Serine protease HTRA1

HTRA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2JOA, 2YTW, 3NUM, 3NWU, 3NZI, 3TJN, 3TJO, 3TJQ
Identifiers
Aliases	HTRA1 , ARMD7, CARASIL, HtrA, L56, ORF480, PRSS11, CADASIL2, HtrA serine peptidase 1
External IDs	OMIM: 602194; MGI: 1929076; HomoloGene: 31114; GeneCards: HTRA1; OMA:HTRA1 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) [1] Band 10q26.13 Start 122,458,551 bp [1] End 122,514,907 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7|7 F3 Start 130,537,841 bp [2] End 130,587,390 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii glomerulus metanephric glomerulus Descending thoracic aorta stromal cell of endometrium ascending aorta synovial membrane middle frontal gyrus synovial joint putamen Top expressed in decidua epithelium of lens facial motor nucleus gastrula cumulus cell calvaria umbilical cord ascending aorta motor neuron tunica media of zone of aorta More reference expression data BioGPS More reference expression data
Gene ontology Molecular function insulin-like growth factor binding growth factor binding peptidase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity protein binding identical protein binding Cellular component cytoplasm cytosol membrane extracellular matrix plasma membrane extracellular exosome extracellular region extracellular space collagen-containing extracellular matrix Biological process negative regulation of defense response to virus chorionic trophoblast cell differentiation positive regulation of epithelial cell proliferation placenta development dentinogenesis negative regulation of transforming growth factor beta receptor signaling pathway proteolysis negative regulation of BMP signaling pathway regulation of cell growth extracellular matrix disassembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5654 56213 Ensembl ENSG00000166033 ENSMUSG00000006205 UniProt Q92743 Q9R118 RefSeq (mRNA) NM_002775 NM_019564 RefSeq (protein) NP_002766 NP_062510 Location (UCSC) Chr 10: 122.46 – 122.51 Mb Chr 7: 130.54 – 130.59 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Serine protease HTRA1 is an enzyme that in humans is encoded by the HTRA1 gene. ^{[5] [6]} The HTRA1 protein is composed of four distinct protein domains. They are from amino-terminus to carboxyl-terminus an Insulin-like growth factor binding domain, a kazal domain, a trypsin-like peptidase domain and a PDZ domain.

This gene encodes a member of the trypsin family of serine proteases. This protein is a secreted enzyme that is proposed to regulate the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. It has also been suggested to be a regulator of cell growth. ^[6]

Mutations of this gene are responsible for the development of CARASIL, a genetic form of cerebral vasculopathy.

References

1. GRCh38: Ensembl release 89: ENSG00000166033 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000006205 – 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. Zumbrunn J, Trueb B (Jan 1997). "Primary structure of a putative serine protease specific for IGF-binding proteins". FEBS Lett. 398 (2–3): 187–92. doi:10.1016/S0014-5793(96)01229-X. PMID   8977104. S2CID   39934612.
6. "Entrez Gene: HTRA1 HtrA serine peptidase 1".

External links

• GeneReviews/NCBI/NIH/UW entry on CARASIL Cerebral Autosomal Recessive Arteriopathy with Subcortical Infarcts and Leukoencephalopathy, Maeda Syndrome
• OMIM entries on CARASIL

Further reading

• Bradley DT, Zipfel PF, Hughes AE (2011). "Complement in age-related macular degeneration: a focus on function". Eye. 25 (6): 683–693. doi:10.1038/eye.2011.37. PMC   3178140 . PMID   21394116.
• Zurawa-Janicka D, Narkiewicz J, Lipińska B (2007). "[Characterization of the HtrA family of proteins]". Postepy Biochem. 53 (1): 27–36. PMID   17718385.
• 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.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Zumbrunn J, Trueb B (1998). "Localization of the gene for a serine protease with IGF-binding domain (PRSS11) to human chromosome 10q25.3-q26.2". Genomics. 45 (2): 461–2. doi:10.1006/geno.1997.4953. PMID   9344681.
• Hu SI, Carozza M, Klein M, et al. (1999). "Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage". J. Biol. Chem. 273 (51): 34406–12. doi: 10.1074/jbc.273.51.34406 . PMID   9852107.
• Baldi A, De Luca A, Morini M, et al. (2002). "The HtrA1 serine protease is down-regulated during human melanoma progression and represses growth of metastatic melanoma cells". Oncogene. 21 (43): 6684–8. doi: 10.1038/sj.onc.1205911 . PMID   12242667. S2CID   9021435.
• 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.
• Nie GY, Hampton A, Li Y, et al. (2003). "Identification and cloning of two isoforms of human high-temperature requirement factor A3 (HtrA3), characterization of its genomic structure and comparison of its tissue distribution with HtrA1 and HtrA2". Biochem. J. 371 (Pt 1): 39–48. doi:10.1042/BJ20021569. PMC   1223265 . PMID   12513693.
• De Luca A, De Falco M, Severino A, et al. (2003). "Distribution of the serine protease HtrA1 in normal human tissues". J. Histochem. Cytochem. 51 (10): 1279–84. doi:10.1177/002215540305101004. PMID   14500695. S2CID   19726897.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Chien J, Staub J, Hu SI, et al. (2004). "A candidate tumor suppressor HtrA1 is downregulated in ovarian cancer". Oncogene. 23 (8): 1636–44. doi: 10.1038/sj.onc.1207271 . PMID   14716297.
• Oka C, Tsujimoto R, Kajikawa M, et al. (2004). "HtrA1 serine protease inhibits signaling mediated by Tgfbeta family proteins". Development. 131 (5): 1041–53. doi:10.1242/dev.00999. PMID   14973287. S2CID   27495047.
• Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC   442148 . PMID   15231748.
• Grau S, Baldi A, Bussani R, et al. (2005). "Implications of the serine protease HtrA1 in amyloid precursor protein processing". Proc. Natl. Acad. Sci. U.S.A. 102 (17): 6021–6. doi: 10.1073/pnas.0501823102 . PMC   1087941 . PMID   15855271.
• Ozturk A, Desai PP, Minster RL, et al. (2005). "Three SNPs in the GSTO1, GSTO2 and PRSS11 genes on chromosome 10 are not associated with age-at-onset of Alzheimer's disease". Neurobiol. Aging. 26 (8): 1161–5. doi: 10.1016/j.neurobiolaging.2004.11.001 . PMID   15917099. S2CID   10878355.
• Grau S, Richards PJ, Kerr B, et al. (2006). "The role of human HtrA1 in arthritic disease". J. Biol. Chem. 281 (10): 6124–9. doi: 10.1074/jbc.M500361200 . PMID   16377621.
• Bowden MA, Di Nezza-Cossens LA, Jobling T, et al. (2006). "Serine proteases HTRA1 and HTRA3 are down-regulated with increasing grades of human endometrial cancer". Gynecol. Oncol. 103 (1): 253–60. doi:10.1016/j.ygyno.2006.03.006. PMID   16650464.
• Chien J, Aletti G, Baldi A, et al. (2006). "Serine protease HtrA1 modulates chemotherapy-induced cytotoxicity". J. Clin. Invest. 116 (7): 1994–2004. doi:10.1172/JCI27698. PMC   1474818 . PMID   16767218.
• Dewan A, Liu M, Hartman S, et al. (2006). "HTRA1 promoter polymorphism in wet age-related macular degeneration". Science. 314 (5801): 989–92. doi:10.1126/science.1133807. PMID   17053108. S2CID   85725181.