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Matrix metalloproteinase-28 (MMP-28) (EC 3.4.24.-) (Epilysin)

 MMP28_HUMAN             Reviewed;         520 AA.
Q9H239; Q96F04; Q96TE2;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
03-OCT-2003, sequence version 2.
20-JUN-2018, entry version 166.
RecName: Full=Matrix metalloproteinase-28;
Short=MMP-28;
EC=3.4.24.-;
AltName: Full=Epilysin;
Flags: Precursor;
Name=MMP28; Synonyms=MMP25; ORFNames=UNQ1893/PRO4339;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=11255011; DOI=10.1016/S0378-1119(01)00360-2;
Marchenko G.N., Strongin A.Y.;
"MMP-28, a new human matrix metalloproteinase with an unusual
cysteine-switch sequence is widely expressed in tumors.";
Gene 265:87-93(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
TISSUE=Testis;
PubMed=11121398; DOI=10.1074/jbc.M001599200;
Lohi J., Wilson C.L., Roby J.D., Parks W.C.;
"Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed
in testis and keratinocytes and in response to injury.";
J. Biol. Chem. 276:10134-10144(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Southan C., Hughes S.A.;
"Cloning and genomic localization of a novel matrix metalloprotease.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
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.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Can degrade casein. Could play a role in tissues
homeostasis and repair.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H239-1; Sequence=Displayed;
Name=2;
IsoId=Q9H239-2; Sequence=VSP_040552, VSP_040553;
-!- 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.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF315683; AAG41981.1; -; mRNA.
EMBL; AF219624; AAK01480.1; -; mRNA.
EMBL; AF330002; AAK01706.1; -; mRNA.
EMBL; AY358987; AAQ89346.1; -; mRNA.
EMBL; AC006237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC015849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011774; AAH11774.1; -; mRNA.
CCDS; CCDS45651.1; -. [Q9H239-2]
CCDS; CCDS74036.1; -. [Q9H239-1]
RefSeq; NP_001027449.1; NM_001032278.2. [Q9H239-2]
RefSeq; NP_077278.1; NM_024302.4. [Q9H239-1]
RefSeq; NP_116568.1; NM_032950.3.
UniGene; Hs.380710; -.
ProteinModelPortal; Q9H239; -.
SMR; Q9H239; -.
BioGrid; 122566; 2.
STRING; 9606.ENSP00000250144; -.
DrugBank; DB00786; Marimastat.
MEROPS; M10.030; -.
iPTMnet; Q9H239; -.
PhosphoSitePlus; Q9H239; -.
BioMuta; MMP28; -.
DMDM; 37538314; -.
PaxDb; Q9H239; -.
PeptideAtlas; Q9H239; -.
PRIDE; Q9H239; -.
ProteomicsDB; 80485; -.
ProteomicsDB; 80486; -. [Q9H239-2]
DNASU; 79148; -.
Ensembl; ENST00000605424; ENSP00000473853; ENSG00000271447. [Q9H239-1]
Ensembl; ENST00000611911; ENSP00000484430; ENSG00000278843. [Q9H239-1]
Ensembl; ENST00000612672; ENSP00000483539; ENSG00000271447. [Q9H239-2]
Ensembl; ENST00000632360; ENSP00000488096; ENSG00000278843. [Q9H239-2]
GeneID; 79148; -.
KEGG; hsa:79148; -.
UCSC; uc002hka.4; human. [Q9H239-1]
CTD; 79148; -.
DisGeNET; 79148; -.
EuPathDB; HostDB:ENSG00000271447.5; -.
GeneCards; MMP28; -.
HGNC; HGNC:14366; MMP28.
MIM; 608417; gene.
neXtProt; NX_Q9H239; -.
OpenTargets; ENSG00000271447; -.
PharmGKB; PA30885; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00910000144034; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9H239; -.
KO; K08006; -.
OMA; YCHSSFD; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q9H239; -.
GeneWiki; MMP28; -.
GenomeRNAi; 79148; -.
PRO; PR:Q9H239; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000271447; -.
CleanEx; HS_MMP25; -.
CleanEx; HS_MMP28; -.
ExpressionAtlas; Q9H239; baseline and differential.
Genevisible; Q9H239; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028735; MMP28.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF16; PTHR10201:SF16; 1.
Pfam; PF00045; Hemopexin; 2.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 122 {ECO:0000250}.
/FTId=PRO_0000028857.
CHAIN 123 520 Matrix metalloproteinase-28.
/FTId=PRO_0000028858.
REPEAT 325 369 Hemopexin 1.
REPEAT 370 409 Hemopexin 2.
REPEAT 415 463 Hemopexin 3.
REPEAT 464 510 Hemopexin 4.
MOTIF 89 96 Cysteine switch. {ECO:0000250}.
ACT_SITE 241 241 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 91 91 Zinc; in inhibited form. {ECO:0000250}.
METAL 240 240 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 244 244 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 250 250 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 324 510 {ECO:0000250}.
VAR_SEQ 128 130 NKW -> EHC (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040552.
VAR_SEQ 131 520 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040553.
CONFLICT 487 487 R -> C (in Ref. 1; AAG41981).
{ECO:0000305}.
SEQUENCE 520 AA; 58939 MW; E85D7ADA3069B063 CRC64;
MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV PKAPTSTRFS
DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA AWAERISDLF ARHRTKMRRK
KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA VRGAVRAAFQ LWSNVSALEF WEAPATGPAD
IRLTFFQGDH NDGLGNAFDG PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH
EIGHTLGLTH SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF
TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV AADGNVSEPR
PLQERWVGLP PNIEAAAVSL NDGDFYFFKG GRCWRFRGPK PVWGLPQLCR AGGLPRHPDA
ALFFPPLRRL ILFKGARYYV LARGGLQVEP YYPRSLQDWG GIPEEVSGAL PRPDGSIIFF
RDDRYWRLDQ AKLQATTSGR WATELPWMGC WHANSGSALF


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