Matrix metalloproteinase-9 precursor - Oryctolagus cuniculus (Rabbit)

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Reviewed, UniProtKB/Swiss-Prot P41246 (MMP9_RABIT)

Last modified September 1, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-9
      Short name=MMP-9
    EC=3.4.24.35
Alternative name(s):
    92 kDa type IV collagenase
    92 kDa gelatinase
    Gelatinase B
      Short name=GELB

Gene names

Name:

MMP9

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	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 activity	Cleavage of gelatin types I and V and collagen types IV and V.
Cofactor	Binds 2 zinc ions per subunit By similarity. Binds 3 calcium ions per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Tissue specificity	Osteoclasts.
Domain	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.
Post-translational modification	N- and O-glycosylated By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 3 fibronectin type-II domains. Contains 4 hemopexin-like domains.

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Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

By similarity

Propeptide

20 – 106

Activation peptide By similarity

PRO_0000028760

Chain

107 – 707

601

Matrix metalloproteinase-9

PRO_0000028761

Regions

Domain

225 – 273

Fibronectin type-II 1

Domain

283 – 331

Fibronectin type-II 2

Domain

342 – 390

Fibronectin type-II 3

Domain

521 – 565

Hemopexin-like 1

Domain

567 – 608

Hemopexin-like 2

Domain

613 – 659

Hemopexin-like 3

Domain

661 – 704

Hemopexin-like 4

Motif

97 – 104

Cysteine switch By similarity

Sites

Active site

402

By similarity

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

131

Calcium 1 By similarity

Metal binding

165

Calcium 2; via carbonyl oxygen By similarity

Metal binding

175

Zinc 1; structural By similarity

Metal binding

177

Zinc 1; structural By similarity

Metal binding

182

Calcium 3 By similarity

Metal binding

183

Calcium 3; via carbonyl oxygen By similarity

Metal binding

185

Calcium 3; via carbonyl oxygen By similarity

Metal binding

187

Calcium 3; via carbonyl oxygen By similarity

Metal binding

190

Zinc 1; structural By similarity

Metal binding

197

Calcium 2; via carbonyl oxygen By similarity

Metal binding

199

Calcium 2; via carbonyl oxygen By similarity

Metal binding

201

Calcium 2 By similarity

Metal binding

203

Zinc 1; structural By similarity

Metal binding

205

Calcium 3 By similarity

Metal binding

206

Calcium 1 By similarity

Metal binding

208

Calcium 1 By similarity

Metal binding

208

Calcium 3 By similarity

Metal binding

401

Zinc 2; catalytic By similarity

Metal binding

405

Zinc 2; catalytic By similarity

Metal binding

411

Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

120

N-linked (GlcNAc...) Potential

Glycosylation

127

N-linked (GlcNAc...) Potential

Disulfide bond

230 ↔ 256

By similarity

Disulfide bond

244 ↔ 271

By similarity

Disulfide bond

288 ↔ 314

By similarity

Disulfide bond

302 ↔ 329

By similarity

Disulfide bond

347 ↔ 373

By similarity

Disulfide bond

361 ↔ 388

By similarity

Disulfide bond

516 ↔ 704

By similarity

Experimental info

Sequence conflict

K → P in AAA64358. Ref.2

Sequence conflict

100 – 102

GVP → ASR in AAA64358. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P41246-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 053BCE8DC4D4758F
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FASTA

707

78,308

        10         20         30         40         50         60 
MSPRQPLVLA LLVLGCCSAA PRRRQPTLVV FPGELRTRLT DRQLAEEYLF RYGYTRVASM 

        70         80         90        100        110        120 
HGDSQSLRLP LLLLQKHLSL PETGELDNAT LEAMRAPRCG VPDVGKFQTF EGDLKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRDVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGPGIQG DAHFDDEELW SLGKGVVVPT YFGNADGAPC HFPFTFEGRS 

       250        260        270        280        290        300 
YTACTTDGRS DGMAWCSTTA DYDTDRRFGF CPSERLYTQD GNADGKPCEF PFIFQGRTYS 

       310        320        330        340        350        360 
ACTTDGRSDG HRWCATTASY DKDKLYGFCP TRADSTVVGG NSAGELCVFP FVFLGKEYSS 

       370        380        390        400        410        420 
CTSEGRRDGR LWCATTSNFD SDKKWGFCPD KGYSLFLVAA HEFGHALGLD HSSVPERLMY 

       430        440        450        460        470        480 
PMYRYLEGSP LHEDDVRGIQ HLYGPNPNPQ PPATTTPEPQ PTAPPTACPT WPATVRPSEH 

       490        500        510        520        530        540 
PTTSPTGAPS AGPTGPPTAS PSAAPTASLD PAEDVCNVNV FDAIAEIGNK LHVFKDGRYW 

       550        560        570        580        590        600 
RFSEGSGRRP QGPFLIADTW PALPAKLDSA FEEPLTKKLF FFSGRQVWVY TGASVLGPRR 

       610        620        630        640        650        660 
LDKLGLGPEV PHVTGALPRA GGKVLLFGAQ RFWRFDVKTQ TVDSRSGAPV DQMFPGVPLN 

       670        680        690        700 
THDVFQYREK AYFCQDRFFW RVSTRNEVNL VDQVGYVSFD ILHCPED

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References

[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: 8195136] [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: 7961810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171. Strain: New Zealand white. Tissue: Liver.

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Cross-references

Sequence databases
	D26514 mRNA. Translation: BAA05520.1. L36050 Genomic DNA. Translation: AAA64358.1.
PIR	A53796.
RefSeq	NP_001075672.1.
UniGene	Ocu.1773
3D structure databases
HSSP	HSSP built from PDB template 1GKC based on UniProtKB P14780.
SMR	P41246. Positions 29-444, 513-707.
ModBase	Search...
Protein-protein interaction databases
STRING	P41246.
Protein family/group databases
MEROPS	M10.004.
Genome annotation databases
GeneID	100008993.
Phylogenomic databases
HOVERGEN	P41246.
Enzyme and pathway databases
BRENDA	3.4.24.35. 255.
Family and domain databases
InterPro	IPR000562. FN_type2_col_bd. IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. IPR006970. PT. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00040. fn2. 3 hits. PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. PF04886. PT. 1 hit. [Graphical view]
PRINTS	PR00013. FNTYPEII. PR00138. MATRIXIN.
ProDom	PD000995. FN_Type_II. 2 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00059. FN2. 3 hits. SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00023. FN2_1. 3 hits. PS51092. FN2_2. 3 hits. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

MMP9_RABIT

Accession

Primary (citable) accession number: P41246

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	September 1, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents