Matrix metalloproteinase-9 precursor

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Reviewed, UniProtKB/Swiss-Prot P52176 (MMP9_BOVIN)

Last modified September 1, 2009. Version 81. 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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	712 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.
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

PRO_0000028750

Chain

107 – 712

606

Matrix metalloproteinase-9

PRO_0000028751

Regions

Domain

225 – 273

Fibronectin type-II 1

Domain

283 – 331

Fibronectin type-II 2

Domain

342 – 390

Fibronectin type-II 3

Domain

526 – 570

Hemopexin-like 1

Domain

572 – 613

Hemopexin-like 2

Domain

618 – 664

Hemopexin-like 3

Domain

666 – 709

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

521 ↔ 709

By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P52176-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E7FDA28372AEE0CE
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FASTA

712

79,088

        10         20         30         40         50         60 
MSPLQPLVLA LLVLACCSAV PRRRQPTVVV FPGEPRTNLT NRQLAEEYLY RYGYTPGAEL 

        70         80         90        100        110        120 
SEDGQSLQRA LLRFQRRLSL PETGELDSTT LNAMRAPRCG VPDVGRFQTF EGELKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY GPEADIVIQF GVREHGDGYP 

       190        200        210        220        230        240 
FDGKNGLLAH AFPPGKGIQG DAHFDDEELW SLGKGVVIPT YFGNAKGAAC HFPFTFEGRS 

       250        260        270        280        290        300 
YSACTTDGRS DDMLWCSTTA DYDADRQFGF CPSERLYTQD GNADGKPCVF PFTFQGRTYS 

       310        320        330        340        350        360 
ACTSDGRSDG YRWCATTANY DQDKLYGFCP TRVDATVTGG NAAGELCVFP FTFLGKEYSA 

       370        380        390        400        410        420 
CTREGRNDGH LWCATTSNFD KDKKWGFCPD QGYSLFLVAA HEFGHALGLD HTSVPEALMY 

       430        440        450        460        470        480 
PMYRFTEEHP LHRDDVQGIQ HLYGPRPEPE PRPPTTTTTT TTEPQPTAPP TVCVTGPPTA 

       490        500        510        520        530        540 
RPSEGPTTGP TGPPAAGPTG PPTAGPSAAP TESPDPAEDV CNVDIFDAIA EIRNRLHFFK 

       550        560        570        580        590        600 
AGKYWRLSEG GGRRVQGPFL VKSKWPALPR KLDSAFEDPL TKKIFFFSGR QVWVYTGASL 

       610        620        630        640        650        660 
LGPRRLDKLG LGPEVAQVTG ALPRPEGKVL LFSGQSFWRF DVKTQKVDPQ SVTPVDQMFP 

       670        680        690        700        710 
GVPISTHDIF QYQEKAYFCQ DHFYWRVSSQ NEVNQVDYVG YVTFDLLKCP ED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes." Baylis H.A., Megson A., Hall R. Mol. Biochem. Parasitol. 69:211-222(1995) [PubMed: 7770085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukocyte.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.

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Cross-references

Sequence databases
	X78324 mRNA. Translation: CAA55127.1. BC142430 mRNA. Translation: AAI42431.1.
IPI	IPI00686326.
PIR	I46031.
RefSeq	NP_777169.1.
UniGene	Bt.4714
3D structure databases
HSSP	HSSP built from PDB template 1GKD based on UniProtKB P14780.
SMR	P52176. Positions 29-444, 518-712.
ModBase	Search...
Protein-protein interaction databases
STRING	P52176.
Protein family/group databases
MEROPS	M10.004.
Genome annotation databases
Ensembl	ENSBTAT00000027556; ENSBTAP00000027556; ENSBTAG00000020676; Bos taurus. [Genome view]
GeneID	282871.
KEGG	bta:282871.
Organism-specific databases
CTD	282871.
Phylogenomic databases
HOVERGEN	P52176.
Enzyme and pathway databases
BRENDA	3.4.24.35. 251.
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. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

MMP9_BOVIN

Accession

Primary (citable) accession number: P52176
Secondary accession number(s): A5PKB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 1, 2009
This is version 81 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents