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Protein

Matrix metalloproteinase-28

Gene

MMP28

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

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 bindingi91 – 911Zinc; in inhibited formBy similarity
Metal bindingi240 – 2401Zinc; catalyticPROSITE-ProRule annotation
Active sitei241 – 2411PROSITE-ProRule annotation
Metal bindingi244 – 2441Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi250 – 2501Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of macrophage chemotaxis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-28 (EC:3.4.24.-)
Short name:
MMP-28
Alternative name(s):
Epilysin
Gene namesi
Name:MMP28
Synonyms:MMP25
ORF Names:UNQ1893/PRO4339
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 17, Unplaced

Organism-specific databases

HGNCiHGNC:14366. MMP28.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30885.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Propeptidei23 – 122100By similarityPRO_0000028857Add
BLAST
Chaini123 – 520398Matrix metalloproteinase-28PRO_0000028858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi324 ↔ 510By similarity
Glycosylationi355 – 3551N-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

PaxDbiQ9H239.
PRIDEiQ9H239.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ9H239.
CleanExiHS_MMP25.
HS_MMP28.
ExpressionAtlasiQ9H239. baseline and differential.
GenevestigatoriQ9H239.

Interactioni

Protein-protein interaction databases

BioGridi122566. 2 interactions.
STRINGi9606.ENSP00000250144.

Structurei

3D structure databases

ProteinModelPortaliQ9H239.
SMRiQ9H239. Positions 33-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati325 – 36945Hemopexin 1Add
BLAST
Repeati370 – 40940Hemopexin 2Add
BLAST
Repeati415 – 46349Hemopexin 3Add
BLAST
Repeati464 – 51047Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi89 – 968Cysteine switchBy similarity

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

Phylogenomic databases

eggNOGiNOG254923.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9H239.
KOiK08006.
OMAiFEAWDPH.
PhylomeDBiQ9H239.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. 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]
PANTHERiPTHR10201:SF16. PTHR10201:SF16. 1 hit.
PfamiPF00045. Hemopexin. 2 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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H239-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV
60 70 80 90 100
PKAPTSTRFS DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA
110 120 130 140 150
AWAERISDLF ARHRTKMRRK KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA
160 170 180 190 200
VRGAVRAAFQ LWSNVSALEF WEAPATGPAD IRLTFFQGDH NDGLGNAFDG
210 220 230 240 250
PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH EIGHTLGLTH
260 270 280 290 300
SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF
310 320 330 340 350
TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV
360 370 380 390 400
AADGNVSEPR PLQERWVGLP PNIEAAAVSL NDGDFYFFKG GRCWRFRGPK
410 420 430 440 450
PVWGLPQLCR AGGLPRHPDA ALFFPPLRRL ILFKGARYYV LARGGLQVEP
460 470 480 490 500
YYPRSLQDWG GIPEEVSGAL PRPDGSIIFF RDDRYWRLDQ AKLQATTSGR
510 520
WATELPWMGC WHANSGSALF
Length:520
Mass (Da):58,939
Last modified:October 2, 2003 - v2
Checksum:iE85D7ADA3069B063
GO
Isoform 2 (identifier: Q9H239-2) [UniParc]FASTAAdd to basket

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

Show »
Length:130
Mass (Da):14,927
Checksum:i8A037DC95502660C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti487 – 4871R → C in AAG41981 (PubMed:11255011).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei128 – 1303NKW → EHC in isoform 2. 1 PublicationVSP_040552
Alternative sequencei131 – 520390Missing in isoform 2. 1 PublicationVSP_040553Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45651.1. [Q9H239-2]
CCDS74036.1. [Q9H239-1]
RefSeqiNP_001027449.1. NM_001032278.2. [Q9H239-2]
NP_077278.1. NM_024302.4. [Q9H239-1]
NP_116568.1. NM_032950.3.
UniGeneiHs.380710.

Genome annotation databases

EnsembliENST00000605424; ENSP00000473853; ENSG00000271447. [Q9H239-1]
ENST00000611911; ENSP00000484430; ENSG00000278843. [Q9H239-1]
ENST00000612672; ENSP00000483539; ENSG00000271447. [Q9H239-2]
GeneIDi79148.
KEGGihsa:79148.
UCSCiuc002hjy.1. human. [Q9H239-1]
uc002hka.3. human. [Q9H239-2]

Polymorphism databases

DMDMi37538314.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45651.1. [Q9H239-2]
CCDS74036.1. [Q9H239-1]
RefSeqiNP_001027449.1. NM_001032278.2. [Q9H239-2]
NP_077278.1. NM_024302.4. [Q9H239-1]
NP_116568.1. NM_032950.3.
UniGeneiHs.380710.

3D structure databases

ProteinModelPortaliQ9H239.
SMRiQ9H239. Positions 33-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122566. 2 interactions.
STRINGi9606.ENSP00000250144.

Chemistry

DrugBankiDB00786. Marimastat.

Protein family/group databases

MEROPSiM10.030.

Polymorphism databases

DMDMi37538314.

Proteomic databases

PaxDbiQ9H239.
PRIDEiQ9H239.

Protocols and materials databases

DNASUi79148.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000605424; ENSP00000473853; ENSG00000271447. [Q9H239-1]
ENST00000611911; ENSP00000484430; ENSG00000278843. [Q9H239-1]
ENST00000612672; ENSP00000483539; ENSG00000271447. [Q9H239-2]
GeneIDi79148.
KEGGihsa:79148.
UCSCiuc002hjy.1. human. [Q9H239-1]
uc002hka.3. human. [Q9H239-2]

Organism-specific databases

CTDi79148.
GeneCardsiGC17M034092.
HGNCiHGNC:14366. MMP28.
MIMi608417. gene.
neXtProtiNX_Q9H239.
PharmGKBiPA30885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG254923.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9H239.
KOiK08006.
OMAiFEAWDPH.
PhylomeDBiQ9H239.

Miscellaneous databases

GeneWikiiMMP28.
GenomeRNAii79148.
NextBioi68057.
PROiQ9H239.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H239.
CleanExiHS_MMP25.
HS_MMP28.
ExpressionAtlasiQ9H239. baseline and differential.
GenevestigatoriQ9H239.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. 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]
PANTHERiPTHR10201:SF16. PTHR10201:SF16. 1 hit.
PfamiPF00045. Hemopexin. 2 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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2000) [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(2000) [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 (NOV-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. 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.
    , 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(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Pancreas.

Entry informationi

Entry nameiMMP28_HUMAN
AccessioniPrimary (citable) accession number: Q9H239
Secondary accession number(s): Q96F04, Q96TE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2001
Last sequence update: October 2, 2003
Last modified: January 6, 2015
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.