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

P24347 (MMP11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromelysin-3

Short name=SL-3
Short name=ST3
EC=3.4.24.-
Alternative name(s):
Matrix metalloproteinase-11
Short name=MMP-11
Gene names
Name:MMP11
Synonyms:STMY3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play an important role in the progression of epithelial malignancies.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Tissue specificity

Specifically expressed in stromal cells of breast carcinomas.

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

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
   PTMCleavage on pair of basic residues
Disulfide bond
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbasement membrane organization

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

multicellular organismal development

Traceable author statement Ref.6. Source: ProtInc

negative regulation of fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

proteolysis

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from direct assay PubMed 18622425. Source: MGI

extracellular region

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Traceable author statement Ref.6. Source: ProtInc

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 – 3131 Potential
Propeptide32 – 9766Activation peptide By similarity
PRO_0000028770
Chain98 – 488391Stromelysin-3
PRO_0000028771

Regions

Repeat291 – 33949Hemopexin 1
Repeat340 – 38243Hemopexin 2
Repeat384 – 43249Hemopexin 3
Repeat433 – 48048Hemopexin 4
Motif78 – 858Cysteine switch By similarity

Sites

Active site2161 By similarity
Metal binding801Zinc 2; in inhibited form By similarity
Metal binding1661Zinc 1 By similarity
Metal binding1711Calcium By similarity
Metal binding1721Calcium; via carbonyl oxygen By similarity
Metal binding1741Calcium; via carbonyl oxygen By similarity
Metal binding1761Calcium; via carbonyl oxygen By similarity
Metal binding1791Zinc 1 By similarity
Metal binding1921Zinc 1 By similarity
Metal binding2151Zinc 2; catalytic By similarity
Metal binding2191Zinc 2; catalytic By similarity
Metal binding2251Zinc 2; catalytic By similarity

Amino acid modifications

Disulfide bond294 ↔ 480 By similarity

Natural variations

Natural variant381A → V. Ref.1 Ref.2
Corresponds to variant rs738792 [ dbSNP | Ensembl ].
VAR_022181
Natural variant441E → K. Ref.2
Corresponds to variant rs28363646 [ dbSNP | Ensembl ].
VAR_022182
Natural variant611P → L. Ref.2
Corresponds to variant rs28363647 [ dbSNP | Ensembl ].
VAR_022183
Natural variant861S → P. Ref.2
Corresponds to variant rs28363648 [ dbSNP | Ensembl ].
VAR_022184
Natural variant1661D → N in a colorectal cancer sample; somatic mutation. Ref.7
VAR_036140
Natural variant1821F → S. Ref.4
Corresponds to variant rs17854940 [ dbSNP | Ensembl ].
VAR_029659

Sequences

Sequence LengthMass (Da)Tools
P24347 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: F03C537EE76706A9

FASTA48854,590
        10         20         30         40         50         60 
MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP WHAALPSSPA 

        70         80         90        100        110        120 
PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL SGGRWEKTDL TYRILRFPWQ 

       130        140        150        160        170        180 
LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA 

       190        200        210        220        230        240 
FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR 

       250        260        270        280        290        300 
YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA 

       310        320        330        340        350        360 
VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA 

       370        380        390        400        410        420 
QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS 

       430        440        450        460        470        480 
PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC 


AEPANTFL 

« Hide

References

« Hide 'large scale' references
[1]"A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas."
Basset P., Bellocq J.-P., Wolf C., Stoll I., Hutin P., Limacher J.-M., Podhajcer O.L., Chenard M.P., Rio M.C., Chambon P.
Nature 348:699-704(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-38.
[2]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-38; LYS-44; LEU-61 AND PRO-86.
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-182.
Tissue: Placenta.
[5]"Structure and promoter characterization of the human stromelysin-3 gene."
Anglard P., Melot T., Guerin E., Thomas G., Basset P.
J. Biol. Chem. 270:20337-20344(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
[6]"Furin-dependent intracellular activation of the human stromelysin-3 zymogen."
Pei D., Weiss S.J.
Nature 375:244-247(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-101.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-166.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57766 mRNA. Translation: CAA40918.1.
AY899208 Genomic DNA. Translation: AAW65373.1.
AP000349 Genomic DNA. No translation available.
BC057788 mRNA. Translation: AAH57788.1.
X84664 Genomic DNA. Translation: CAA59150.1.
PIRS13423.
RefSeqNP_005931.2. NM_005940.3.
UniGeneHs.143751.

3D structure databases

ProteinModelPortalP24347.
SMRP24347. Positions 48-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000215743.

Chemistry

BindingDBP24347.
ChEMBLCHEMBL2867.

Protein family/group databases

MEROPSM10.007.

PTM databases

PhosphoSiteP24347.

Polymorphism databases

DMDM317373418.

Proteomic databases

PaxDbP24347.
PRIDEP24347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215743; ENSP00000215743; ENSG00000099953.
GeneID4320.
KEGGhsa:4320.
UCSCuc002zxx.3. human.

Organism-specific databases

CTD4320.
GeneCardsGC22P024110.
H-InvDBHIX0203187.
HGNCHGNC:7157. MMP11.
HPACAB002593.
MIM185261. gene.
neXtProtNX_P24347.
PharmGKBPA30869.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236137.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidP24347.
KOK07993.
OMAVDTNEIA.
OrthoDBEOG7XPZ57.
PhylomeDBP24347.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP24347.
BgeeP24347.
CleanExHS_MMP11.
GenevestigatorP24347.

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.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR028705. Stromelysin-3.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. 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

GeneWikiMMP11.
GenomeRNAi4320.
NextBio16997.
PROP24347.
SOURCESearch...

Entry information

Entry nameMMP11_HUMAN
AccessionPrimary (citable) accession number: P24347
Secondary accession number(s): Q5FX24, Q6PEZ6, Q9UC26
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 148 of the entry and version 3 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 22

Human chromosome 22: entries, gene names and cross-references to MIM