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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)DescriptionActionsGraphical viewLength
Metal bindingi107Zinc; in inhibited formBy similarity1
Metal bindingi255Zinc; catalyticPROSITE-ProRule annotation1
Active sitei256PROSITE-ProRule annotation1
Metal bindingi259Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi265Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • metalloendopeptidase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.B5. 3474.
ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109320. Mmp15.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini128 – 614ExtracellularSequence analysisAdd BLAST487
Transmembranei615 – 635HelicalSequence analysisAdd BLAST21
Topological domaini636 – 657CytoplasmicSequence analysisAdd BLAST22

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 36Sequence analysisAdd BLAST36
PropeptideiPRO_000002881037 – 127By similarityAdd BLAST91
ChainiPRO_0000028811128 – 657Matrix metalloproteinase-15Add BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi146N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi366 ↔ 555By similarity
Glycosylationi414N-linked (GlcNAc...)Sequence analysis1

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.
PaxDbiO54732.
PeptideAtlasiO54732.
PRIDEiO54732.

PTM databases

iPTMnetiO54732.
PhosphoSitePlusiO54732.
SwissPalmiO54732.

Expressioni

Gene expression databases

BgeeiENSMUSG00000031790.
CleanExiMM_MMP15.
GenevisibleiO54732. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034243.

Structurei

3D structure databases

ProteinModelPortaliO54732.
SMRiO54732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati363 – 411Hemopexin 1Add BLAST49
Repeati412 – 457Hemopexin 2Add BLAST46
Repeati459 – 507Hemopexin 3Add BLAST49
Repeati508 – 555Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi105 – 112Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi122 – 127Poly-Arg6

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiO54732.
KOiK07995.
OMAiCVLGLTY.
OrthoDBiEOG091G03DP.
PhylomeDBiO54732.
TreeFamiTF352396.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 3 hits.
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_008609.4.
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_008609.4.
UniGeneiMm.217116.

3D structure databases

ProteinModelPortaliO54732.
SMRiO54732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034243.

Protein family/group databases

MEROPSiM10.015.

PTM databases

iPTMnetiO54732.
PhosphoSitePlusiO54732.
SwissPalmiO54732.

Proteomic databases

MaxQBiO54732.
PaxDbiO54732.
PeptideAtlasiO54732.
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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiO54732.
KOiK07995.
OMAiCVLGLTY.
OrthoDBiEOG091G03DP.
PhylomeDBiO54732.
TreeFamiTF352396.

Enzyme and pathway databases

BRENDAi3.4.24.B5. 3474.
ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

PROiO54732.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031790.
CleanExiMM_MMP15.
GenevisibleiO54732. MM.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 3 hits.
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...

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: November 30, 2016
This is version 148 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

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 one 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.