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Q3U435 (MMP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-25

Short name=MMP-25
EC=3.4.24.-
Gene names
Name:Mmp25
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May activate progelatinase A By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

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

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Caution

In contrast to the human ortholog it does not have a signal sequence as it has an additional 53 residue sequence at the N-terminus. At the position of the human initiation methionine there is a leucine (Leu-54).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 162162 By similarity
PRO_0000288635
Chain163 – 593431Matrix metalloproteinase-25
PRO_0000288636
Propeptide594 – 61522Removed in mature form Potential
PRO_0000288637

Regions

Transmembrane53 – 7321Helical; Potential
Repeat368 – 41750Hemopexin 1
Repeat421 – 46646Hemopexin 2
Repeat467 – 51549Hemopexin 3
Repeat516 – 56247Hemopexin 4
Motif143 – 1508Cysteine switch By similarity
Compositional bias158 – 1625Poly-Arg
Compositional bias340 – 36829Pro-rich

Sites

Active site2881 By similarity
Metal binding1451Zinc; in inhibited form By similarity
Metal binding2871Zinc; catalytic By similarity
Metal binding2911Zinc; catalytic By similarity
Metal binding2971Zinc; catalytic By similarity

Amino acid modifications

Lipidation5931GPI-anchor amidated alanine Potential
Disulfide bond371 ↔ 562 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3U435 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 7B0842CACF06382D

FASTA61568,496
        10         20         30         40         50         60 
MCFPGSQISP ARLYYLVSAP WICTGSLTSS RLPRRRESGP LRVPPRSVQA ERILRLPAFG 

        70         80         90        100        110        120 
LPLLALLLVP LLPVRAQNPD AKVVSMGVEW LTRYGYLPPA DPVHAQMQSL EKLQDAIKVM 

       130        140        150        160        170        180 
QRFAGLPETG QMDPMTIKTM RKPRCSLPDV LGAAGLVRRR RRYSLSGSVW KKRTLTWSIR 

       190        200        210        220        230        240 
SFSQKSQLSP QIVRTLLSYA LAVWATESGL TFQEVNSQYQ EPDIIIHFAR AYHQDSYPFD 

       250        260        270        280        290        300 
GSGGTLAHAF FPGEHPISGD THFDDEETWT FGSTDDNGID LFAVAVHEFG HALGLGHSSA 

       310        320        330        340        350        360 
PNSIMRPFYQ GPVGDPATYR LPQDDRDGLQ QLYGRVSQNP NARPTRKPLV PPPQPPAMPP 

       370        380        390        400        410        420 
DSPATPVPDR CEGNFDAVAN IRGEIFLFKG PWFWRLQPSG QLVSPRPAGL HRFWEGLPTH 

       430        440        450        460        470        480 
VKVIQAAYAR PLDGRIILFS GPQFWVFQER QLEGAARPLV EFGLPPGEDV DAVFSWPHNG 

       490        500        510        520        530        540 
KTYLIRGQKY WRYDEVAARP DPGYPRALSL WDGAPFAPDD VTISNTGDTY FFKGTHFWRF 

       550        560        570        580        590        600 
AEGSVKAESD SPQPIGPKWL DCPAPNSDPR VTSPPKTTSK TRSCDCHCEL NQASEQLSPL 

       610 
LLPLLPLVAG EVFSY 

« Hide

References

[1]"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: NOD.
[2]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK154458 mRNA. Translation: BAE32600.1.
BC112379 mRNA. Translation: AAI12380.1.
RefSeqNP_001028511.1. NM_001033339.3.
UniGeneMm.235343.

3D structure databases

ProteinModelPortalQ3U435.
SMRQ3U435. Positions 84-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000024696.

Protein family/group databases

MEROPSM10.024.

PTM databases

PhosphoSiteQ3U435.

Proteomic databases

PRIDEQ3U435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024696; ENSMUSP00000024696; ENSMUSG00000023903.
GeneID240047.
KEGGmmu:240047.
UCSCuc008asq.1. mouse.

Organism-specific databases

CTD64386.
MGIMGI:2443938. Mmp25.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00750000117336.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ3U435.
KOK08003.
OMAHYWRFPK.
OrthoDBEOG7XPZ57.
PhylomeDBQ3U435.
TreeFamTF315428.

Gene expression databases

BgeeQ3U435.
CleanExMM_MMP25.
GenevestigatorQ3U435.

Family and domain databases

Gene3D1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF22. PTHR10201:SF22. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384387.
PROQ3U435.
SOURCESearch...

Entry information

Entry nameMMP25_MOUSE
AccessionPrimary (citable) accession number: Q3U435
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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