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Q9H306

- MMP27_HUMAN

UniProt

Q9H306 - MMP27_HUMAN

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Protein

Matrix metalloproteinase-27

Gene

MMP27

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Ca(2+) ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Zinc 2; in inhibited formBy similarity
Metal bindingi121 – 1211Calcium 1By similarity
Metal bindingi155 – 1551Calcium 2By similarity
Metal bindingi165 – 1651Zinc 1By similarity
Metal bindingi173 – 1731Calcium 3By similarity
Metal bindingi174 – 1741Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi181 – 1811Zinc 1By similarity
Metal bindingi188 – 1881Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium 2By similarity
Metal bindingi194 – 1941Zinc 1By similarity
Metal bindingi196 – 1961Calcium 3By similarity
Metal bindingi199 – 1991Calcium 1By similarity
Metal bindingi199 – 1991Calcium 3By similarity
Metal bindingi216 – 2161Zinc 2; catalyticBy similarity
Active sitei217 – 2171PROSITE-ProRule annotation
Metal bindingi220 – 2201Zinc 2; catalyticBy similarity
Metal bindingi226 – 2261Zinc 2; catalyticBy similarity
Metal bindingi286 – 2861Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi377 – 3771Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi426 – 4261Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14250. MMP27.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein 1 Publication
Note: Retained in the endoplasmic reticulum.1 Publication

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551N → Q: Loss of N-glycosylation; when associated with Q-110 and Q-452. 1 Publication
Mutagenesisi110 – 1101N → Q: Loss of N-glycosylation; when associated with Q-55 and Q-452. 1 Publication
Mutagenesisi452 – 4521N → Q: Loss of N-glycosylation; when associated with Q-55 and Q-110. 1 Publication

Organism-specific databases

PharmGKBiPA30884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 9881Activation peptideBy similarityPRO_0000287561Add
BLAST
Chaini99 – 513415Matrix metalloproteinase-27PRO_0000287562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)1 Publication
Glycosylationi110 – 1101N-linked (GlcNAc...)1 PublicationSequence Analysis
Disulfide bondi279 ↔ 465By similarity
Glycosylationi452 – 4521N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9H306.
PRIDEiQ9H306.

PTM databases

PhosphoSiteiQ9H306.

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

BgeeiQ9H306.
CleanExiHS_MMP27.
GenevestigatoriQ9H306.

Interactioni

Protein-protein interaction databases

BioGridi122039. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9H306.
SMRiQ9H306. Positions 30-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati276 – 32550Hemopexin 1Add
BLAST
Repeati326 – 37146Hemopexin 2Add
BLAST
Repeati373 – 42149Hemopexin 3Add
BLAST
Repeati422 – 46544Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni466 – 51348Required for retention in the endoplasmic reticulum1 PublicationAdd
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

eggNOGiNOG260291.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ9H306.
KOiK08005.
OMAiQFYSLEI.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ9H306.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221R → W.
Corresponds to variant rs12099177 [ dbSNP | Ensembl ].
VAR_032326
Natural varianti24 – 241T → M.1 Publication
Corresponds to variant rs1939015 [ dbSNP | Ensembl ].
VAR_032327
Natural varianti30 – 301M → V.1 Publication
Corresponds to variant rs2846707 [ dbSNP | Ensembl ].
VAR_032328
Natural varianti266 – 2661E → V.1 Publication
Corresponds to variant rs1276286 [ dbSNP | Ensembl ].
VAR_032329
Natural varianti304 – 3041W → L.
Corresponds to variant rs35616217 [ dbSNP | Ensembl ].
VAR_032330
Natural varianti447 – 4471D → N.1 Publication
Corresponds to variant rs2509010 [ dbSNP | Ensembl ].
VAR_032331
Natural varianti477 – 4771I → V.
Corresponds to variant rs35822551 [ dbSNP | Ensembl ].
VAR_032332

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.1. human.

Polymorphism databases

DMDMi296437372.

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.
CCDSi CCDS8319.1.
RefSeqi NP_071405.2. NM_022122.2.
UniGenei Hs.534479.

3D structure databases

ProteinModelPortali Q9H306.
SMRi Q9H306. Positions 30-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122039. 1 interaction.

Chemistry

DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.027.

PTM databases

PhosphoSitei Q9H306.

Polymorphism databases

DMDMi 296437372.

Proteomic databases

PaxDbi Q9H306.
PRIDEi Q9H306.

Protocols and materials databases

DNASUi 64066.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260229 ; ENSP00000260229 ; ENSG00000137675 .
GeneIDi 64066.
KEGGi hsa:64066.
UCSCi uc001phd.1. human.

Organism-specific databases

CTDi 64066.
GeneCardsi GC11M102596.
H-InvDB HIX0201706.
HGNCi HGNC:14250. MMP27.
neXtProti NX_Q9H306.
PharmGKBi PA30884.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG260291.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi Q9H306.
KOi K08005.
OMAi QFYSLEI.
OrthoDBi EOG7XPZ57.
PhylomeDBi Q9H306.
TreeFami TF315428.

Miscellaneous databases

GeneWikii MMP27.
GenomeRNAii 64066.
NextBioi 65838.
PROi Q9H306.

Gene expression databases

Bgeei Q9H306.
CleanExi HS_MMP27.
Genevestigatori Q9H306.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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 ]
PANTHERi PTHR10201:SF115. PTHR10201:SF115. 1 hit.
Pfami PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel matrix metalloproteinase homologous to stromelysins."
    Benoit de Coignac A., Elson G., Magistrelli G., Jeannin P., Delneste Y., Aubry J.-P., Berthier O., Bonnefoy J.-Y., Gauchat J.-F.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-24 AND VAL-30.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-266 AND ASN-447.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis."
    Bar-Or A., Nuttall R.K., Duddy M., Alter A., Kim H.J., Ifergan I., Pennington C.J., Bourgoin P., Edwards D.R., Yong V.W.
    Brain 126:2738-2749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Matrix metalloproteinase-27 is expressed in CD163+/CD206+ M2 macrophages in the cycling human endometrium and in superficial endometriotic lesions."
    Cominelli A., Gaide Chevronnay H.P., Lemoine P., Courtoy P.J., Marbaix E., Henriet P.
    Mol. Hum. Reprod. 20:767-775(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum."
    Cominelli A., Halbout M., N'Kuli F., Lemoine P., Courtoy P.J., Marbaix E., Tyteca D., Henriet P.
    Traffic 15:401-417(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-55; ASN-110 AND ASN-452, TOPOLOGY, REGION, MUTAGENESIS OF ASN-55; ASN-110 AND ASN-452.

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 26, 2014
This is version 106 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

External Data

Dasty 3