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Reviewed, UniProtKB/Swiss-Prot P51511 (MMP15_HUMAN)

Last modified November 25, 2008. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Matrix metalloproteinase-15
      Short name=MMP-15
    EC=3.4.24.-
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
    SMCP-2
Gene names
Name: MMP15
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein; Extracellular sidePotential.

Tissue specificity

Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.

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-like domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PROCP040702EBI-1383043,EBI-1383018

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141Or 45 Potential
Propeptide42 – 13190 By similarity
PRO_0000028808
Chain132 – 669538Matrix metalloproteinase-15
PRO_0000028809

Regions

Topological domain132 – 625494Extracellular Potential
Transmembrane626 – 64621 Potential
Topological domain647 – 66923Cytoplasmic Potential
Domain374 – 41744Hemopexin-like 1
Domain419 – 46345Hemopexin-like 2
Domain466 – 51247Hemopexin-like 3
Domain514 – 55946Hemopexin-like 4
Motif109 – 1168Cysteine switch By similarity
Compositional bias331 – 34010Poly-Pro

Sites

Active site2601 By similarity
Metal binding1111Zinc; in inhibited form By similarity
Metal binding2591Zinc; catalytic By similarity
Metal binding2631Zinc; catalytic By similarity
Metal binding2691Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1501N-linked (GlcNAc...) Potential
Disulfide bond370 ↔ 559 By similarity

Natural variations

Natural variant2001L → P
VAR_030523
Natural variant3501P → L
VAR_030524
Natural variant5961D → G
VAR_030525
Natural variant6091G → R: dbSNP rs3743563.
VAR_020055
Natural variant6221R → W: dbSNP rs41434246.
VAR_030526

Sequences

Sequence LengthMass (Da)Tools
P51511-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FE875EC0674B297F

FASTA66975,807
        10         20         30         40         50         60 
MGSDPSAPGR PGWTGSLLGD REEAARPRLL PLLLVLLGCL GLGVAAEDAE VHAENWLRLY 

        70         80         90        100        110        120 
GYLPQPSRHM STMRSAQILA SALAEMQRFY GIPVTGVLDE ETKEWMKRPR CGVPDQFGVR 

       130        140        150        160        170        180 
VKANLRRRRK RYALTGRKWN NHHLTFSIQN YTEKLGWYHS MEAVRRAFRV WEQATPLVFQ 

       190        200        210        220        230        240 
EVPYEDIRLR RQKEADIMVL FASGFHGDSS PFDGTGGFLA HAYFPGPGLG GDTHFDADEP 

       250        260        270        280        290        300 
WTFSSTDLHG NNLFLVAVHE LGHALGLEHS SNPNAIMAPF YQWKDVDNFK LPEDDLRGIQ 

       310        320        330        340        350        360 
QLYGTPDGQP QPTQPLPTVT PRRPGRPDHR PPRPPQPPPP GGKPERPPKP GPPVQPRATE 

       370        380        390        400        410        420 
RPDQYGPNIC DGDFDTVAML RGEMFVFKGR WFWRVRHNRV LDNYPMPIGH FWRGLPGDIS 

       430        440        450        460        470        480 
AAYERQDGRF VFFKGDRYWL FREANLEPGY PQPLTSYGLG IPYDRIDTAI WWEPTGHTFF 

       490        500        510        520        530        540 
FQEDRYWRFN EETQRGDPGY PKPISVWQGI PASPKGAFLS NDAAYTYFYK GTKYWKFDNE 

       550        560        570        580        590        600 
RLRMEPGYPK SILRDFMGCQ EHVEPGPRWP DVARPPFNPH GGAEPGADSA EGDVGDGDGD 

       610        620        630        640        650        660 
FGAGVNKDGG SRVVVQMEEV ARTVNVVMVL VPLLLLLCVL GLTYALVQMQ RKGAPRVLLY 


CKRSLQEWV 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment."
Will H., Hinzmann B.
Eur. J. Biochem. 231:602-608(1995) [PubMed: 7649159] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Stanaway I.B., Nguyen C.P., Gildersleeve H., Johnson E.J., Swanson J.E., McFarland I., Park C., Nickerson D.A.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-200; LEU-350; GLY-596; ARG-609 AND TRP-622.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization."
Sato H., Tanaka M., Takino T., Inoue M., Seiki M.
Genomics 39:412-413(1997) [PubMed: 9119382] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-669, VARIANT ARG-609.
[5]Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-669.
Tissue: Placenta.
[6]"Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases."
d'Ortho M.P., Will H., Atkinson S., Butler G., Messent A., Gavrilovic J., Smith B., Timpl R., Zardi L., Murphy G.
Eur. J. Biochem. 250:751-757(1997) [PubMed: 9461298] [Abstract]
Cited for: FUNCTION.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-596.
+Additional computationally mapped references.

Cross-references

Sequence databases

Z48482 mRNA. Translation: CAA88373.1.
EF032329 Genomic DNA. Translation: ABJ53423.1.
BC036495 mRNA. Translation: AAH36495.1.
BC055428 mRNA. Translation: AAH55428.1.
D86331 mRNA. Translation: BAA13071.1. Different initiation.
D85510 mRNA. Translation: BAA22225.1.
PIRI38029.
RefSeqNP_002419.1.
UniGeneHs.80343

3D structure databases

HSSPHSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMRP51511. Positions 134-304.
ModBaseSearch...

Protein-protein interaction databases

IntActP51511.

Protein family/group databases

MEROPSM10.015.

PTM databases

PhosphoSiteP51511.

Polymorphism databases

NIEHS-SNPsSearch...

Genome annotation databases

EnsemblENSG00000102996. Homo sapiens. [Contig view]
GeneID4324.
KEGGhsa:4324.
NMPDRfig|9606.3.peg.12328.

Organism-specific databases

H-InvDBHIX0013084.
HGNCHGNC:7161. MMP15.
HPACAB002611.
MIM602261. gene.
PharmGKBPA30873.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP51511.
HOVERGENP51511.

Gene expression databases

ArrayExpressP51511.
CleanExHS_MMP15.
GermOnlineENSG00000102996. Homo sapiens.

Family and domain databases

InterProIPR000585. Hemopexin.
IPR001818. Pept_M10A_M12B.
IPR016293. Pept_M10A_matrix.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 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]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP51511.
NextBio17013.
SOURCESearch...

Entry information

Entry nameMMP15_HUMAN
AccessionPrimary (citable) accession number: P51511
Secondary accession number(s): A0A2U6, Q14111
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 25, 2008
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents