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P41245 (MMP9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Synonyms:Clg4b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length730 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Induction

Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Ref.8

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 10788Activation peptide By similarity
PRO_0000028758
Chain108 – 730623Matrix metalloproteinase-9
PRO_0000028759

Regions

Domain225 – 27349Fibronectin type-II 1
Domain283 – 33149Fibronectin type-II 2
Domain342 – 39049Fibronectin type-II 3
Domain539 – 58345Hemopexin-like 1
Domain585 – 62642Hemopexin-like 2
Domain631 – 67747Hemopexin-like 3
Domain679 – 72345Hemopexin-like 4
Motif98 – 1058Cysteine switch By similarity

Sites

Active site4021 By similarity
Metal binding1001Zinc 2; in inhibited form By similarity
Metal binding1311Calcium 1 By similarity
Metal binding1651Calcium 2; via carbonyl oxygen By similarity
Metal binding1751Zinc 1; structural By similarity
Metal binding1771Zinc 1; structural By similarity
Metal binding1821Calcium 3 By similarity
Metal binding1831Calcium 3; via carbonyl oxygen By similarity
Metal binding1851Calcium 3; via carbonyl oxygen By similarity
Metal binding1871Calcium 3; via carbonyl oxygen By similarity
Metal binding1901Zinc 1; structural By similarity
Metal binding1971Calcium 2; via carbonyl oxygen By similarity
Metal binding1991Calcium 2; via carbonyl oxygen By similarity
Metal binding2011Calcium 2 By similarity
Metal binding2031Zinc 1; structural By similarity
Metal binding2051Calcium 3 By similarity
Metal binding2061Calcium 1 By similarity
Metal binding2081Calcium 1 By similarity
Metal binding2081Calcium 3 By similarity
Metal binding4011Zinc 2; catalytic By similarity
Metal binding4051Zinc 2; catalytic By similarity
Metal binding4111Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Disulfide bond230 ↔ 256 By similarity
Disulfide bond244 ↔ 271 By similarity
Disulfide bond288 ↔ 314 By similarity
Disulfide bond302 ↔ 329 By similarity
Disulfide bond347 ↔ 373 By similarity
Disulfide bond361 ↔ 388 By similarity
Disulfide bond534 ↔ 729 By similarity

Natural variations

Natural variant5141P → A. Ref.2
Natural variant6391L → P. Ref.2
Natural variant7111H → P. Ref.2

Experimental info

Sequence conflict201A → C in AAB28942. Ref.2
Sequence conflict25 – 262QP → HA in AAB28942. Ref.2
Sequence conflict4661P → T in BAB23442. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P41245 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E16F45C24D4D1024

FASTA73080,535
        10         20         30         40         50         60 
MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL YRYGYTRAAQ 

        70         80         90        100        110        120 
MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC GVPDVGRFQT FKGLKWDHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRDMIDDA FARAFAVWGE VAPLTFTRVY GPEADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGAGVQG DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS 

       250        260        270        280        290        300 
YSACTTDGRN DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS 

       310        320        330        340        350        360 
ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP FVFLGKQYSS 

       370        380        390        400        410        420 
CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 

       430        440        450        460        470        480 
PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD PRPPATTTTE PQPTAPPTMC PTIPPTAYPT 

       490        500        510        520        530        540 
VGPTVGPTGA PSPGPTSSPS PGPTGAPSPG PTAPPTAGSS EASTESLSPA DNPCNVDVFD 

       550        560        570        580        590        600 
AIAEIQGALH FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF 

       610        620        630        640        650        660 
SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRLG KALLFSKGRV WRFDLKSQKV 

       670        680        690        700        710        720 
DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV SFQNEVNKVD HEVNQVDDVG 

       730 
YVTYDLLQCP

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA."
Tanaka H., Hojo K., Yoshida H., Yoshioka T., Sugita K.
Biochem. Biophys. Res. Commun. 190:732-740(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and expression of the cDNA encoding mouse neutrophil gelatinase: demonstration of coordinate secondary granule protein gene expression during terminal neutrophil maturation."
Graubert T., Johnston J., Berliner N.
Blood 82:3192-3197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-514; PRO-639 AND PRO-711.
[3]"Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation."
Masure S., Nys G., Fiten P., van Damme J., Opdenakker G.
Eur. J. Biochem. 218:129-141(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: C57BL/6.
Tissue: Liver.
[4]"High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development."
Reponen P., Sahlberg C., Munaut C., Thesleff I., Tryggvason K.
J. Cell Biol. 124:1091-1102(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Olfactory epithelium.
[8]"The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+)mice."
Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.
EMBO Rep. 10:1355-1362(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D12712 mRNA. Translation: BAA02208.1.
S67830 mRNA. Translation: AAB28942.1.
X72794 Genomic DNA. Translation: CAA51314.1.
X72795 mRNA. Translation: CAA51315.1.
Z27231 mRNA. Translation: CAA81745.1.
AK004651 mRNA. Translation: BAB23442.1.
AK159292 mRNA. Translation: BAE34968.1.
AL591495 Genomic DNA. Translation: CAM26465.1.
BC046991 mRNA. Translation: AAH46991.1.
IPIIPI00319200.
PIRI52580.
JC1456.
RefSeqNP_038627.1. NM_013599.2.
UniGeneMm.4406.

3D structure databases

ProteinModelPortalP41245.
SMRP41245. Positions 29-730.
ModBaseSearch...

Protein family/group databases

MEROPSM10.004.

PTM databases

PhosphoSiteP41245.

Proteomic databases

PaxDbP41245.
PRIDEP41245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737.
GeneID17395.
KEGGmmu:17395.

Organism-specific databases

CTD4318.
MGIMGI:97011. Mmp9.

Phylogenomic databases

eggNOGNOG328372.
GeneTreeENSGT00700000104196.
HOGENOMHOG000217926.
HOVERGENHBG052484.
InParanoidQ80XI8.
KOK01403.
OMAEGDLKWH.
OrthoDBEOG4H9XJZ.

Gene expression databases

ArrayExpressP41245.
BgeeP41245.
CleanExMM_MMP9.
GenevestigatorP41245.
GermOnlineENSMUSG00000017737. Mus musculus.

Family and domain databases

Gene3D2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProIPR000562. 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]
PfamPF00040. fn2. 3 hits.
PF00045. Hemopexin. 2 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF57440. Kringle-like. 3 hits.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. 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]
ProtoNetSearch...

Other

BindingDBP41245.
ChEMBLCHEMBL2214.
NextBio292032.
SOURCESearch...

Entry information

Entry nameMMP9_MOUSE
AccessionPrimary (citable) accession number: P41245
Secondary accession number(s): Q06788, Q80XI8, Q9DC02
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents