Matrix metalloproteinase-9 precursor - Rattus norvegicus (Rat)

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P50282 (MMP9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Matrix metalloproteinase-9
Short name=MMP-9
EC=3.4.24.35

Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name=GELB

Gene names

Name:

Mmp9

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	708 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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.
Subunit structure	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.
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.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anatomical structure regression Inferred from expression pattern PubMed 19906188. Source: RGD cell growth Inferred from expression pattern PubMed 16563274. Source: RGD cellular response to cell-matrix adhesion Inferred from mutant phenotype PubMed 12963432. Source: RGD cellular response to interleukin-1 Inferred from expression pattern PubMed 16046515 PubMed 20145375. Source: RGD cellular response to iron(III) ion Inferred from expression pattern PubMed 21683124. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern PubMed 21683124. Source: RGD cellular response to low-density lipoprotein particle stimulus Inferred from expression pattern PubMed 19554388. Source: RGD cellular response to tumor necrosis factor Inferred from expression pattern PubMed 22410640. Source: RGD collagen catabolic process Inferred from direct assay PubMed 22410640. Source: RGD ossification Inferred from expression pattern PubMed 15883642. Source: RGD positive regulation of angiogenesis Inferred from mutant phenotype PubMed 19948826. Source: RGD positive regulation of synaptic plasticity Inferred from mutant phenotype PubMed 17493927. Source: RGD protein oligomerization Inferred from direct assay PubMed 9732233. Source: RGD proteolysis Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from direct assay PubMed 16846501. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 19889233. Source: RGD response to ethanol Inferred from expression pattern PubMed 17603938 PubMed 20405265. Source: RGD response to heat Inferred from expression pattern PubMed 17156757. Source: RGD response to hyperoxia Inferred from expression pattern PubMed 19099751. Source: RGD response to hypoxia Inferred from expression pattern PubMed 17289933. Source: RGD response to mechanical stimulus Inferred from expression pattern PubMed 17158349. Source: RGD response to nicotine Inferred from expression pattern PubMed 19879865. Source: RGD response to oxidative stress Inferred from direct assay PubMed 15642321. Source: RGD response to radiation Inferred from expression pattern PubMed 17337891 PubMed 20159792. Source: RGD response to retinoic acid Inferred from expression pattern PubMed 19099751. Source: RGD response to vitamin A Inferred from expression pattern PubMed 17164434. Source: RGD tissue remodeling Inferred from direct assay PubMed 16740171. Source: RGD transformation of host cell by virus Inferred from direct assay PubMed 20000122. Source: RGD
Cellular_component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from direct assay PubMed 16935996. Source: RGD proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB protein complex binding Inferred from direct assay PubMed 16935996. Source: RGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

By similarity

Propeptide

20 – 107

Activation peptide By similarity

PRO_0000028762

Chain

108 – 708

601

Matrix metalloproteinase-9

PRO_0000028763

Regions

Domain

226 – 274

Fibronectin type-II 1

Domain

284 – 332

Fibronectin type-II 2

Domain

343 – 391

Fibronectin type-II 3

Domain

524 – 568

Hemopexin-like 1

Domain

570 – 611

Hemopexin-like 2

Domain

616 – 662

Hemopexin-like 3

Domain

667 – 707

Hemopexin-like 4

Motif

98 – 105

Cysteine switch By similarity

Sites

Active site

403

By similarity

Metal binding

100

Zinc 2; in inhibited form By similarity

Metal binding

132

Calcium 1 By similarity

Metal binding

166

Calcium 2; via carbonyl oxygen By similarity

Metal binding

176

Zinc 1; structural By similarity

Metal binding

178

Zinc 1; structural By similarity

Metal binding

183

Calcium 3 By similarity

Metal binding

184

Calcium 3; via carbonyl oxygen By similarity

Metal binding

186

Calcium 3; via carbonyl oxygen By similarity

Metal binding

188

Calcium 3; via carbonyl oxygen By similarity

Metal binding

191

Zinc 1; structural By similarity

Metal binding

198

Calcium 2; via carbonyl oxygen By similarity

Metal binding

200

Calcium 2; via carbonyl oxygen By similarity

Metal binding

202

Calcium 2 By similarity

Metal binding

204

Zinc 1; structural By similarity

Metal binding

206

Calcium 3 By similarity

Metal binding

207

Calcium 1 By similarity

Metal binding

209

Calcium 1 By similarity

Metal binding

209

Calcium 3 By similarity

Metal binding

402

Zinc 2; catalytic By similarity

Metal binding

406

Zinc 2; catalytic By similarity

Metal binding

412

Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

121

N-linked (GlcNAc...) Potential

Disulfide bond

231 ↔ 257

By similarity

Disulfide bond

245 ↔ 272

By similarity

Disulfide bond

289 ↔ 315

By similarity

Disulfide bond

303 ↔ 330

By similarity

Disulfide bond

348 ↔ 374

By similarity

Disulfide bond

362 ↔ 389

By similarity

Disulfide bond

519 ↔ 707

By similarity

Experimental info

Sequence conflict

S → N in AAA90911. Ref.1

Sequence conflict

112

D → E in AAA90911. Ref.1

Sequence conflict

326 – 327

AD → LY in AAA90911. Ref.1

Sequence conflict

364

S → G in AAA90911. Ref.1

Sequence conflict

441

H → Q in AAA90911. Ref.1

Sequence conflict

472

S → P in AAA90911. Ref.1

Sequence conflict

515

D → V in AAA90911. Ref.1

Sequence conflict

551

N → S in AAA90911. Ref.1

Sequence conflict

566

F → L in AAA90911. Ref.1

Sequence conflict

568

S → A in AAA90911. Ref.1

Sequence conflict

579

P → S in AAA90911. Ref.1

Sequence conflict

586 – 589

LWAQ → SGRK in AAA90911. Ref.1

Sequence conflict

597

S → T in AAA90911. Ref.1

Sequence conflict

669

Q → H in AAA90911. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P50282 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D57DC0D1B93A778C
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FASTA

708

78,611

        10         20         30         40         50         60 
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL YRYGYTRAAQ 

        70         80         90        100        110        120 
MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC GVPDVGKFQT FDGDLKWHHH 

       130        140        150        160        170        180 
NITYWIQSYT EDLPRDVIDD SFARAFAVWS AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY 

       190        200        210        220        230        240 
PFDGKDGLLA HAFPPGPGIQ GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR 

       250        260        270        280        290        300 
SYLSCTTDGR NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY 

       310        320        330        340        350        360 
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF PFVFLGKQYS 

       370        380        390        400        410        420 
TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSVPEALM 

       430        440        450        460        470        480 
YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP DPRPPATTAA EPQPTAPPTM CSTAPPMAYP 

       490        500        510        520        530        540 
TGGPTVAPTG APSPGPTGPP TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG 

       550        560        570        580        590        600 
RYWKFSNHGG NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG 

       610        620        630        640        650        660 
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV TRLDNEFSGV 

       670        680        690        700 
PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV TYDLLQCP

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References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U24441 mRNA. Translation: AAA90911.1. U36476 mRNA. Translation: AAB01721.1.
IPI	IPI00196591.
PIR	JC4364. S62907.
RefSeq	NP_112317.1. NM_031055.1.
UniGene	Rn.10209.
3D structure databases
ProteinModelPortal	P50282.
SMR	P50282. Positions 29-445.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000023965.
Protein family/group databases
MEROPS	M10.004.
Proteomic databases
PaxDb	P50282.
PRIDE	P50282.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	81687.
KEGG	rno:81687.
Organism-specific databases
CTD	4318.
RGD	621320. Mmp9.
Phylogenomic databases
eggNOG	NOG328372.
HOGENOM	HOG000217926.
HOVERGEN	HBG052484.
InParanoid	P50282.
KO	K01403.
Gene expression databases
ArrayExpress	P50282.
Genevestigator	P50282.
GermOnline	ENSRNOG00000017539. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.101.10. 1 hit. 2.10.10.10. 3 hits. 2.110.10.10. 1 hit. 3.40.390.10. 2 hits.
InterPro	IPR000562. FN_type2_col-bd. IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR018486. Hemopexin_CS. IPR013806. Kringle-like. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. IPR006970. PT. [Graphical view]
Pfam	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]
PRINTS	PR00138. MATRIXIN.
SMART	SM00059. FN2. 3 hits. SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF57440. Kringle-like. 3 hits. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00023. FN2_1. 2 hits. PS51092. FN2_2. 3 hits. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P50282.
ChEMBL	CHEMBL3870.
NextBio	615324.

Entry information

Entry name

MMP9_RAT

Accession

Primary (citable) accession number: P50282

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents