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P24347

- MMP11_HUMAN

UniProt

P24347 - MMP11_HUMAN

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Protein

Stromelysin-3

Gene
MMP11, STMY3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Cofactori

Binds 1 calcium ion per subunit By similarity.
Binds 2 zinc ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 2; in inhibited form By similarity
Metal bindingi166 – 1661Zinc 1 By similarity
Metal bindingi171 – 1711Calcium By similarity
Metal bindingi172 – 1721Calcium; via carbonyl oxygen By similarity
Metal bindingi174 – 1741Calcium; via carbonyl oxygen By similarity
Metal bindingi176 – 1761Calcium; via carbonyl oxygen By similarity
Metal bindingi179 – 1791Zinc 1 By similarity
Metal bindingi192 – 1921Zinc 1 By similarity
Metal bindingi215 – 2151Zinc 2; catalytic By similarity
Active sitei216 – 2161 By similarity
Metal bindingi219 – 2191Zinc 2; catalytic By similarity
Metal bindingi225 – 2251Zinc 2; catalytic By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. basement membrane organization Source: Ensembl
  2. collagen catabolic process Source: Reactome
  3. collagen fibril organization Source: Ensembl
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. multicellular organismal development Source: ProtInc
  7. negative regulation of fat cell differentiation Source: Ensembl
  8. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-3 (EC:3.4.24.-)
Short name:
SL-3
Short name:
ST3
Alternative name(s):
Matrix metalloproteinase-11
Short name:
MMP-11
Gene namesi
Name:MMP11
Synonyms:STMY3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:7157. MMP11.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: MGI
  2. extracellular region Source: Reactome
  3. Golgi lumen Source: Reactome
  4. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed predictionAdd
BLAST
Propeptidei32 – 9766Activation peptide By similarityPRO_0000028770Add
BLAST
Chaini98 – 488391Stromelysin-3PRO_0000028771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi294 ↔ 480 By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiP24347.
PRIDEiP24347.

PTM databases

PhosphoSiteiP24347.

Expressioni

Tissue specificityi

Specifically expressed in stromal cells of breast carcinomas.

Gene expression databases

ArrayExpressiP24347.
BgeeiP24347.
CleanExiHS_MMP11.
GenevestigatoriP24347.

Organism-specific databases

HPAiCAB002593.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000215743.

Structurei

3D structure databases

ProteinModelPortaliP24347.
SMRiP24347. Positions 75-460.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati291 – 33949Hemopexin 1Add
BLAST
Repeati340 – 38243Hemopexin 2Add
BLAST
Repeati384 – 43249Hemopexin 3Add
BLAST
Repeati433 – 48048Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 858Cysteine switch By 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.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG236137.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP24347.
KOiK07993.
OMAiVDTNEIA.
OrthoDBiEOG7XPZ57.
PhylomeDBiP24347.
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.
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]
PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF50923. 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.

P24347-1 [UniParc]FASTAAdd to Basket

« Hide

MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP    50
WHAALPSSPA PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL 100
SGGRWEKTDL TYRILRFPWQ LVQEQVRQTM AEALKVWSDV TPLTFTEVHE 150
GRADIMIDFA RYWHGDDLPF DGPGGILAHA FFPKTHREGD VHFDYDETWT 200
IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR YPLSLSPDDC 250
RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA 300
VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA 350
QGHIWFFQGA QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI 400
YFFRGRDYWR FHPSTRRVDS PVPRRATDWR GVPSEIDAAF QDADGYAYFL 450
RGRLYWKFDP VKVKALEGFP RLVGPDFFGC AEPANTFL 488
Length:488
Mass (Da):54,590
Last modified:January 11, 2011 - v3
Checksum:iF03C537EE76706A9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381A → V.2 Publications
Corresponds to variant rs738792 [ dbSNP | Ensembl ].
VAR_022181
Natural varianti44 – 441E → K.1 Publication
Corresponds to variant rs28363646 [ dbSNP | Ensembl ].
VAR_022182
Natural varianti61 – 611P → L.1 Publication
Corresponds to variant rs28363647 [ dbSNP | Ensembl ].
VAR_022183
Natural varianti86 – 861S → P.1 Publication
Corresponds to variant rs28363648 [ dbSNP | Ensembl ].
VAR_022184
Natural varianti166 – 1661D → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036140
Natural varianti182 – 1821F → S.1 Publication
Corresponds to variant rs17854940 [ dbSNP | Ensembl ].
VAR_029659

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13816.1.
PIRiS13423.
RefSeqiNP_005931.2. NM_005940.3.
UniGeneiHs.143751.

Genome annotation databases

EnsembliENST00000215743; ENSP00000215743; ENSG00000099953.
GeneIDi4320.
KEGGihsa:4320.
UCSCiuc002zxx.3. human.

Polymorphism databases

DMDMi317373418.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13816.1.
PIRi S13423.
RefSeqi NP_005931.2. NM_005940.3.
UniGenei Hs.143751.

3D structure databases

ProteinModelPortali P24347.
SMRi P24347. Positions 75-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000215743.

Chemistry

BindingDBi P24347.
ChEMBLi CHEMBL2867.

Protein family/group databases

MEROPSi M10.007.

PTM databases

PhosphoSitei P24347.

Polymorphism databases

DMDMi 317373418.

Proteomic databases

PaxDbi P24347.
PRIDEi P24347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215743 ; ENSP00000215743 ; ENSG00000099953 .
GeneIDi 4320.
KEGGi hsa:4320.
UCSCi uc002zxx.3. human.

Organism-specific databases

CTDi 4320.
GeneCardsi GC22P024110.
H-InvDB HIX0203187.
HGNCi HGNC:7157. MMP11.
HPAi CAB002593.
MIMi 185261. gene.
neXtProti NX_P24347.
PharmGKBi PA30869.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236137.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P24347.
KOi K07993.
OMAi VDTNEIA.
OrthoDBi EOG7XPZ57.
PhylomeDBi P24347.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Miscellaneous databases

GeneWikii MMP11.
GenomeRNAii 4320.
NextBioi 16997.
PROi P24347.
SOURCEi Search...

Gene expression databases

ArrayExpressi P24347.
Bgeei P24347.
CleanExi HS_MMP11.
Genevestigatori P24347.

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.
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 ]
PANTHERi PTHR10201:SF20. PTHR10201:SF20. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 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 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. "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.
    , 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-166.

Entry informationi

Entry nameiMMP11_HUMAN
AccessioniPrimary (citable) accession number: P24347
Secondary accession number(s): Q5FX24, Q6PEZ6, Q9UC26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 151 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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