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Protein

Matrix metalloproteinase-15

Gene

Mmp15

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

Functioni

Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi107 – 1071Zinc; in inhibited formBy similarity
Metal bindingi255 – 2551Zinc; catalyticPROSITE-ProRule annotation
Active sitei256 – 2561PROSITE-ProRule annotation
Metal bindingi259 – 2591Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi265 – 2651Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. response to estradiol Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Protein family/group databases

MEROPSiM10.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-15 (EC:3.4.24.-)
Short name:
MMP-15
Alternative name(s):
Membrane-type matrix metalloproteinase 2
Short name:
MT-MMP 2
Short name:
MTMMP2
Membrane-type-2 matrix metalloproteinase
Short name:
MT2-MMP
Short name:
MT2MMP
Gene namesi
Name:Mmp15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:109320. Mmp15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini128 – 614487ExtracellularSequence AnalysisAdd
BLAST
Transmembranei615 – 63521HelicalSequence AnalysisAdd
BLAST
Topological domaini636 – 65722CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. integral component of plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence AnalysisAdd
BLAST
Propeptidei37 – 12791By similarityPRO_0000028810Add
BLAST
Chaini128 – 657530Matrix metalloproteinase-15PRO_0000028811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi366 ↔ 555By similarity
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO54732.
PRIDEiO54732.

PTM databases

PhosphoSiteiO54732.

Expressioni

Gene expression databases

BgeeiO54732.
CleanExiMM_MMP15.
ExpressionAtlasiO54732. baseline and differential.
GenevestigatoriO54732.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034243.

Structurei

3D structure databases

ProteinModelPortaliO54732.
SMRiO54732. Positions 79-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati363 – 41149Hemopexin 1Add
BLAST
Repeati412 – 45746Hemopexin 2Add
BLAST
Repeati459 – 50749Hemopexin 3Add
BLAST
Repeati508 – 55548Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi105 – 1128Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 1276Poly-Arg

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, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiO54732.
KOiK07995.
OMAiVEPGPRW.
OrthoDBiEOG7XPZ57.
PhylomeDBiO54732.
TreeFamiTF352396.

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.
IPR028729. MMP15.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF25. PTHR10201:SF25. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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.

O54732-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSDRSALGR PGCTGSCLSS RASLLPLLLV LLDCLGHGTA SKDAEVYAAE
60 70 80 90 100
NWLRLYGYLP QPSRHMSTMR SAQILASALA EMQSFYGIPV TGVLDEETKT
110 120 130 140 150
WMKRPRCGVP DQFGVHVKAN LRRRRKRYTL TGKAWNNYHL TFSIQNYTEK
160 170 180 190 200
LGWYNSMEAV RRAFQVWEQV TPLVFQEVSY DDIRLRRRAE ADIMVLFASG
210 220 230 240 250
FHGDSSPFDG VGGFLAHAYF PGPGLGGDTH FDADEPWTFS STDLHGISLF
260 270 280 290 300
LVAVHELGHA LGLEHSSNPS AIMAPFYQWM DTDNFQLPED DLRGIQQLYG
310 320 330 340 350
SPDGKPQPTR PLPTVRPRRP GRPDHQPPRP PQPPHPGGKP ERPPKPGPPP
360 370 380 390 400
QPRATERPDQ YGPNICDGNF DTVAVLRGEM FVFKGRWFWR VRHNRVLDNY
410 420 430 440 450
PMPIGHFWRG LPGNISAAYE RQDGHFVFFK GNRYWLFREA NLEPGYPQPL
460 470 480 490 500
SSYGTDIPYD RIDTAIWWEP TGHTFFFQAD RYWRFNEETQ HGDPGYPKPI
510 520 530 540 550
SVWQGIPTSP KGAFLSNDAA YTYFYKGTKY WKFNNERLRM EPGHPKSILR
560 570 580 590 600
DFMGCQEHVE PRSRWPDVAR PPFNPNGGAE PEADGDSKEE NAGDKDEGSR
610 620 630 640 650
VVVQMEEVVR TVNVVMVLVP LLLLLCILGL AFALVQMQRK GAPRMLLYCK

RSLQEWV
Length:657
Mass (Da):74,666
Last modified:June 1, 1998 - v1
Checksum:i26803400A6836EF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86332 mRNA. Translation: BAA23667.1.
BC047278 mRNA. Translation: AAH47278.1.
BC057952 mRNA. Translation: AAH57952.1.
CCDSiCCDS22561.1.
RefSeqiNP_032635.1. NM_008609.3.
UniGeneiMm.217116.

Genome annotation databases

EnsembliENSMUST00000034243; ENSMUSP00000034243; ENSMUSG00000031790.
GeneIDi17388.
KEGGimmu:17388.
UCSCiuc009myh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86332 mRNA. Translation: BAA23667.1.
BC047278 mRNA. Translation: AAH47278.1.
BC057952 mRNA. Translation: AAH57952.1.
CCDSiCCDS22561.1.
RefSeqiNP_032635.1. NM_008609.3.
UniGeneiMm.217116.

3D structure databases

ProteinModelPortaliO54732.
SMRiO54732. Positions 79-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034243.

Protein family/group databases

MEROPSiM10.015.

PTM databases

PhosphoSiteiO54732.

Proteomic databases

MaxQBiO54732.
PRIDEiO54732.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034243; ENSMUSP00000034243; ENSMUSG00000031790.
GeneIDi17388.
KEGGimmu:17388.
UCSCiuc009myh.1. mouse.

Organism-specific databases

CTDi4324.
MGIiMGI:109320. Mmp15.

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiO54732.
KOiK07995.
OMAiVEPGPRW.
OrthoDBiEOG7XPZ57.
PhylomeDBiO54732.
TreeFamiTF352396.

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

NextBioi292004.
PROiO54732.
SOURCEiSearch...

Gene expression databases

BgeeiO54732.
CleanExiMM_MMP15.
ExpressionAtlasiO54732. baseline and differential.
GenevestigatoriO54732.

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.
IPR028729. MMP15.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF25. PTHR10201:SF25. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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. "Isolation of a mouse MT2-MMP gene from a lung cDNA library and identification of its product."
    Tanaka M., Sato H., Takino T., Iwata K., Inoue M., Seiki M.
    FEBS Lett. 402:219-222(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  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].
    Strain: NMRI.
    Tissue: Mammary gland and Olfactory epithelium.

Entry informationi

Entry nameiMMP15_MOUSE
AccessioniPrimary (citable) accession number: O54732
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 133 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.