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Protein

Stromelysin-2

Gene

Mmp10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc; in inhibited formBy similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi170 – 1701Zinc 1By similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi196 – 1961Zinc 1By similarity
Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
Active sitei219 – 2191PROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
Metal bindingi228 – 2281Zinc 2; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • collagen catabolic process Source: UniProtKB-KW
  • regulation of cell migration Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.
REACT_332323. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiM10.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-2 (EC:3.4.24.22)
Short name:
SL-2
Alternative name(s):
Matrix metalloproteinase-10
Short name:
MMP-10
Transin-2
Gene namesi
Name:Mmp10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97007. Mmp10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717CuratedAdd
BLAST
Propeptidei18 – 9982Activation peptideBy similarityPRO_0000028766Add
BLAST
Chaini100 – 476377Stromelysin-2PRO_0000028767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi289 ↔ 476By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PRIDEiO55123.

PTM databases

PhosphoSiteiO55123.

Expressioni

Tissue specificityi

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

Inductioni

By wounding.

Gene expression databases

BgeeiO55123.
CleanExiMM_MMP10.
ExpressionAtlasiO55123. baseline and differential.
GenevestigatoriO55123.

Structurei

3D structure databases

ProteinModelPortaliO55123.
SMRiO55123. Positions 31-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati286 – 33550Hemopexin 1Add
BLAST
Repeati336 – 38247Hemopexin 2Add
BLAST
Repeati384 – 43249Hemopexin 3Add
BLAST
Repeati433 – 47644Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switchBy similarity

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG270148.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO55123.
KOiK01396.
OMAiMEQGFPR.
OrthoDBiEOG7XPZ57.
PhylomeDBiO55123.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O55123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPLAILALL SLPICSAYPL HGAVTQGHPS MDLAQQYLEK YYNFKKNEKQ
60 70 80 90 100
IFKRKDSSPV VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF
110 120 130 140 150
STFPGSPKWR KSHITYRIVN YTPDLPRQSV DSAIEKALKV WEEVTPLTFS
160 170 180 190 200
RISEGEADIM ISFAVGEHGD FYPFDGPGQS LAHAYPPGPG FYGDVHFDDD
210 220 230 240 250
EKWTLAPSGT NLFLVAAHEL GHSLGLFHSD KKESLMYPVY RFSTSPANFH
260 270 280 290 300
LSQDDIEGIQ SLYGAGPSSD ATVVPVLSVS PRPETPDKCD PALSFDSVST
310 320 330 340 350
LRGEVLFFKD RYFWRRSHWN PEPEFHLISA FWPTLPSDLD AAYEAHNTDS
360 370 380 390 400
VLIFKGSQFW AVRGNEVQAG YPKGIHTLGF PPTVKKIDAA VFEKEKKKTY
410 420 430 440 450
FFVGDKYWRF DETRHVMDKG FPRQITDDFP GIEPQVDAVL HEFGFFYFFR
460 470
GSSQFEFDPN ARTVTHILKS NSWLLC
Length:476
Mass (Da):53,911
Last modified:June 1, 1998 - v1
Checksum:i2EB1CC41468F0AC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13185 mRNA. Translation: CAA73641.1.
AK020292 mRNA. Translation: BAB32058.1.
CCDSiCCDS22807.1.
PIRiJC6505.
RefSeqiNP_062344.1. NM_019471.3.
UniGeneiMm.14126.

Genome annotation databases

EnsembliENSMUST00000034488; ENSMUSP00000034488; ENSMUSG00000047562.
GeneIDi17384.
KEGGimmu:17384.
UCSCiuc009ocq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13185 mRNA. Translation: CAA73641.1.
AK020292 mRNA. Translation: BAB32058.1.
CCDSiCCDS22807.1.
PIRiJC6505.
RefSeqiNP_062344.1. NM_019471.3.
UniGeneiMm.14126.

3D structure databases

ProteinModelPortaliO55123.
SMRiO55123. Positions 31-476.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.011.

PTM databases

PhosphoSiteiO55123.

Proteomic databases

PRIDEiO55123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034488; ENSMUSP00000034488; ENSMUSG00000047562.
GeneIDi17384.
KEGGimmu:17384.
UCSCiuc009ocq.1. mouse.

Organism-specific databases

CTDi4319.
MGIiMGI:97007. Mmp10.

Phylogenomic databases

eggNOGiNOG270148.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiO55123.
KOiK01396.
OMAiMEQGFPR.
OrthoDBiEOG7XPZ57.
PhylomeDBiO55123.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_313067. Collagen degradation.
REACT_332323. Activation of Matrix Metalloproteinases.

Miscellaneous databases

NextBioi291988.
PROiO55123.
SOURCEiSearch...

Gene expression databases

BgeeiO55123.
CleanExiMM_MMP10.
ExpressionAtlasiO55123. baseline and differential.
GenevestigatoriO55123.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMMP10_MOUSE
AccessioniPrimary (citable) accession number: O55123
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 1998
Last modified: April 1, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.