P08254 (MMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix disassembly Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.1. Source: ProtInc regulation of cell migration Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement Ref.1. Source: ProtInc intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Probable

Propeptide

18 – 99

82

Activation peptide

PRO_0000028728

Chain

100 – 477

378

Stromelysin-1

PRO_0000028729

Regions

Domain

296 – 338

43

Hemopexin-like 1

Domain

340 – 383

44

Hemopexin-like 2

Domain

388 – 435

48

Hemopexin-like 3

Domain

437 – 477

41

Hemopexin-like 4

Motif

90 – 97

8

Cysteine switch By similarity

Sites

Active site

219

1

Metal binding

92

1

Zinc 2; in inhibited form

Metal binding

124

1

Calcium 1

Metal binding

158

1

Calcium 2

Metal binding

168

1

Zinc 1

Metal binding

170

1

Zinc 1

Metal binding

175

1

Calcium 3

Metal binding

176

1

Calcium 3; via carbonyl oxygen

Metal binding

178

1

Calcium 3; via carbonyl oxygen

Metal binding

180

1

Calcium 3; via carbonyl oxygen

Metal binding

183

1

Zinc 1

Metal binding

190

1

Calcium 2; via carbonyl oxygen

Metal binding

192

1

Calcium 2; via carbonyl oxygen

Metal binding

194

1

Calcium 2

Metal binding

196

1

Zinc 1

Metal binding

198

1

Calcium 3

Metal binding

199

1

Calcium 1

Metal binding

201

1

Calcium 1

Metal binding

201

1

Calcium 3

Metal binding

218

1

Zinc 2; catalytic Ref.16

Metal binding

222

1

Zinc 2; catalytic Ref.16

Metal binding

228

1

Zinc 2; catalytic Ref.16

Metal binding

297

1

Calcium 4; via carbonyl oxygen By similarity

Metal binding

389

1

Calcium 4; via carbonyl oxygen By similarity

Metal binding

438

1

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Disulfide bond

290 ↔ 477

By similarity

Natural variations

Natural variant

45

1

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

VAR_013090

Experimental info

Sequence conflict

420

1

P → L Ref.3

Secondary structure

1

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477

Helix Strand Turn

Details...

Helix

34 – 41

8

Helix

58 – 70

13

Helix

81 – 86

6

Beta strand

96 – 98

3

Beta strand

102 – 104

3

Beta strand

110 – 118

9

Beta strand

123 – 125

3

Helix

127 – 142

16

Beta strand

144 – 146

3

Beta strand

148 – 151

4

Beta strand

153 – 155

3

Beta strand

158 – 164

7

Beta strand

169 – 171

3

Beta strand

176 – 179

4

Beta strand

182 – 184

3

Beta strand

187 – 189

3

Turn

190 – 193

4

Beta strand

195 – 198

4

Beta strand

199 – 201

3

Beta strand

203 – 211

9

Helix

212 – 223

12

Turn

231 – 233

3

Beta strand

237 – 239

3

Helix

240 – 243

4

Helix

246 – 248

3

Helix

253 – 263

11

Sequences

	Sequence		Length	Mass (Da)
	P08254 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 96194833B907668D	FASTA	477	53,977
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

SeattleSNPs

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.

IPI

IPI00027782.

PIR

KCHUS1. A28156.

RefSeq

NP_002413.1. NM_002422.3.

UniGene

Hs.375129.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B3D	X-ray	2.30	A/B	100-272	[»]
1B8Y	X-ray	2.00	A	100-266	[»]
1BIW	X-ray	2.50	A/B	100-272	[»]
1BM6	NMR	-	A	100-272	[»]
1BQO	X-ray	2.30	A/B	100-272	[»]
1C3I	X-ray	1.83	A/B	100-272	[»]
1C8T	X-ray	2.60	A/B	103-268	[»]
1CAQ	X-ray	1.80	A	100-267	[»]
1CIZ	X-ray	1.64	A	100-267	[»]
1CQR	X-ray	2.00	A/B	100-272	[»]
1D5J	X-ray	2.60	A/B	100-272	[»]
1D7X	X-ray	2.00	A/B	100-272	[»]
1D8F	X-ray	2.40	A/B	100-272	[»]
1D8M	X-ray	2.44	A/B	100-272	[»]
1G05	X-ray	2.45	A/B	100-272	[»]
1G49	X-ray	1.90	A/B	100-272	[»]
1G4K	X-ray	2.00	A/B/C	100-267	[»]
1HFS	X-ray	1.70	A	105-264	[»]
1HY7	X-ray	1.50	A/B	100-272	[»]
1M1W	model	-	A	100-268	[»]
1OO9	NMR	-	A	100-267	[»]
1QIA	X-ray	2.00	A/B/C/D	106-267	[»]
1QIC	X-ray	2.00	A/B/C/D	106-266	[»]
1SLM	X-ray	1.90	A	18-272	[»]
1SLN	X-ray	2.27	A	100-272	[»]
1UEA	X-ray	2.80	A/C	100-272	[»]
1UMS	NMR	-	A	100-273	[»]
1UMT	NMR	-	A	100-273	[»]
1USN	X-ray	1.80	A	100-264	[»]
2D1O	X-ray	2.02	A/B	100-270	[»]
2JNP	NMR	-	A	105-265	[»]
2JT5	NMR	-	A	105-265	[»]
2JT6	NMR	-	A	105-265	[»]
2SRT	NMR	-	A	100-272	[»]
2USN	X-ray	2.20	A	100-264	[»]
3OHL	X-ray	2.36	A	100-266	[»]
3OHO	X-ray	2.50	A	100-268	[»]
3USN	NMR	-	A	100-267	[»]
4DPE	X-ray	1.96	A/B	100-272	[»]
4JA1	X-ray	1.96	A/B	100-272	[»]

ProteinModelPortal

P08254.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-269333.

STRING

9606.ENSP00000299855.

Protein family/group databases

MEROPS

M10.005.

PTM databases

PhosphoSite

P08254.

Polymorphism databases

DMDM

116857.

Proteomic databases

PaxDb

P08254.

PRIDE

P08254.

Protocols and materials databases

DNASU

4314.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299855; ENSP00000299855; ENSG00000149968.
ENST00000572537; ENSP00000458496; ENSG00000263313.

GeneID

4314.

KEGG

hsa:4314.

UCSC

uc001phj.1. human.

Organism-specific databases

CTD

4314.

GeneCards

GC11M102706.

HGNC

HGNC:7173. MMP3.

HPA

CAB016139.
HPA007875.

MIM

185250. gene.
614466. phenotype.

neXtProt

NX_P08254.

PharmGKB

PA30886.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258253.

HOGENOM

HOG000217927.

HOVERGEN

HBG052484.

InParanoid

P08254.

KO

K01394.

OMA

AVCSAYP.

OrthoDB

EOG4KKZ2X.

PhylomeDB

P08254.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_133391. Extracellular matrix organization.

Gene expression databases

ArrayExpress

P08254.

Bgee

P08254.

CleanEx

HS_MMP3.

Genevestigator

P08254.

GermOnline

ENSG00000149968. Homo sapiens.

Family and domain databases

Gene3D

2.110.10.10. 1 hit.
3.40.390.10. 1 hit.

InterPro

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_Metazoans.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]

Pfam

PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001191. Peptidase_M10A_matrix. 1 hit.

PRINTS

PR00138. MATRIXIN.

SMART

SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]

SUPFAM

SSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.

PROSITE

PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08254.

ChEMBL

CHEMBL283.

ChiTaRS

MMP3. human.

DrugBank

DB00786. Marimastat.
DB00641. Simvastatin.

EvolutionaryTrace

P08254.

GenomeRNAi

4314.

NextBio

16977.

PMAP-CutDB

P08254.

SOURCE

Search...

Entry information

Entry name

MMP3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.