MMP19

Protein-coding gene in the species Homo sapiens
MMP19
Identifiers
AliasesMMP19, MMP18, RASI-1, CODA, matrix metallopeptidase 19
External IDsOMIM: 601807; MGI: 1927899; HomoloGene: 1820; GeneCards: MMP19; OMA:MMP19 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for MMP19
Genomic location for MMP19
Band12q13.2Start55,835,433 bp[1]
End55,842,966 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for MMP19
Genomic location for MMP19
Band10 D3|10 77.16 cMStart128,626,779 bp[2]
End128,636,693 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left uterine tube

  • gallbladder

  • olfactory bulb

  • upper lobe of left lung

  • spleen

  • ascending aorta

  • stromal cell of endometrium

  • Descending thoracic aorta

  • smooth muscle tissue

  • right ovary
Top expressed in
  • liver

  • stroma of bone marrow

  • blood

  • left lobe of liver

  • adrenal gland

  • uterus

  • aortic valve

  • ascending aorta

  • muscle of thigh

  • belly cord
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • zinc ion binding
  • metal ion binding
  • peptidase activity
  • hydrolase activity
  • metallopeptidase activity
  • metalloendopeptidase activity
  • serine-type endopeptidase activity
Cellular component
  • extracellular region
  • extracellular matrix
  • extracellular space
Biological process
  • cell differentiation
  • ovulation from ovarian follicle
  • extracellular matrix disassembly
  • luteolysis
  • proteolysis
  • multicellular organism development
  • angiogenesis
  • ovarian follicle development
  • response to hormone
  • response to cAMP
  • collagen catabolic process
  • extracellular matrix organization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4327

58223

Ensembl

ENSG00000123342

ENSMUSG00000025355

UniProt

Q99542

Q9JHI0

RefSeq (mRNA)

NM_001032360
NM_001272101
NM_002429
NM_022790
NM_022792

NM_001164197
NM_021412

RefSeq (protein)

NP_001259030
NP_002420

NP_001157669
NP_067387

Location (UCSC)Chr 12: 55.84 – 55.84 MbChr 10: 128.63 – 128.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Matrix metalloproteinase-19 (MMP-19) also known as matrix metalloproteinase RASI is an enzyme that in humans is encoded by the MMP19 gene.[5][6]

Function

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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This protein is expressed in human epidermis and endothelial cells and it has a role in cellular proliferation, migration, angiogenesis and adhesion. Multiple transcript variants encoding distinct isoforms have been identified for this gene.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123342 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025355 – 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. ^ Kolb C, Mauch S, Peter HH, Krawinkel U, Sedlacek R (Oct 1997). "The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient". Immunol Lett. 57 (1–3): 83–8. doi:10.1016/S0165-2478(97)00057-6. PMID 9232430.
  6. ^ a b "Entrez Gene: MMP19 matrix metallopeptidase 19".

Further reading

  • Murphy G, Knäuper V, Cowell S, et al. (1999). "Evaluation of some newer matrix metalloproteinases". Ann. N. Y. Acad. Sci. 878 (1): 25–39. Bibcode:1999NYASA.878...25M. doi:10.1111/j.1749-6632.1999.tb07672.x. PMID 10415718. S2CID 38505267.
  • Nagase H, Woessner JF (1999). "Matrix metalloproteinases". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
  • Fosang AJ, Last K, Neame PJ, et al. (1995). "Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan". Biochem. J. 304 (Pt 2): 347–51. doi:10.1042/bj3040347. PMC 1137499. PMID 7998967.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Fosang AJ, Last K, Knäuper V, et al. (1993). "Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain". Biochem. J. 295 (Pt 1): 273–6. doi:10.1042/bj2950273. PMC 1134849. PMID 8216228.
  • Cossins J, Dudgeon TJ, Catlin G, et al. (1996). "Identification of MMP-18, a putative novel human matrix metalloproteinase". Biochem. Biophys. Res. Commun. 228 (2): 494–8. doi:10.1006/bbrc.1996.1688. PMID 8920941.
  • Pendás AM, Knäuper V, Puente XS, et al. (1997). "Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location, and tissue distribution". J. Biol. Chem. 272 (7): 4281–6. doi:10.1074/jbc.272.7.4281. PMID 9020145.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Sedlacek R, Mauch S, Kolb B, et al. (1998). "Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis". Immunobiology. 198 (4): 408–23. doi:10.1016/s0171-2985(98)80049-1. PMID 9562866.
  • Fosang AJ, Last K, Fujii Y, et al. (1998). "Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain". FEBS Lett. 430 (3): 186–90. Bibcode:1998FEBSL.430..186F. doi:10.1016/S0014-5793(98)00667-X. PMID 9688535. S2CID 21861810.
  • Stracke JO, Hutton M, Stewart M, et al. (2000). "Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme". J. Biol. Chem. 275 (20): 14809–16. doi:10.1074/jbc.275.20.14809. PMID 10809722.
  • Mueller MS, Mauch S, Sedlacek R (2000). "Structure of the human MMP-19 gene". Gene. 252 (1–2): 27–37. doi:10.1016/S0378-1119(00)00236-5. PMID 10903435.
  • Stracke JO, Fosang AJ, Last K, et al. (2000). "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)". FEBS Lett. 478 (1–2): 52–6. Bibcode:2000FEBSL.478...52S. doi:10.1016/S0014-5793(00)01819-6. PMID 10922468. S2CID 37366875.
  • 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.
  • Mauch S, Kolb C, Kolb B, et al. (2002). "Matrix metalloproteinase-19 is expressed in myeloid cells in an adhesion-dependent manner and associates with the cell surface". J. Immunol. 168 (3): 1244–51. doi:10.4049/jimmunol.168.3.1244. PMID 11801661.
  • Rodríguez-Manzaneque JC, Westling J, Thai SN, et al. (2002). "ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors". Biochem. Biophys. Res. Commun. 293 (1): 501–8. doi:10.1016/S0006-291X(02)00254-1. PMID 12054629.
  • 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.
  • Titz B, Dietrich S, Sadowski T, Beck C, Petersen A, Sedlacek R (2004). "Activity of MMP-19 inhibits capillary-like formation due to processing of nidogen-1". Cell Mol Life Sci. 61 (14): 1826–33. doi:10.1007/s00018-004-4105-0. PMC 11138908. PMID 15241558. S2CID 6853562.

External links

  • The MEROPS online database for peptidases and their inhibitors: M10.021
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