Q9H239 (MMP28_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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-like domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Non-traceable author statement. Source: UniProtKB
Cellular_component	proteinaceous extracellular matrix Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Traceable author statement Ref.2Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 122	100	By similarity		PRO_0000028857
	Chain	123 – 520	398	Matrix metalloproteinase-28		PRO_0000028858
Regions
	Domain	328 – 371	44	Hemopexin-like 1
	Domain	373 – 416	44	Hemopexin-like 2
	Domain	418 – 464	47	Hemopexin-like 3
	Domain	466 – 510	45	Hemopexin-like 4
	Motif	89 – 96	8	Cysteine switch By similarity
Sites
	Active site	241	1	By similarity
	Metal binding	91	1	Zinc; in inhibited form By similarity
	Metal binding	240	1	Zinc; catalytic By similarity
	Metal binding	244	1	Zinc; catalytic By similarity
	Metal binding	250	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
	Disulfide bond	324 ↔ 510		By similarity
Natural variations
	Alternative sequence	128 – 130	3	NKW → EHC in isoform 2.		VSP_040552
	Alternative sequence	131 – 520	390	Missing in isoform 2.		VSP_040553
Experimental info
	Sequence conflict	487	1	R → C in AAG41981. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 3, 2003. Version 2. Checksum: E85D7ADA3069B063	FASTA	520	58,939
	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
	Isoform 2 [UniParc]. Checksum: 8A037DC95502660C	FASTA	130	14,927
	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 KRFAKQGEHC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00425258. IPI00792702.
RefSeq	NP_001027449.1. NM_001032278.1. NP_077278.1. NM_024302.3.
UniGene	Hs.380710.
3D structure databases
ProteinModelPortal	Q9H239.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000250144.
Protein family/group databases
MEROPS	M10.030.
Polymorphism databases
DMDM	37538314.
Proteomic databases
PaxDb	Q9H239.
PRIDE	Q9H239.
Protocols and materials databases
DNASU	79148.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000250144; ENSP00000250144; ENSG00000129270.
GeneID	79148.
KEGG	hsa:79148.
UCSC	uc002hjy.1. human. uc002hka.3. human.
Organism-specific databases
CTD	79148.
GeneCards	GC17M034092.
HGNC	HGNC:14366. MMP28.
MIM	608417. gene.
neXtProt	NX_Q9H239.
PharmGKB	PA30885.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG254923.
HOGENOM	HOG000217927.
HOVERGEN	HBG052484.
InParanoid	Q9H239.
KO	K08006.
OrthoDB	EOG4JDH6M.
Gene expression databases
Bgee	Q9H239.
CleanEx	HS_MMP25. HS_MMP28.
Genevestigator	Q9H239.
GermOnline	ENSG00000129270. Homo sapiens.
Family and domain databases
Gene3D	1.10.101.10. 1 hit. 2.110.10.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR016293. Pept_M10A_Metazoans. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Pfam	PF00045. Hemopexin. 2 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. False negative. PS00024. HEMOPEXIN. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4870.
GenomeRNAi	79148.
NextBio	68057.
SOURCE	Search...

Entry information

Entry name

MMP28_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.