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Reviewed, UniProtKB/Swiss-Prot Q5RES1 (MMP14_PONAB)

Last modified January 19, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Matrix metalloproteinase-14
      Short name=MMP-14
    EC=3.4.24.80
Gene names
Name: MMP14
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface By similarity.

Catalytic activity

Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Melanosome By similarity.

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-like domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 11191Activation peptide
PRO_0000330604
Chain112 – 582471Matrix metalloproteinase-14
PRO_0000330605

Regions

Topological domain112 – 541430Extracellular Potential
Transmembrane542 – 56221 Potential
Topological domain563 – 58220Cytoplasmic Potential
Domain323 – 36644Hemopexin-like 1
Domain368 – 41245Hemopexin-like 2
Domain415 – 46147Hemopexin-like 3
Domain463 – 50846Hemopexin-like 4
Motif91 – 988Cysteine switch By similarity

Sites

Active site2401 By similarity
Metal binding931Zinc; in inhibited form By similarity
Metal binding2391Zinc; catalytic
Metal binding2431Zinc; catalytic
Metal binding2491Zinc; catalytic

Amino acid modifications

Disulfide bond319 ↔ 508 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5RES1-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9CC4480F6DEE9003

FASTA58265,832
        10         20         30         40         50         60 
MSPAPRPSRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQK FYGLRVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADVMIF 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVGNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPEDDRRGIQ QLYGSESGFP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPK NPTYGPNTCD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFDNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV

« Hide

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857445 mRNA. Translation: CAH89736.1.
RefSeqNP_001124793.1.
UniGenePab.12271

3D structure databases

HSSPHSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMRQ5RES1. Positions 114-287, 316-508.
ModBaseSearch...

Protein family/group databases

MEROPSM10.014.

Genome annotation databases

GeneID100171646.

Organism-specific databases

CTD100171646.

Phylogenomic databases

HOVERGENQ5RES1.
InParanoidQ5RES1.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR001818. Pept_M10A_M12B.
IPR016293. Pept_M10A_matrix.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 1 hit.
PfamPF00045. Hemopexin. 4 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]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit. Uncertain.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMMP14_PONAB
AccessionPrimary (citable) accession number: Q5RES1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents