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Q9NPA2 (MMP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-25

Short name=MMP-25
EC=3.4.24.-
Alternative name(s):
Leukolysin
Membrane-type matrix metalloproteinase 6
Short name=MT-MMP 6
Short name=MTMMP6
Membrane-type-6 matrix metalloproteinase
Short name=MT6-MMP
Short name=MT6MMP
Gene names
Name:MMP25
Synonyms:MMP20, MMPL1, MT6MMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May activate progelatinase A.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor; Extracellular side. Secretedextracellular spaceextracellular matrix Ref.3.

Tissue specificity

Expressed predominantly in leukocytes, lung and spleen. Expressed also in colon carcinoma, astrocytoma and glioblastomas.

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 repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 10786 By similarity
PRO_0000028852
Chain108 – 539432Matrix metalloproteinase-25
PRO_0000028853
Propeptide540 – 56223Removed in mature form Potential
PRO_0000028854

Regions

Repeat314 – 36350Hemopexin 1
Repeat367 – 41246Hemopexin 2
Repeat413 – 46149Hemopexin 3
Repeat462 – 50847Hemopexin 4
Motif88 – 958Cysteine switch By similarity
Compositional bias103 – 1075Poly-Arg
Compositional bias549 – 5557Poly-Leu

Sites

Active site2341 By similarity
Metal binding901Zinc; in inhibited form By similarity
Metal binding2331Zinc; catalytic By similarity
Metal binding2371Zinc; catalytic By similarity
Metal binding2431Zinc; catalytic By similarity

Amino acid modifications

Lipidation5391GPI-anchor amidated alanine Potential
Disulfide bond317 ↔ 508 By similarity

Experimental info

Sequence conflict471P → R in BAB20584. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9NPA2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A6A50AE05D969C64

FASTA56262,554
        10         20         30         40         50         60 
MRLRLRLLAL LLLLLAPPAR APKPSAQDVS LGVDWLTRYG YLPPPHPAQA QLQSPEKLRD 

        70         80         90        100        110        120 
AIKVMQRFAG LPETGRMDPG TVATMRKPRC SLPDVLGVAG LVRRRRRYAL SGSVWKKRTL 

       130        140        150        160        170        180 
TWRVRSFPQS SQLSQETVRV LMSYALMAWG MESGLTFHEV DSPQGQEPDI LIDFARAFHQ 

       190        200        210        220        230        240 
DSYPFDGLGG TLAHAFFPGE HPISGDTHFD DEETWTFGSK DGEGTDLFAV AVHEFGHALG 

       250        260        270        280        290        300 
LGHSSAPNSI MRPFYQGPVG DPDKYRLSQD DRDGLQQLYG KAPQTPYDKP TRKPLAPPPQ 

       310        320        330        340        350        360 
PPASPTHSPS FPIPDRCEGN FDAIANIRGE TFFFKGPWFW RLQPSGQLVS PRPARLHRFW 

       370        380        390        400        410        420 
EGLPAQVRVV QAAYARHRDG RILLFSGPQF WVFQDRQLEG GARPLTELGL PPGEEVDAVF 

       430        440        450        460        470        480 
SWPQNGKTYL VRGRQYWRYD EAAARPDPGY PRDLSLWEGA PPSPDDVTVS NAGDTYFFKG 

       490        500        510        520        530        540 
AHYWRFPKNS IKTEPDAPQP MGPNWLDCPA PSSGPRAPRP PKATPVSETC DCQCELNQAA 

       550        560 
GRWPAPIPLL LLPLLVGGVA SR 

« Hide

References

« Hide 'large scale' references
[1]"Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors."
Velasco G., Cal S., Merlos-Suarez A., Ferrando A.A., Alvarez S., Nakano A., Arribas J., Lopez-Otin C.
Cancer Res. 60:877-882(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[2]"Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase specifically expressed in the leukocyte lineage."
Pei D.Q.
Cell Res. 9:291-303(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP."
Kojima S., Itoh Y., Matsumoto S., Masuho Y., Seiki M.
FEBS Lett. 480:142-146(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GPI-ANCHOR.
[4]"Molecular cloning of a novel human membrane-type matrix metalloproteinase (MT-MMP) predominantly expressed in dendritic cells."
de Saint-Vis B.M., Clair-Moninot V.A., Lambert C.A., Vanbervliet B., Pin J.J., Chalus L., Ait-Yahia S., Caux C., Richelle-Nusgens B.V., Fossiez F., Lebecque S.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ239053 mRNA. Translation: CAB94713.1.
AF145442 mRNA. Translation: AAF66697.2.
AF185270 mRNA. Translation: AAG17007.1.
AB042328 mRNA. Translation: BAB20584.1.
AJ272137 mRNA. Translation: CAC03490.1.
CH471112 Genomic DNA. Translation: EAW85413.1.
CH471112 Genomic DNA. Translation: EAW85415.1.
RefSeqNP_071913.1. NM_022468.4.
UniGeneHs.654979.

3D structure databases

ProteinModelPortalQ9NPA2.
SMRQ9NPA2. Positions 26-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122149. 2 interactions.
STRING9606.ENSP00000337816.

Chemistry

BindingDBQ9NPA2.
ChEMBLCHEMBL1795103.

Protein family/group databases

MEROPSM10.024.

PTM databases

PhosphoSiteQ9NPA2.

Polymorphism databases

DMDM12585274.

Proteomic databases

PaxDbQ9NPA2.
PRIDEQ9NPA2.

Protocols and materials databases

DNASU64386.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336577; ENSP00000337816; ENSG00000008516.
GeneID64386.
KEGGhsa:64386.
UCSCuc002cth.3. human.

Organism-specific databases

CTD64386.
GeneCardsGC16P003127.
HGNCHGNC:14246. MMP25.
HPACAB025177.
MIM608482. gene.
neXtProtNX_Q9NPA2.
PharmGKBPA30882.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295915.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ9NPA2.
KOK08003.
OMAHYWRFPK.
OrthoDBEOG7XPZ57.
PhylomeDBQ9NPA2.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeQ9NPA2.
CleanExHS_MMP20.
HS_MMP25.
GenevestigatorQ9NPA2.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028733. MMP25.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF22. PTHR10201:SF22. 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]
SUPFAMSSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP25.
GenomeRNAi64386.
NextBio66313.
PROQ9NPA2.
SOURCESearch...

Entry information

Entry nameMMP25_HUMAN
AccessionPrimary (citable) accession number: Q9NPA2
Secondary accession number(s): D3DUA8, Q9H3Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human chromosome 16

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