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Protein

Matrix metalloproteinase-27

Gene

MMP27

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

Functioni

Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi91Zinc 2; in inhibited formBy similarity1
Metal bindingi121Calcium 1By similarity1
Metal bindingi155Calcium 2By similarity1
Metal bindingi165Zinc 1By similarity1
Metal bindingi173Calcium 3By similarity1
Metal bindingi174Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi178Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi181Zinc 1By similarity1
Metal bindingi188Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi192Calcium 2By similarity1
Metal bindingi194Zinc 1By similarity1
Metal bindingi196Calcium 3By similarity1
Metal bindingi199Calcium 1By similarity1
Metal bindingi199Calcium 3By similarity1
Metal bindingi216Zinc 2; catalyticBy similarity1
Active sitei217PROSITE-ProRule annotation1
Metal bindingi220Zinc 2; catalyticBy similarity1
Metal bindingi226Zinc 2; catalyticBy similarity1
Metal bindingi286Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi377Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi426Calcium 4; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137675-MONOMER.

Protein family/group databases

MEROPSiM10.027.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-27 (EC:3.4.24.-)
Short name:
MMP-27
Gene namesi
Name:MMP27
ORF Names:UNQ2503/PRO5992
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:14250. MMP27.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: InterPro
  • extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi55N → Q: Loss of N-glycosylation; when associated with Q-110 and Q-452. 1 Publication1
Mutagenesisi110N → Q: Loss of N-glycosylation; when associated with Q-55 and Q-452. 1 Publication1
Mutagenesisi452N → Q: Loss of N-glycosylation; when associated with Q-55 and Q-110. 1 Publication1

Organism-specific databases

OpenTargetsiENSG00000137675.
PharmGKBiPA30884.

Chemistry databases

DrugBankiDB00786. Marimastat.

Polymorphism and mutation databases

BioMutaiMMP27.
DMDMi296437372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000028756118 – 98Activation peptideBy similarityAdd BLAST81
ChainiPRO_000028756299 – 513Matrix metalloproteinase-27Add BLAST415

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi55N-linked (GlcNAc...)1 Publication1
Glycosylationi110N-linked (GlcNAc...)Sequence analysis1 Publication1
Disulfide bondi279 ↔ 465By similarity
Glycosylationi452N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9H306.
PeptideAtlasiQ9H306.
PRIDEiQ9H306.

PTM databases

iPTMnetiQ9H306.
PhosphoSitePlusiQ9H306.

Expressioni

Tissue specificityi

Expressed in B-cells (PubMed:14506071). Expressed in a subset of endometrial macrophages related to menstruation and in ovarian and peritoneal endometriotic lesions (at protein level)(PubMed:24810263).2 Publications

Gene expression databases

BgeeiENSG00000137675.
CleanExiHS_MMP27.
GenevisibleiQ9H306. HS.

Organism-specific databases

HPAiHPA069097.

Interactioni

Protein-protein interaction databases

BioGridi122039. 1 interactor.
STRINGi9606.ENSP00000260229.

Structurei

3D structure databases

ProteinModelPortaliQ9H306.
SMRiQ9H306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati276 – 325Hemopexin 1Add BLAST50
Repeati326 – 371Hemopexin 2Add BLAST46
Repeati373 – 421Hemopexin 3Add BLAST49
Repeati422 – 465Hemopexin 4Add BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni466 – 513Required for retention in the endoplasmic reticulum1 PublicationAdd BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi89 – 96Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9H306.
KOiK08005.
OMAiPHACDPD.
OrthoDBiEOG091G03DP.
PhylomeDBiQ9H306.
TreeFamiTF315428.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028732. MMP27.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF115. PTHR10201:SF115. 1 hit.
PfamiPF00045. Hemopexin. 3 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.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRLLLLFLF FITFSSAFPL VRMTENEENM QLAQAYLNQF YSLEIEGNHL
60 70 80 90 100
VQSKNRSLID DKIREMQAFF GLTVTGKLDS NTLEIMKTPR CGVPDVGQYG
110 120 130 140 150
YTLPGWRKYN LTYRIINYTP DMARAAVDEA IQEGLEVWSK VTPLKFTKIS
160 170 180 190 200
KGIADIMIAF RTRVHGRCPR YFDGPLGVLG HAFPPGPGLG GDTHFDEDEN
210 220 230 240 250
WTKDGAGFNL FLVAAHEFGH ALGLSHSNDQ TALMFPNYVS LDPRKYPLSQ
260 270 280 290 300
DDINGIQSIY GGLPKEPAKP KEPTIPHACD PDLTFDAITT FRREVMFFKG
310 320 330 340 350
RHLWRIYYDI TDVEFELIAS FWPSLPADLQ AAYENPRDKI LVFKDENFWM
360 370 380 390 400
IRGYAVLPDY PKSIHTLGFP GRVKKIDAAV CDKTTRKTYF FVGIWCWRFD
410 420 430 440 450
EMTQTMDKGF PQRVVKHFPG ISIRVDAAFQ YKGFFFFSRG SKQFEYDIKT
460 470 480 490 500
KNITRIMRTN TWFQCKEPKN SSFGFDINKE KAHSGGIKIL YHKSLSLFIF
510
GIVHLLKNTS IYQ
Length:513
Mass (Da):59,026
Last modified:May 18, 2010 - v2
Checksum:i941D5B8DA55BD32A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03232622R → W.Corresponds to variant rs12099177dbSNPEnsembl.1
Natural variantiVAR_03232724T → M.1 PublicationCorresponds to variant rs1939015dbSNPEnsembl.1
Natural variantiVAR_03232830M → V.1 PublicationCorresponds to variant rs2846707dbSNPEnsembl.1
Natural variantiVAR_032329266E → V.1 PublicationCorresponds to variant rs1276286dbSNPEnsembl.1
Natural variantiVAR_032330304W → L.Corresponds to variant rs35616217dbSNPEnsembl.1
Natural variantiVAR_032331447D → N.1 PublicationCorresponds to variant rs2509010dbSNPEnsembl.1
Natural variantiVAR_032332477I → V.Corresponds to variant rs35822551dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195192 mRNA. Translation: AAG28453.1.
AY358752 mRNA. Translation: AAQ89112.1.
AP000647 Genomic DNA. No translation available.
AP000851 Genomic DNA. No translation available.
CCDSiCCDS8319.1.
RefSeqiNP_071405.2. NM_022122.2.
UniGeneiHs.534479.

Genome annotation databases

EnsembliENST00000260229; ENSP00000260229; ENSG00000137675.
GeneIDi64066.
KEGGihsa:64066.
UCSCiuc001phd.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195192 mRNA. Translation: AAG28453.1.
AY358752 mRNA. Translation: AAQ89112.1.
AP000647 Genomic DNA. No translation available.
AP000851 Genomic DNA. No translation available.
CCDSiCCDS8319.1.
RefSeqiNP_071405.2. NM_022122.2.
UniGeneiHs.534479.

3D structure databases

ProteinModelPortaliQ9H306.
SMRiQ9H306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122039. 1 interactor.
STRINGi9606.ENSP00000260229.

Chemistry databases

DrugBankiDB00786. Marimastat.

Protein family/group databases

MEROPSiM10.027.

PTM databases

iPTMnetiQ9H306.
PhosphoSitePlusiQ9H306.

Polymorphism and mutation databases

BioMutaiMMP27.
DMDMi296437372.

Proteomic databases

PaxDbiQ9H306.
PeptideAtlasiQ9H306.
PRIDEiQ9H306.

Protocols and materials databases

DNASUi64066.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260229; ENSP00000260229; ENSG00000137675.
GeneIDi64066.
KEGGihsa:64066.
UCSCiuc001phd.2. human.

Organism-specific databases

CTDi64066.
GeneCardsiMMP27.
H-InvDBHIX0201706.
HGNCiHGNC:14250. MMP27.
HPAiHPA069097.
neXtProtiNX_Q9H306.
OpenTargetsiENSG00000137675.
PharmGKBiPA30884.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9H306.
KOiK08005.
OMAiPHACDPD.
OrthoDBiEOG091G03DP.
PhylomeDBiQ9H306.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137675-MONOMER.

Miscellaneous databases

GeneWikiiMMP27.
GenomeRNAii64066.
PROiQ9H306.

Gene expression databases

BgeeiENSG00000137675.
CleanExiHS_MMP27.
GenevisibleiQ9H306. HS.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR028732. MMP27.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF115. PTHR10201:SF115. 1 hit.
PfamiPF00045. Hemopexin. 3 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.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP27_HUMAN
AccessioniPrimary (citable) accession number: Q9H306
Secondary accession number(s): Q6UWK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 120 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.