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Q9H239 (MMP28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-28

Short name=MMP-28
EC=3.4.24.-
Alternative name(s):
Epilysin
Gene names
Name:MMP28
Synonyms:MMP25
ORF Names:UNQ1893/PRO4339
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Can degrade casein. Could play a role in tissues homeostasis and repair.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Expressed at high levels in testes and lung. Low levels are detected in kidney, pancreas and skin. Also expressed in fetal lung, brain, skeletal muscle and kidney. Expressed selectively in keratinocytes. Widely expressed in several carcinomas as well. Is up-regulated in response to injury in the skin.

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H239-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H239-2)

The sequence of this isoform differs from the canonical sequence as follows:
     128-130: NKW → EHC
     131-520: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 122100 By similarity
PRO_0000028857
Chain123 – 520398Matrix metalloproteinase-28
PRO_0000028858

Regions

Repeat325 – 36945Hemopexin 1
Repeat370 – 40940Hemopexin 2
Repeat415 – 46349Hemopexin 3
Repeat464 – 51047Hemopexin 4
Motif89 – 968Cysteine switch By similarity

Sites

Active site2411 By similarity
Metal binding911Zinc; in inhibited form By similarity
Metal binding2401Zinc; catalytic By similarity
Metal binding2441Zinc; catalytic By similarity
Metal binding2501Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Disulfide bond324 ↔ 510 By similarity

Natural variations

Alternative sequence128 – 1303NKW → EHC in isoform 2.
VSP_040552
Alternative sequence131 – 520390Missing in isoform 2.
VSP_040553

Experimental info

Sequence conflict4871R → C in AAG41981. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2003. Version 2.
Checksum: E85D7ADA3069B063

FASTA52058,939
        10         20         30         40         50         60 
MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV PKAPTSTRFS 

        70         80         90        100        110        120 
DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA AWAERISDLF ARHRTKMRRK 

       130        140        150        160        170        180 
KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA VRGAVRAAFQ LWSNVSALEF WEAPATGPAD 

       190        200        210        220        230        240 
IRLTFFQGDH NDGLGNAFDG PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH 

       250        260        270        280        290        300 
EIGHTLGLTH SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF 

       310        320        330        340        350        360 
TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV AADGNVSEPR 

       370        380        390        400        410        420 
PLQERWVGLP PNIEAAAVSL NDGDFYFFKG GRCWRFRGPK PVWGLPQLCR AGGLPRHPDA 

       430        440        450        460        470        480 
ALFFPPLRRL ILFKGARYYV LARGGLQVEP YYPRSLQDWG GIPEEVSGAL PRPDGSIIFF 

       490        500        510        520 
RDDRYWRLDQ AKLQATTSGR WATELPWMGC WHANSGSALF 

« Hide

Isoform 2 [UniParc].

Checksum: 8A037DC95502660C
Show »

FASTA13014,927

References

« Hide 'large scale' references
[1]"MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors."
Marchenko G.N., Strongin A.Y.
Gene 265:87-93(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Lung.
[2]"Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury."
Lohi J., Wilson C.L., Roby J.D., Parks W.C.
J. Biol. Chem. 276:10134-10144(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
Tissue: Testis.
[3]"Cloning and genomic localization of a novel matrix metalloprotease."
Southan C., Hughes S.A.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 2).
Tissue: Pancreas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF315683 mRNA. Translation: AAG41981.1.
AF219624 mRNA. Translation: AAK01480.1.
AF330002 mRNA. Translation: AAK01706.1.
AY358987 mRNA. Translation: AAQ89346.1.
AC006237 Genomic DNA. No translation available.
AC015849 Genomic DNA. No translation available.
BC011774 mRNA. Translation: AAH11774.1.
RefSeqNP_001027449.1. NM_001032278.1.
NP_077278.1. NM_024302.3.
UniGeneHs.380710.

3D structure databases

ProteinModelPortalQ9H239.
SMRQ9H239. Positions 34-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000250144.

Protein family/group databases

MEROPSM10.030.

Polymorphism databases

DMDM37538314.

Proteomic databases

PaxDbQ9H239.
PRIDEQ9H239.

Protocols and materials databases

DNASU79148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250144; ENSP00000250144; ENSG00000129270. [Q9H239-2]
GeneID79148.
KEGGhsa:79148.
UCSCuc002hjy.1. human. [Q9H239-1]
uc002hka.3. human. [Q9H239-2]

Organism-specific databases

CTD79148.
GeneCardsGC17M034092.
HGNCHGNC:14366. MMP28.
MIM608417. gene.
neXtProtNX_Q9H239.
PharmGKBPA30885.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254923.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ9H239.
KOK08006.
PhylomeDBQ9H239.

Gene expression databases

ArrayExpressQ9H239.
BgeeQ9H239.
CleanExHS_MMP25.
HS_MMP28.
GenevestigatorQ9H239.

Family and domain databases

Gene3D1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028735. MMP28.
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:SF16. PTHR10201:SF16. 1 hit.
PfamPF00045. Hemopexin. 2 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]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP28.
GenomeRNAi79148.
NextBio68057.
PROQ9H239.
SOURCESearch...

Entry information

Entry nameMMP28_HUMAN
AccessionPrimary (citable) accession number: Q9H239
Secondary accession number(s): Q96F04, Q96TE2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 3, 2003
Last modified: April 16, 2014
This is version 131 of the entry and version 2 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 17

Human chromosome 17: entries, gene names and cross-references to MIM