Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9H306 (MMP27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-27

Short name=MMP-27
EC=3.4.24.-
Gene names
Name:MMP27
ORF Names:UNQ2503/PRO5992
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Cofactor

Binds 4 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed in B-cells. Ref.4

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.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 9881Activation peptide By similarity
PRO_0000287561
Chain99 – 513415Matrix metalloproteinase-27
PRO_0000287562

Regions

Repeat276 – 32550Hemopexin 1
Repeat326 – 37146Hemopexin 2
Repeat373 – 42149Hemopexin 3
Repeat422 – 46544Hemopexin 4
Motif89 – 968Cysteine switch By similarity

Sites

Active site2171 By similarity
Metal binding911Zinc 2; in inhibited form By similarity
Metal binding1211Calcium 1 By similarity
Metal binding1551Calcium 2 By similarity
Metal binding1651Zinc 1 By similarity
Metal binding1731Calcium 3 By similarity
Metal binding1741Calcium 3; via carbonyl oxygen By similarity
Metal binding1781Calcium 3; via carbonyl oxygen By similarity
Metal binding1811Zinc 1 By similarity
Metal binding1881Calcium 2; via carbonyl oxygen By similarity
Metal binding1921Calcium 2 By similarity
Metal binding1941Zinc 1 By similarity
Metal binding1961Calcium 3 By similarity
Metal binding1991Calcium 1 By similarity
Metal binding1991Calcium 3 By similarity
Metal binding2161Zinc 2; catalytic By similarity
Metal binding2201Zinc 2; catalytic By similarity
Metal binding2261Zinc 2; catalytic By similarity
Metal binding2861Calcium 4; via carbonyl oxygen By similarity
Metal binding3771Calcium 4; via carbonyl oxygen By similarity
Metal binding4261Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Potential
Disulfide bond279 ↔ 465 By similarity

Natural variations

Natural variant221R → W.
Corresponds to variant rs12099177 [ dbSNP | Ensembl ].
VAR_032326
Natural variant241T → M. Ref.1
Corresponds to variant rs1939015 [ dbSNP | Ensembl ].
VAR_032327
Natural variant301M → V. Ref.1
Corresponds to variant rs2846707 [ dbSNP | Ensembl ].
VAR_032328
Natural variant2661E → V. Ref.2
Corresponds to variant rs1276286 [ dbSNP | Ensembl ].
VAR_032329
Natural variant3041W → L.
Corresponds to variant rs35616217 [ dbSNP | Ensembl ].
VAR_032330
Natural variant4471D → N. Ref.2
Corresponds to variant rs2509010 [ dbSNP | Ensembl ].
VAR_032331
Natural variant4771I → V.
Corresponds to variant rs35822551 [ dbSNP | Ensembl ].
VAR_032332

Sequences

Sequence LengthMass (Da)Tools
Q9H306 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 941D5B8DA55BD32A

FASTA51359,026
        10         20         30         40         50         60 
MKRLLLLFLF FITFSSAFPL VRMTENEENM QLAQAYLNQF YSLEIEGNHL VQSKNRSLID 

        70         80         90        100        110        120 
DKIREMQAFF GLTVTGKLDS NTLEIMKTPR CGVPDVGQYG YTLPGWRKYN LTYRIINYTP 

       130        140        150        160        170        180 
DMARAAVDEA IQEGLEVWSK VTPLKFTKIS KGIADIMIAF RTRVHGRCPR YFDGPLGVLG 

       190        200        210        220        230        240 
HAFPPGPGLG GDTHFDEDEN WTKDGAGFNL FLVAAHEFGH ALGLSHSNDQ TALMFPNYVS 

       250        260        270        280        290        300 
LDPRKYPLSQ DDINGIQSIY GGLPKEPAKP KEPTIPHACD PDLTFDAITT FRREVMFFKG 

       310        320        330        340        350        360 
RHLWRIYYDI TDVEFELIAS FWPSLPADLQ AAYENPRDKI LVFKDENFWM IRGYAVLPDY 

       370        380        390        400        410        420 
PKSIHTLGFP GRVKKIDAAV CDKTTRKTYF FVGIWCWRFD EMTQTMDKGF PQRVVKHFPG 

       430        440        450        460        470        480 
ISIRVDAAFQ YKGFFFFSRG SKQFEYDIKT KNITRIMRTN TWFQCKEPKN SSFGFDINKE 

       490        500        510 
KAHSGGIKIL YHKSLSLFIF GIVHLLKNTS IYQ 

« Hide

References

« Hide 'large scale' references
[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]"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. expand/collapse author list , 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], VARIANTS VAL-266 AND ASN-447.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF195192 mRNA. Translation: AAG28453.1.
AY358752 mRNA. Translation: AAQ89112.1.
AP000647 Genomic DNA. No translation available.
AP000851 Genomic DNA. No translation available.
RefSeqNP_071405.2. NM_022122.2.
UniGeneHs.534479.

3D structure databases

ProteinModelPortalQ9H306.
SMRQ9H306. Positions 30-465.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.027.

PTM databases

PhosphoSiteQ9H306.

Polymorphism databases

DMDM296437372.

Proteomic databases

PaxDbQ9H306.
PRIDEQ9H306.

Protocols and materials databases

DNASU64066.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260229; ENSP00000260229; ENSG00000137675.
GeneID64066.
KEGGhsa:64066.
UCSCuc001phd.1. human.

Organism-specific databases

CTD64066.
GeneCardsGC11M102596.
H-InvDBHIX0201706.
HGNCHGNC:14250. MMP27.
neXtProtNX_Q9H306.
PharmGKBPA30884.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260291.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ9H306.
KOK08005.
OMAQFYSLEI.
OrthoDBEOG7XPZ57.
PhylomeDBQ9H306.
TreeFamTF315428.

Gene expression databases

BgeeQ9H306.
CleanExHS_MMP27.
GenevestigatorQ9H306.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF39. PTHR10201:SF39. 1 hit.
PfamPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP27.
GenomeRNAi64066.
NextBio65838.
PROQ9H306.

Entry information

Entry nameMMP27_HUMAN
AccessionPrimary (citable) accession number: Q9H306
Secondary accession number(s): Q6UWK6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM