TIMP3

Metalloproteinase inhibitor 3 is a protein that in humans is encoded by the TIMP3 gene.[5][6]

TIMP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3CKI
Identifiers
Aliases	TIMP3, HSMRK222, K222, K222TA2, SFD, TIMP metallopeptidase inhibitor 3
External IDs	OMIM: 188826 MGI: 98754 HomoloGene: 36322 GeneCards: TIMP3
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q12.3 Start 32,801,701 bp[1] End 32,863,043 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 42.83 cM Start 86,300,372 bp[2] End 86,349,506 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • peptidase inhibitor activity • GO:0048551 enzyme inhibitor activity • metal ion binding • protease binding • GO:0001948 protein binding • metalloendopeptidase inhibitor activity Cellular component • extracellular matrix • proteinaceous extracellular matrix • basement membrane • extracellular exosome • cell nucleus • extracellular region • platelet dense granule lumen • extracellular • collagen-containing extracellular matrix Biological process • cellular response to organic substance • negative regulation of peptidase activity • response to stimulus • positive regulation of TRAIL-activated apoptotic signaling pathway • negative regulation of ERK1 and ERK2 cascade • negative regulation of membrane protein ectodomain proteolysis • visual perception • platelet degranulation • response to organic substance • negative regulation of metalloendopeptidase activity • response to hormone • negative regulation of endopeptidase activity • response to cytokine Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7078	21859
Ensembl	ENSG00000100234	ENSMUSG00000020044
UniProt	P35625	P39876
RefSeq (mRNA)	NM_000362	NM_011595
RefSeq (protein)	NP_000353	NP_035725
Location (UCSC)	Chr 22: 32.8 – 32.86 Mb	Chr 10: 86.3 – 86.35 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

This gene belongs to the tissue inhibitor of metalloproteinases gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix (ECM). Expression of this gene is induced in response to mitogenic stimulation and this netrin domain-containing protein is localized to the ECM. Mutations in this gene have been associated with the autosomal dominant disorder Sorsby's fundus dystrophy.[7]

See also

• TIMP1, TIMP2, TIMP4

References

1. GRCh38: Ensembl release 89: ENSG00000100234 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020044 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Apte SS, Mattei MG, Olsen BR (Jun 1994). "Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22". Genomics. 19 (1): 86–90. doi:10.1006/geno.1994.1016. PMID 8188246.
6. Qi JH, Ebrahem Q, Moore N, Murphy G, Claesson-Welsh L, Bond M, Baker A, Anand-Apte B (Apr 2003). "A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2". Nat Med. 9 (4): 407–15. doi:10.1038/nm846. PMID 12652295.
7. "Entrez Gene: TIMP3 TIMP metallopeptidase inhibitor 3 (Sorsby fundus dystrophy, pseudoinflammatory)".

Further reading

• Li Z, Clarke MP, Barker MD, McKie N (2007). "TIMP3 mutation in Sorsby's fundus dystrophy: molecular insights". Expert Reviews in Molecular Medicine. 7 (24): 1–15. doi:10.1017/S1462399405010045. PMID 16259644.
• Docherty AJ, Lyons A, Smith BJ, et al. (1985). "Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity". Nature. 318 (6041): 66–9. Bibcode:1985Natur.318...66D. doi:10.1038/318066a0. PMID 3903517.
• Forsius HR, Eriksson AW, Suvanto EA, Alanko HI (1983). "Pseudoinflammatory fundus dystrophy with autosomal recessive inheritance". Am. J. Ophthalmol. 94 (5): 634–49. doi:10.1016/0002-9394(82)90009-5. PMID 7148944.
• Wick M, Härönen R, Mumberg D, et al. (1995). "Structure of the human TIMP-3 gene and its cell cycle-regulated promoter". Biochem. J. 311. ( Pt 2) (2): 549–54. doi:10.1042/bj3110549. PMC 1136034. PMID 7487894.
• Jacobson SG, Cideciyan AV, Regunath G, et al. (1995). "Night blindness in Sorsby's fundus dystrophy reversed by vitamin A.". Nat. Genet. 11 (1): 27–32. doi:10.1038/ng0995-27. PMID 7550309.
• Higuchi T, Kanzaki H, Nakayama H, et al. (1995). "Induction of tissue inhibitor of metalloproteinase 3 gene expression during in vitro decidualization of human endometrial stromal cells". Endocrinology. 136 (11): 4973–81. doi:10.1210/en.136.11.4973. PMID 7588231.
• Wilde CG, Hawkins PR, Coleman RT, et al. (1995). "Cloning and characterization of human tissue inhibitor of metalloproteinases-3". DNA Cell Biol. 13 (7): 711–8. doi:10.1089/dna.1994.13.711. PMID 7772252.
• Apte SS, Olsen BR, Murphy G (1995). "The gene structure of tissue inhibitor of metalloproteinases (TIMP)-3 and its inhibitory activities define the distinct TIMP gene family". J. Biol. Chem. 270 (24): 14313–8. doi:10.1074/jbc.270.24.14313. PMID 7782289.
• Kishnani NS, Staskus PW, Yang TT, et al. (1995). "Identification and characterization of human tissue inhibitor of metalloproteinase-3 and detection of three additional metalloproteinase inhibitor activities in extracellular matrix". Matrix Biol. 14 (6): 479–88. doi:10.1016/0945-053X(95)90005-5. PMID 7795886.
• Weber BH, Vogt G, Pruett RC, et al. (1995). "Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy". Nat. Genet. 8 (4): 352–6. doi:10.1038/ng1294-352. PMID 7894485.
• Weber BH, Vogt G, Wolz W, et al. (1994). "Sorsby's fundus dystrophy is genetically linked to chromosome 22q13-qter". Nat. Genet. 7 (2): 158–61. doi:10.1038/ng0694-158. PMID 7920634.
• Jones SE, Jomary C, Neal MJ (1994). "Expression of TIMP3 mRNA is elevated in retinas affected by simplex retinitis pigmentosa". FEBS Lett. 352 (2): 171–4. doi:10.1016/0014-5793(94)00951-1. PMID 7925969.
• Wick M, Bürger C, Brüsselbach S, et al. (1994). "A novel member of human tissue inhibitor of metalloproteinases (TIMP) gene family is regulated during G1 progression, mitogenic stimulation, differentiation, and senescence". J. Biol. Chem. 269 (29): 18953–60. PMID 8034652.
• Silbiger SM, Jacobsen VL, Cupples RL, Koski RA (1994). "Cloning of cDNAs encoding human TIMP-3, a novel member of the tissue inhibitor of metalloproteinase family". Gene. 141 (2): 293–7. doi:10.1016/0378-1119(94)90588-6. PMID 8163205.
• Uría JA, Ferrando AA, Velasco G, et al. (1994). "Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor family". Cancer Res. 54 (8): 2091–4. PMID 8174111.
• Byrne JA, Tomasetto C, Rouyer N, et al. (1996). "The tissue inhibitor of metalloproteinases-3 gene in breast carcinoma: identification of multiple polyadenylation sites and a stromal pattern of expression". Mol. Med. 1 (4): 418–27. doi:10.1007/BF03401579. PMC 2229996. PMID 8521299.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Felbor U, Stöhr H, Amann T, et al. (1996). "A novel Ser156Cys mutation in the tissue inhibitor of metalloproteinases-3 (TIMP3) in Sorsby's fundus dystrophy with unusual clinical features". Hum. Mol. Genet. 4 (12): 2415–6. doi:10.1093/hmg/4.12.2415. PMID 8634721.
• Carrero-Valenzuela RD, Klein ML, Weleber RG, et al. (1996). "Sorsby fundus dystrophy. A family with the Ser181Cys mutation of the tissue inhibitor of metalloproteinases 3". Arch. Ophthalmol. 114 (6): 737–8. doi:10.1001/archopht.1996.01100130729016. PMID 8639088.

External links

• The MEROPS online database for peptidases and their inhibitors: I35.003