCCSAA PRRRQPTLVV FPGELRTRLT DRQLAEEYLF
60 70 80 90 100
RYGYTRVASM HGDSQSLRLP LLLLQKHLSL PETGELDNAT LEAMRAPRCG
110 120 130 140 150
VPDVGKFQTF EGDLKWHHHN ITYWIQNYSE DLPRDVIDDA FARAFALWSA
160 170 180 190 200
VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG
210 220 230 240 250
DAHFDDEELW SLGKGVVVPT YFGNADGAPC HFPFTFEGRS YTACTTDGRS
260 270 280 290 300
DGMAWCSTTA DYDTDRRFGF CPSERLYTQD GNADGKPCEF PFIFQGRTYS
310 320 330 340 350
ACTTDGRSDG HRWCATTASY DKDKLYGFCP TRADSTVVGG NSAGELCVFP
360 370 380 390 400
FVFLGKEYSS CTSEGRRDGR LWCATTSNFD SDKKWGFCPD KGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPERLMY PMYRYLEGSP LHEDDVRGIQ HLYGPNPNPQ
460 470 480 490 500
PPATTTPEPQ PTAPPTACPT WPATVRPSEH PTTSPTGAPS AGPTGPPTAS
510 520 530 540 550
PSAAPTASLD PAEDVCNVNV FDAIAEIGNK LHVFKDGRYW RFSEGSGRRP
560 570 580 590 600
QGPFLIADTW PALPAKLDSA FEEPLTKKLF FFSGRQVWVY TGASVLGPRR
610 620 630 640 650
LDKLGLGPEV PHVTGALPRA GGKVLLFGAQ RFWRFDVKTQ TVDSRSGAPV
660 670 680 690 700
DQMFPGVPLN THDVFQYREK AYFCQDRFFW RVSTRNEVNL VDQVGYVSFD

ILHCPED
Length:707
Mass (Da):78,308
Last modified:February 1, 1995 - v1
Checksum:i053BCE8DC4D4758F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761K → P in AAA64358. (PubMed:7961810)Curated
Sequence conflicti100 – 1023GVP → ASR in AAA64358. (PubMed:7961810)Curated

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.
InParanoidi P41246.

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: October 29, 2014
This is version 120 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