NAPSA

NAPSA
Identifiers
Aliases	NAPSA, KAP, Kdap, NAP1, NAPA, SNAPA, napsin A aspartic peptidase
External IDs	OMIM: 605631; MGI: 109365; GeneCards: NAPSA
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.33 Start 50,358,477 bp End 50,365,830 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 B3 Start 44,221,804 bp End 44,236,286 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lower lobe of lung upper lobe of lung upper lobe of left lung visceral pleura right lung human kidney testicle right uterine tube mucosa of transverse colon caput epididymis Top expressed in right kidney human kidney left lung right lung left lung lobe right lung lobe proximal tubule spleen granulocyte tibiofemoral joint More reference expression data BioGPS n/a
Gene ontology Molecular function endopeptidase activity hydrolase activity aspartic-type endopeptidase activity peptidase activity Cellular component extracellular region lysosome extracellular exosome alveolar lamellar body multivesicular body lumen extracellular space Biological process surfactant homeostasis protein catabolic process proteolysis membrane protein proteolysis autophagy Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 9476 16541 Ensembl ENSG00000131400 ENSMUSG00000002204 UniProt O96009 O09043 RefSeq (mRNA) NM_004851 NM_008437 RefSeq (protein) NP_004842 NP_032463 Location (UCSC) Chr 19: 50.36 – 50.37 Mb Chr 7: 44.22 – 44.24 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Napsin-A is an aspartic proteinase that is encoded in humans by the NAPSA gene. The name napsin comes from novel aspartic proteinase of the pepsin family.

The activation peptide of an aspartic proteinase acts as an inhibitor of the active site. These peptide segments, or pro-parts, are deemed important for correct folding, targeting, and control of the activation of aspartic proteinase zymogens. The pronapsin A gene is expressed predominantly in lung and kidney. Its translation product is predicted to be a fully functional, glycosylated aspartic proteinase precursor containing an RGD motif and an additional 18 residues at its C-terminus.

Utility

Detection of NAPSA gene expression can be used to distinguish adenocarcinomas from other forms of lung cancer.

Further reading

• Koelsch G, Mares M, Metcalf P, Fusek M (1994). "Multiple functions of pro-parts of aspartic proteinase zymogens". FEBS Letters. 343 (1): 6–10. Bibcode:1994FEBSL.343....6K. doi:10.1016/0014-5793(94)80596-2. PMID 8163018. S2CID 32345795.
• Blundell TL, Guruprasad K, Albert A, Williams M, Sibanda BL, Dhanaraj V (1998). Aspartic Proteinases. Adv. Exp. Med. Biol. Vol. 436. pp. 1–13. doi:10.1007/978-1-4615-5373-1_1. ISBN 978-1-4613-7452-7. PMID 9561193.
• Chuman Y, Bergman A, Ueno T, Saito S, Sakaguchi K, Alaiya AA, et al. (November 1999). "Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas". FEBS Letters. 462 (1–2): 129–134. doi:10.1016/S0014-5793(99)01493-3. PMID 10580105. S2CID 23355055.
• Schauer-Vukasinovic V, Bur D, Kling D, Grüninger F, Giller T (November 1999). "Human napsin A: expression, immunochemical detection, and tissue localization". FEBS Letters. 462 (1–2): 135–139. doi:10.1016/S0014-5793(99)01458-1. PMID 10580106. S2CID 32798620.
• Yan R, Bienkowski MJ, Shuck ME, Miao H, Tory MC, Pauley AM, et al. (December 1999). "Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity". Nature. 402 (6761): 533–537. Bibcode:1999Natur.402..533Y. doi:10.1038/990107. PMID 10591213. S2CID 4320087.
• Cook M, Bühling F, Ansorge S, Tatnell PJ, Kay J (August 2002). "Pronapsin A and B gene expression in normal and malignant human lung and mononuclear blood cells". Biochimica et Biophysica Acta. 1577 (1): 10–16. doi:10.1016/s0167-4781(02)00400-1. PMID 12151090.
• Brasch F, Ochs M, Kahne T, Guttentag S, Schauer-Vukasinovic V, Derrick M, et al. (December 2003). "Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type-II pneumocytes of the human lung". The Journal of Biological Chemistry. 278 (49): 49006–49014. doi:10.1074/jbc.M306844200. PMID 13129928.
• Innocenti M, Zucconi A, Disanza A, Frittoli E, Areces LB, Steffen A, et al. (April 2004). "Abi1 is essential for the formation and activation of a WAVE2 signalling complex". Nature Cell Biology. 6 (4): 319–327. doi:10.1038/ncb1105. PMID 15048123. S2CID 22767022.