MMP23B

MMP23B
Identifiers
Aliases	MMP23B , MIFR, MIFR-1, MMP22, MMP23A, matrix metallopeptidase 23B
External IDs	OMIM: 603321; MGI: 1347361; HomoloGene: 3424; GeneCards: MMP23B; OMA:MMP23B - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p36.33 Start 1,632,163 bp [1] End 1,635,263 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 E2 Start 155,735,112 bp [2] End 155,737,841 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right ovary left uterine tube right coronary artery left ovary left ventricle thoracic aorta ascending aorta Descending thoracic aorta granulocyte Top expressed in ascending aorta aortic valve calvaria uterus stroma of bone marrow tunica media of zone of aorta body of femur renal corpuscle pericardial cavity efferent ductule More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component integral component of membrane intracellular anatomical structure endoplasmic reticulum membrane endoplasmic reticulum membrane extracellular matrix collagen-containing extracellular matrix extracellular space Biological process reproduction proteolysis extracellular matrix organization collagen catabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8510 26561 Ensembl ENSG00000189409 ENSMUSG00000029061 UniProt O75900 O88676 RefSeq (mRNA) NM_006983 NM_011985 NM_001320235 RefSeq (protein) NP_008914 NP_001307164 NP_036115 Location (UCSC) Chr 1: 1.63 – 1.64 Mb Chr 4: 155.74 – 155.74 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Matrix metalloproteinase-23 is an enzyme that in humans is encoded by the MMP23B gene. ^{[5] [6] [7]}

Function

This gene (MMP23B) encodes a member of the matrix metalloproteinase (MMP) family, and it is part of a duplicated region of chromosome 1p36.3. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. This gene belongs to the copy of the duplicated region of the gene that is closer to the end of the chromosome (more telemeric). ^[7]

MMP23B is strongly expressed in ovary and heart. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000189409 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029061 – 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. Gururajan R, Grenet J, Lahti JM, Kidd VJ (May 1999). "Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3". Genomics. 52 (1): 101–6. doi:10.1006/geno.1998.5401. PMID   9740677.
6. Gururajan R, Lahti JM, Grenet J, Easton J, Gruber I, Ambros PF, Kidd VJ (Nov 1998). "Duplication of a genomic region containing the Cdc2L1-2 and MMP21-22 genes on human chromosome 1p36.3 and their linkage to D1Z2". Genome Res. 8 (9): 929–39. doi:10.1101/gr.8.9.929. PMC   310781 . PMID   9750192.
7. "Entrez Gene: MMP23B matrix metallopeptidase 23B".
8. Zhao S, Zhao Y, Niu P, Wang N, Tang Z, Zan L, Li K (2011). "Molecular characterization of porcine MMP19 and MMP23B genes and its association with immune traits". Int. J. Biol. Sci. 7 (8): 1101–13. doi:10.7150/ijbs.7.1101. PMC   3174387 . PMID   21927579.

Further reading

• Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi: 10.1074/jbc.274.31.21491 . PMID   10419448.
• Velasco G, Pendás AM, Fueyo A, et al. (1999). "Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members". J. Biol. Chem. 274 (8): 4570–6. doi: 10.1074/jbc.274.8.4570 . PMID   9988691.
• Terp GE, Christensen IT, Jørgensen FS (2000). "Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes". J. Biomol. Struct. Dyn. 17 (6): 933–46. doi:10.1080/07391102.2000.10506582. PMID   10949161. S2CID   1270176.
• Ohnishi J, Ohnishi E, Jin M, et al. (2001). "Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development". Mol. Endocrinol. 15 (5): 747–64. doi: 10.1210/mend.15.5.0638 . PMID   11328856. S2CID   22774708.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Gajecka M, Yu W, Ballif BC, et al. (2005). "Delineation of mechanisms and regions of dosage imbalance in complex rearrangements of 1p36 leads to a putative gene for regulation of cranial suture closure". Eur. J. Hum. Genet. 13 (2): 139–49. doi: 10.1038/sj.ejhg.5201302 . PMID   15483646.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID   16710414.

External links

• The MEROPS online database for peptidases and their inhibitors: M10.022