TMPRSS11D

TMPRSS11D
Identifiers
Aliases	TMPRSS11D, HAT, transmembrane protease, serine 11D, transmembrane serine protease 11D, ASP
External IDs	OMIM: 605369; MGI: 2385221; GeneCards: TMPRSS11D
Gene location (Human) Chr. Chromosome 4 (human) Band 4q13.2 Start 67,820,876 bp End 67,884,002 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 E1 Start 86,450,076 bp End 86,521,279 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gums gingival epithelium cervix epithelium oral cavity body of tongue amniotic fluid mucosa of pharynx buccal mucosa cell periodontal fiber human penis Top expressed in esophagus external naris mucosa of esophagus epithelium of esophagus lip cervix cornea stomach neural layer of retina lacrimal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity Cellular component integral component of membrane extracellular region plasma membrane integral component of plasma membrane extracellular exosome membrane Biological process respiratory gaseous exchange by respiratory system proteolysis Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 9407 231382 Ensembl ENSG00000153802 ENSMUSG00000061259 UniProt O60235 Q8VHK8 RefSeq (mRNA) NM_004262 NM_145561 RefSeq (protein) NP_004253 NP_663536 Location (UCSC) Chr 4: 67.82 – 67.88 Mb Chr 5: 86.45 – 86.52 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Transmembrane protease, serine 11D is an enzyme that in humans is encoded by the TMPRSS11D gene.

This gene encodes a trypsin-like serine protease released from the submucosal serous glands onto mucous membrane. It is a type II integral membrane protein and has 29-38% identity in the sequence of the catalytic region with human hepsin, enteropeptidase, acrosin, and mast cell tryptase. The noncatalytic region has little similarity to other known proteins. This protein may play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions.

Further reading

• Takahashi M, Sano T, Yamaoka K, et al. (2001). "Localization of human airway trypsin-like protease in the airway: an immunohistochemical study". Histochem. Cell Biol. 115 (3): 181–7. doi:10.1007/s004180000243. PMID 11326745. S2CID 25025224.
• 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.
• Miki M, Nakamura Y, Takahashi A, et al. (2003). "Effect of human airway trypsin-like protease on intracellular free Ca2+ concentration in human bronchial epithelial cells". J. Med. Invest. 50 (1–2): 95–107. PMID 12630574.
• 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.
• Iwakiri K, Ghazizadeh M, Jin E, et al. (2004). "Human airway trypsin-like protease induces PAR-2-mediated IL-8 release in psoriasis vulgaris". J. Invest. Dermatol. 122 (4): 937–44. doi:10.1111/j.0022-202X.2004.22415.x. PMID 15102084.
• 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.
• Matsushima R, Takahashi A, Nakaya Y, et al. (2006). "Human airway trypsin-like protease stimulates human bronchial fibroblast proliferation in a protease-activated receptor-2-dependent pathway". Am. J. Physiol. Lung Cell Mol. Physiol. 290 (2): L385–95. doi:10.1152/ajplung.00098.2005. PMID 16199437.
• Chokki M, Eguchi H, Hamamura I, et al. (2006). "Human airway trypsin-like protease induces amphiregulin release through a mechanism involving protease-activated receptor-2-mediated ERK activation and TNF alpha-converting enzyme activity in airway epithelial cells". FEBS J. 272 (24): 6387–99. doi:10.1111/j.1742-4658.2005.05035.x. PMID 16336275. S2CID 34294232.
• Böttcher E, Matrosovich T, Beyerle M, et al. (2006). "Proteolytic Activation of Influenza Viruses by Serine Proteases TMPRSS2 and HAT from Human Airway Epithelium". J. Virol. 80 (19): 9896–8. doi:10.1128/JVI.01118-06. PMC 1617224. PMID 16973594.

External links

• Overview of all the structural information available in the PDB for UniProt: Q8VHK8 (Mouse Transmembrane protease serine 11D) at the PDBe-KB.