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P08254 (MMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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-1

Short name=SL-1
EC=3.4.24.17
Alternative name(s):
Matrix metalloproteinase-3
Short name=MMP-3
Transin-1
Gene names
Name:MMP3
Synonyms:STMY1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

Catalytic activity

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

Cofactor

Binds 4 calcium ions per subunit.

Binds 2 zinc ions per subunit.

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

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. Ref.13

Involvement in disease

Coronary heart disease 6 (CHDS6) [MIM:614466]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions. Ref.11 Ref.12

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Probable
Propeptide18 – 9982Activation peptide
PRO_0000028728
Chain100 – 477378Stromelysin-1
PRO_0000028729

Regions

Repeat287 – 33650Hemopexin 1
Repeat337 – 38347Hemopexin 2
Repeat385 – 43349Hemopexin 3
Repeat434 – 47744Hemopexin 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191
Metal binding921Zinc 2; in inhibited form
Metal binding1241Calcium 1
Metal binding1581Calcium 2
Metal binding1681Zinc 1
Metal binding1701Zinc 1
Metal binding1751Calcium 3
Metal binding1761Calcium 3; via carbonyl oxygen
Metal binding1781Calcium 3; via carbonyl oxygen
Metal binding1801Calcium 3; via carbonyl oxygen
Metal binding1831Zinc 1
Metal binding1901Calcium 2; via carbonyl oxygen
Metal binding1921Calcium 2; via carbonyl oxygen
Metal binding1941Calcium 2
Metal binding1961Zinc 1
Metal binding1981Calcium 3
Metal binding1991Calcium 1
Metal binding2011Calcium 1
Metal binding2011Calcium 3
Metal binding2181Zinc 2; catalytic Ref.16
Metal binding2221Zinc 2; catalytic Ref.16
Metal binding2281Zinc 2; catalytic Ref.16
Metal binding2971Calcium 4; via carbonyl oxygen By similarity
Metal binding3891Calcium 4; via carbonyl oxygen By similarity
Metal binding4381Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Disulfide bond290 ↔ 477 By similarity

Natural variations

Natural variant451K → E. Ref.6 Ref.7 Ref.9
Corresponds to variant rs679620 [ dbSNP | Ensembl ].
VAR_013090

Experimental info

Sequence conflict4201P → L Ref.3

Secondary structure

................................................. 477
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08254 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 96194833B907668D

FASTA47753,977
        10         20         30         40         50         60 
MKSLPILLLL CVAVCSAYPL DGAARGEDTS MNLVQKYLEN YYDLKKDVKQ FVRRKDSGPV 

        70         80         90        100        110        120 
VKKIREMQKF LGLEVTGKLD SDTLEVMRKP RCGVPDVGHF RTFPGIPKWR KTHLTYRIVN 

       130        140        150        160        170        180 
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV 

       190        200        210        220        230        240 
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY 

       250        260        270        280        290        300 
HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ETPLVPTEPV PPEPGTPANC DPALSFDAVS 

       310        320        330        340        350        360 
TLRGEILIFK DRHFWRKSLR KLEPELHLIS SFWPSLPSGV DAAYEVTSKD LVFIFKGNQF 

       370        380        390        400        410        420 
WAIRGNEVRA GYPRGIHTLG FPPTVRKIDA AISDKEKNKT YFFVEDKYWR FDEKRNSMEP 

       430        440        450        460        470 
GFPKQIAEDF PGIDSKIDAV FEEFGFFYFF TGSSQLEFDP NAKKVTHTLK SNSWLNC 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin."
Saus J., Quinones S., Otani Y., Nagase H., Harris E.D. Jr., Kurkinen M.
J. Biol. Chem. 263:6742-6745(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-24.
[2]"Comparison of human stromelysin and collagenase by cloning and sequence analysis."
Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A., Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.
Biochem. J. 240:913-916(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[3]"Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells."
Wilhelm S.M., Collier I.E., Kronberger A., Eisen A.Z., Marmer B.L., Grant G.A., Bauer E.A., Goldberg G.I.
Proc. Natl. Acad. Sci. U.S.A. 84:6725-6729(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Three matrix metalloproteinases on 81kb of P1 insert."
Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A., Chung E., Davis K., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lashkari D., Lew H., Namath A., Oefner P., Roberts D., Heller R., Davis R.W.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovium.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-45.
Tissue: Synovium.
[7]SeattleSNPs variation discovery resource
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-45.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 GLU-45.
Tissue: Lung.
[10]"Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate."
Nagase H., Enghild J.J., Suzuki K., Salvesen G.
Biochemistry 29:5783-5789(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ZYMOGEN ACTIVATION.
[11]"Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin-1 promoter which results in reduced gene expression."
Ye S., Eriksson P., Hamsten A., Kurkinen M., Humphries S.E., Henney A.M.
J. Biol. Chem. 271:13055-13060(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHDS6.
[12]"Prediction of the risk of myocardial infarction from polymorphisms in candidate genes."
Yamada Y., Izawa H., Ichihara S., Takatsu F., Ishihara H., Hirayama H., Sone T., Tanaka M., Yokota M.
N. Engl. J. Med. 347:1916-1923(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CHDS6.
[13]"The NMR structure of the inhibited catalytic domain of human stromelysin-1."
Gooley P.R., O'Connell J.F., Marcy A.I., Cuca G.C., Salowe S.P., Bush B.L., Hermes J.D., Esser C.K., Hagmann W.K., Springer J.P., Johnson B.A.
Nat. Struct. Biol. 1:111-118(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF CATALYTIC DOMAIN.
[14]"Solution structures of stromelysin complexed to thiadiazole inhibitors."
Stockman B.J., Waldon D.J., Gates J.A., Scahill T.A., Kloosterman D.A., Mizsak S.A., Jacobsen E.J., Belonga K.L., Mitchell M.A., Mao B., Petke J.D., Goodman L., Powers E.A., Ledbetter S.R., Kaytes P.S., Vogeli G., Marshall V.P., Petzold G.L., Poorman R.A.
Protein Sci. 7:2281-2286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 100-267.
[15]"Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme."
Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M.D., Cameron P.M., Esser C.K., Hagmann W.K., Hermes J.D., Springer J.P.
Protein Sci. 4:1966-1976(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 18-272.
[16]"X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily."
Dhanaraj V., Ye Q.-Z., Johnson L.L., Hupe D.J., Otwine D.F., Dunbar J.B. Jr., Rubin J.R., Pavlovsky A., Humblet C., Blundell T.L.
Structure 4:375-386(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-266.
[17]"Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl carboxyalkyl dipeptides."
Esser C.K., Bugianesi R.L., Caldwell C.G., Chapman K.T., Durette P.L., Girotra N.N., Kopka I.E., Lanza T.J., Levorse D.A., Maccoss M., Owens K.A., Ponpipom M.M., Simeone J.P., Harrison R.K., Niedzwiecki L., Becker J.W., Marcy A.I., Axel M.G. expand/collapse author list , Christen A.J., McDonnell J., Moore V.L., Olszewski J.M., Saphos C., Visco D.M., Shen F., Colletti A., Kriter P.A., Hagmann W.K.
J. Med. Chem. 40:1026-1040(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 105-264.
[18]"Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1."
Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R., Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P., Bartunik H., Bode W.
Nature 389:77-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 100-267 IN COMPLEX WITH TIMP1.
[19]"Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity."
Finzel B.C., Baldwin E.T., Bryant G.L. Jr., Hess G.F., Wilks J.W., Trepod C.M., Mott J.E., Marshall V.P., Petzold G.L., Poorman R.A., O'Sullivan T.J., Schostarez H.J., Mitchell M.A.
Protein Sci. 7:2118-2126(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-264.
[20]"Crystal structure of the stromelysin catalytic domain at 2.0-A resolution: inhibitor-induced conformational changes."
Chen L., Rydel T.J., Gu F., Dunaway C.M., Pikul S., Dunham K.M., Barnett B.L.
J. Mol. Biol. 293:545-557(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-272.
[21]"X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity."
Pavlovsky A.G., Williams M.G., Ye Q.-Z., Ortwine D.F., Purchase C.F. II, White A.D., Dhanaraj V., Roth B.D., Johnson L.L., Hupe D., Humblet C., Blundell T.L.
Protein Sci. 8:1455-1462(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 100-267.
[22]"Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor."
Li Y.C., Zhang X., Melton R., Ganu V., Gonnella N.C.
Biochemistry 37:14048-14056(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 100-272.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05232 mRNA. Translation: CAA28859.1.
J03209 mRNA. Translation: AAA36321.1.
U78045 Genomic DNA. Translation: AAB36942.1.
AK223283 mRNA. Translation: BAD97003.1.
AK223291 mRNA. Translation: BAD97011.1.
AK313310 mRNA. Translation: BAG36115.1.
AF405705 Genomic DNA. Translation: AAK95247.1.
CH471065 Genomic DNA. Translation: EAW67032.1.
BC069676 mRNA. Translation: AAH69676.1.
BC069716 mRNA. Translation: AAH69716.1.
BC074815 mRNA. Translation: AAH74815.1.
BC074869 mRNA. Translation: AAH74869.1.
BC105954 mRNA. Translation: AAI05955.1.
BC107490 mRNA. Translation: AAI07491.1.
BC107491 mRNA. Translation: AAI07492.1.
PIRKCHUS1. A28156.
RefSeqNP_002413.1. NM_002422.3.
UniGeneHs.375129.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3DX-ray2.30A/B100-272[»]
1B8YX-ray2.00A100-266[»]
1BIWX-ray2.50A/B100-272[»]
1BM6NMR-A100-272[»]
1BQOX-ray2.30A/B100-272[»]
1C3IX-ray1.83A/B100-272[»]
1C8TX-ray2.60A/B103-268[»]
1CAQX-ray1.80A100-267[»]
1CIZX-ray1.64A100-267[»]
1CQRX-ray2.00A/B100-272[»]
1D5JX-ray2.60A/B100-272[»]
1D7XX-ray2.00A/B100-272[»]
1D8FX-ray2.40A/B100-272[»]
1D8MX-ray2.44A/B100-272[»]
1G05X-ray2.45A/B100-272[»]
1G49X-ray1.90A/B100-272[»]
1G4KX-ray2.00A/B/C100-267[»]
1HFSX-ray1.70A105-264[»]
1HY7X-ray1.50A/B100-272[»]
1M1Wmodel-A100-268[»]
1OO9NMR-A100-267[»]
1QIAX-ray2.00A/B/C/D106-267[»]
1QICX-ray2.00A/B/C/D106-266[»]
1SLMX-ray1.90A18-272[»]
1SLNX-ray2.27A100-272[»]
1UEAX-ray2.80A/C100-272[»]
1UMSNMR-A100-273[»]
1UMTNMR-A100-273[»]
1USNX-ray1.80A100-264[»]
2D1OX-ray2.02A/B100-270[»]
2JNPNMR-A105-265[»]
2JT5NMR-A105-265[»]
2JT6NMR-A105-265[»]
2SRTNMR-A100-272[»]
2USNX-ray2.20A100-264[»]
3OHLX-ray2.36A100-266[»]
3OHOX-ray2.50A100-268[»]
3USNNMR-A100-267[»]
4DPEX-ray1.96A/B100-272[»]
4G9LX-ray1.88A/B100-272[»]
4JA1X-ray1.96A/B100-272[»]
ProteinModelPortalP08254.
SMRP08254. Positions 32-477.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110458. 3 interactions.
MINTMINT-269333.
STRING9606.ENSP00000299855.

Chemistry

BindingDBP08254.
ChEMBLCHEMBL2111321.
DrugBankDB00786. Marimastat.
DB00641. Simvastatin.
GuidetoPHARMACOLOGY1630.

Protein family/group databases

MEROPSM10.005.

PTM databases

PhosphoSiteP08254.

Polymorphism databases

DMDM116857.

Proteomic databases

PaxDbP08254.
PRIDEP08254.

Protocols and materials databases

DNASU4314.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299855; ENSP00000299855; ENSG00000149968.
ENST00000572537; ENSP00000458496; ENSG00000263313.
GeneID4314.
KEGGhsa:4314.
UCSCuc001phj.1. human.

Organism-specific databases

CTD4314.
GeneCardsGC11M102706.
HGNCHGNC:7173. MMP3.
HPACAB016139.
HPA007875.
MIM185250. gene.
614466. phenotype.
neXtProtNX_P08254.
PharmGKBPA30886.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258253.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidP08254.
KOK01394.
OMAVAVCSAY.
PhylomeDBP08254.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP08254.
BgeeP08254.
CleanExHS_MMP3.
GenevestigatorP08254.

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.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1/2.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF38. PTHR10201:SF38. 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]
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

ChiTaRSMMP3. human.
EvolutionaryTraceP08254.
GeneWikiMMP3.
GenomeRNAi4314.
NextBio16977.
PMAP-CutDBP08254.
PROP08254.
SOURCESearch...

Entry information

Entry nameMMP3_HUMAN
AccessionPrimary (citable) accession number: P08254
Secondary accession number(s): B2R8B8, Q3B7S0, Q6GRF8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: April 16, 2014
This is version 162 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 11

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