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O55123 (MMP10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. 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:
Stromelysin-2
Short name=SL-2
EC=3.4.24.22
Alternative name(s):
Matrix metalloproteinase-10
Short name=MMP-10
Transin-2
Gene names
Name:Mmp10
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 length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.

Catalytic activity

Similar to stromelysin 1, but action on collagen types III, IV and V is weak.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Calcium By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix Probable.

Tissue specificity

Expressed in small intestine. Weak levels in heart and lung.

Induction

By wounding.

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.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Probable
Propeptide18 – 9982Activation peptide By similarity
PRO_0000028766
Chain100 – 476377Stromelysin-2
PRO_0000028767

Regions

Domain295 – 33743Hemopexin-like 1
Domain339 – 38244Hemopexin-like 2
Domain387 – 43448Hemopexin-like 3
Domain436 – 47641Hemopexin-like 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191 By similarity
Metal binding921Zinc; in inhibited form By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity

Amino acid modifications

Disulfide bond289 ↔ 476 By similarity

Sequences

Sequence LengthMass (Da)Tools
O55123 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2EB1CC41468F0AC6

FASTA47653,911
        10         20         30         40         50         60 
MEPLAILALL SLPICSAYPL HGAVTQGHPS MDLAQQYLEK YYNFKKNEKQ IFKRKDSSPV 

        70         80         90        100        110        120 
VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF STFPGSPKWR KSHITYRIVN 

       130        140        150        160        170        180 
YTPDLPRQSV DSAIEKALKV WEEVTPLTFS RISEGEADIM ISFAVGEHGD FYPFDGPGQS 

       190        200        210        220        230        240 
LAHAYPPGPG FYGDVHFDDD EKWTLAPSGT NLFLVAAHEL GHSLGLFHSD KKESLMYPVY 

       250        260        270        280        290        300 
RFSTSPANFH LSQDDIEGIQ SLYGAGPSSD ATVVPVLSVS PRPETPDKCD PALSFDSVST 

       310        320        330        340        350        360 
LRGEVLFFKD RYFWRRSHWN PEPEFHLISA FWPTLPSDLD AAYEAHNTDS VLIFKGSQFW 

       370        380        390        400        410        420 
AVRGNEVQAG YPKGIHTLGF PPTVKKIDAA VFEKEKKKTY FFVGDKYWRF DETRHVMDKG 

       430        440        450        460        470 
FPRQITDDFP GIEPQVDAVL HEFGFFYFFR GSSQFEFDPN ARTVTHILKS NSWLLC

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of the gene encoding murine stromelysin-2 (MMP-10)."
Madlener M., Werner S.
Gene 202:75-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"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: Cecum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13185 mRNA. Translation: CAA73641.1.
AK020292 mRNA. Translation: BAB32058.1.
IPIIPI00115822.
PIRJC6505.
RefSeqNP_062344.1. NM_019471.2.
UniGeneMm.14126.

3D structure databases

ProteinModelPortalO55123.
SMRO55123. Positions 31-476.
ModBaseSearch...

Protein family/group databases

MEROPSM10.011.

PTM databases

PhosphoSiteO55123.

Proteomic databases

PRIDEO55123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034488; ENSMUSP00000034488; ENSMUSG00000047562.
GeneID17384.
KEGGmmu:17384.

Organism-specific databases

CTD4319.
MGIMGI:97007. Mmp10.

Phylogenomic databases

eggNOGNOG270148.
GeneTreeENSGT00630000089491.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidO55123.
KOK01396.
OMAMEQGFPR.
OrthoDBEOG4KKZ2X.

Gene expression databases

ArrayExpressO55123.
BgeeO55123.
CleanExMM_MMP10.
GenevestigatorO55123.
GermOnlineENSMUSG00000047562. Mus musculus.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_Metazoans.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
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]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291988.
SOURCESearch...

Entry information

Entry nameMMP10_MOUSE
AccessionPrimary (citable) accession number: O55123
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 117 of the entry and version 1 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