Cystinyl aminopeptidase

Leucyl/cystinyl aminopeptidase
Identifiers
Symbols	LNPEP; CAP; IRAP; P-LAP; PLAP
External IDs	OMIM: 151300 MGI: 2387123 HomoloGene: 21148 GeneCards: LNPEP Gene
EC number	3.4.11.3
Gene Ontology Molecular function • aminopeptidase activity • peptidase activity • metallopeptidase activity • zinc ion binding • metal ion binding Cellular component • extracellular region • intracellular • membrane fraction • microsome • plasma membrane • integral to plasma membrane • perinuclear region of cytoplasm Biological process • proteolysis • cell-cell signaling • female pregnancy • protein catabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4012	240028
Ensembl	ENSG00000113441	ENSMUSG00000023845
UniProt	Q9UIQ6	n/a
RefSeq (mRNA)	NM_005575.2	NM_172827.3
RefSeq (protein)	NP_005566.2	NP_766415.1
Location (UCSC)	Chr 5: 96.27 – 96.37 Mb	Chr 17: 17.66 – 17.76 Mb
PubMed search	[1]	[2]

Leucyl-cystinyl aminopeptidase is an enzyme that in humans is encoded by the LNPEP gene.^[1][2]

This gene encodes a zinc-dependent aminopeptidase (metalloexopeptidase) that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms.^[2]

Interactions

Cystinyl aminopeptidase has been shown to interact with TNKS2.^[3][4][5]

References

1. ^ Rogi T, Tsujimoto M, Nakazato H, Mizutani S, Tomoda Y (Feb 1996). "Human placental leucine aminopeptidase/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family". J Biol Chem 271 (1): 56–61. doi:10.1074/jbc.271.1.56. PMID 8550619. 
2. ^ ^{a b} "Entrez Gene: LNPEP leucyl/cystinyl aminopeptidase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4012. 
3. ^ Sbodio, Juan I; Chi Nai-Wen (Aug. 2002). "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. (United States) 277 (35): 31887–92. doi:10.1074/jbc.M203916200. ISSN 0021-9258. PMID 12080061. 
4. ^ Chi, N W; Lodish H F (Dec. 2000). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles". J. Biol. Chem. (UNITED STATES) 275 (49): 38437–44. doi:10.1074/jbc.M007635200. ISSN 0021-9258. PMID 10988299. 
5. ^ Sbodio, Juan I; Lodish Harvey F, Chi Nai-Wen (Feb. 2002). "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. (England) 361 (Pt 3): 451–9. doi:10.1042/0264-6021:3610451. ISSN 0264-6021. PMC 1222327. PMID 11802774. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222327. 

Further reading

• Albiston AL, Mustafa T, McDowall SG, et al. (2003). "AT4 receptor is insulin-regulated membrane aminopeptidase: potential mechanisms of memory enhancement.". Trends Endocrinol. Metab. 14 (2): 72–7. doi:10.1016/S1043-2760(02)00037-1. PMID 12591177. 
• Keller SR (2004). "The insulin-regulated aminopeptidase: a companion and regulator of GLUT4.". Front. Biosci. 8: s410–20. doi:10.2741/1078. PMID 12700100. 
• Keller SR (2005). "Role of the insulin-regulated aminopeptidase IRAP in insulin action and diabetes.". Biol. Pharm. Bull. 27 (6): 761–4. doi:10.1248/bpb.27.761. PMID 15187412. 
• Nomura S, Ito T, Yamamoto E, et al. (2005). "Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy.". Biochim. Biophys. Acta 1751 (1): 19–25. doi:10.1016/j.bbapap.2005.04.006. PMID 15894523. 
• Tsujimoto M, Hattori A (2005). "The oxytocinase subfamily of M1 aminopeptidases.". Biochim. Biophys. Acta 1751 (1): 9–18. doi:10.1016/j.bbapap.2004.09.011. PMID 16054015. 
• Mizutani S, Shibata K, Kikkawa F, et al. (2007). "Essential role of placental leucine aminopeptidase in gynecologic malignancy.". Expert Opin. Ther. Targets 11 (4): 453–61. doi:10.1517/14728222.11.4.453. PMID 17373876. 
• Tsujimoto M, Mizutani S, Adachi H, et al. (1992). "Identification of human placental leucine aminopeptidase as oxytocinase.". Arch. Biochem. Biophys. 292 (2): 388–92. doi:10.1016/0003-9861(92)90007-J. PMID 1731608. 
• Mizutani S, Akiyama H, Kurauchi O, et al. (1985). "In vitro degradation of angiotensin II (A-II) by human placental subcellular fractions, pregnancy sera and purified placental aminopeptidases.". Acta Endocrinol. 110 (1): 135–9. PMID 3898693. 
• Beckman L, Björling G, Christodoulou C (1966). "Pregnancy enzymes and placental polymorphism. II. Leucine aminopeptidase.". Acta genetica et statistica medica 16 (2): 122–31. PMID 5953194. 
• Itoh C, Watanabe M, Nagamatsu A, et al. (1997). "Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization.". Biol. Pharm. Bull. 20 (1): 20–4. doi:10.1248/bpb.20.20. PMID 9013800. 
• Laustsen PG, Rasmussen TE, Petersen K, et al. (1997). "The complete amino acid sequence of human placental oxytocinase.". Biochim. Biophys. Acta 1352 (1): 1–7. doi:10.1016/S0167-4781(97)00036-5. PMID 9177475. 
• Nagasaka T, Nomura S, Okamura M, et al. (1998). "Immunohistochemical localization of placental leucine aminopeptidase/oxytocinase in normal human placental, fetal and adult tissues.". Reprod. Fertil. Dev. 9 (8): 747–53. doi:10.1071/R97055. PMID 9733056. 
• Horio J, Nomura S, Okada M, et al. (1999). "Structural organization of the 5'-end and chromosomal assignment of human placental leucine aminopeptidase/insulin-regulated membrane aminopeptidase gene.". Biochem. Biophys. Res. Commun. 262 (1): 269–74. doi:10.1006/bbrc.1999.1184. PMID 10448104. 
• Rasmussen TE, Pedraza-Díaz S, Hardré R, et al. (2000). "Structure of the human oxytocinase/insulin-regulated aminopeptidase gene and localization to chromosome 5q21.". Eur. J. Biochem. 267 (8): 2297–306. doi:10.1046/j.1432-1327.2000.01234.x. PMID 10759854. 
• Nakanishi Y, Nomura S, Okada M, et al. (2001). "Immunoaffinity purification and characterization of native placental leucine aminopeptidase/oxytocinase from human placenta.". Placenta 21 (7): 628–34. doi:10.1053/plac.2000.0564. PMID 10985965. 
• Chi NW, Lodish HF (2001). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles.". J. Biol. Chem. 275 (49): 38437–44. doi:10.1074/jbc.M007635200. PMID 10988299. 
• Matsumoto H, Nagasaka T, Hattori A, et al. (2001). "Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides.". Eur. J. Biochem. 268 (11): 3259–66. doi:10.1046/j.1432-1327.2001.02221.x. PMID 11389728. 
• Iwase A, Nomura S, Mizutani S (2001). "Characterization of a secretase activity for placental leucine aminopeptidase.". Arch. Biochem. Biophys. 393 (1): 163–9. doi:10.1006/abbi.2001.2489. PMID 11516173. 
• Ito T, Nomura S, Okada M, et al. (2001). "Transcriptional regulation of human placental leucine aminopeptidase/oxytocinase gene.". Mol. Hum. Reprod. 7 (9): 887–94. doi:10.1093/molehr/7.9.887. PMID 11517297. 

External links

• The MEROPS online database for peptidases and their inhibitors: M01.011

External links

• MeSH Cystinyl+aminopeptidase

This hydrolase article is a stub. You can help Wikipedia by expanding it.v · Categories: Human proteins Hydrolase stubs Wikimedia Foundation. 2010. Игры ⚽ Нужно сделать НИР? Rassie Erasmus Weaver Community, West Virginia Look at other dictionaries: cystinyl aminopeptidase — cys·ti·nyl ami·no·pep·ti·dase (sisґtĭ nəl ə me″no pepґtĭ dās) [EC 3.4.11.3] a zinc containing enzyme released by the placenta that acts to break down oxytocin and vasopressin; called also oxytocinase and… …   Medical dictionary Alanine aminopeptidase — Alanyl (membrane) aminopeptidase Identifiers Symbols ANPEP; APN; CD13; GP150; LAP1; P150; PEPN External IDs …   Wikipedia List of EC numbers (EC 3) — This list contains a list of EC numbers for the third group, EC 3, hydrolases, placed in numerical order as determined by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.EC 3.1: Acting on Ester BondsEC… …   Wikipedia Hydrolase — Cristal de lysozyme Les hydrolases constituent une classe d enzymes qui catalysent les réactions d hydrolyse de molécules suivant la réaction générale : R R + H2O ⇌ R OH + R H On y trouve par exemple les estérases, qui hydrolysent les …   Wikipédia en Français EC 3.4 — Le groupe EC3.4 est un groupe d enzymes appartenant à la famille des hydrolases. Leur rôle est de découper un polypeptide, d où leur nom générique de peptidases. La réaction chimique qu elles catalysent est : AA1 CO NH AA2 + H2O ⇌ AA1 COOH + …   Wikipédia en Français Oxytocin — Strukturformel …   Deutsch Wikipedia oxytocinase — oxy·to·ci·nase (ok″se toґsĭ nās) cystinyl aminopeptidase …   Medical dictionary vasopressinase — vaso·pres·sin·ase (va″zo ) (vas″o presґin ās) cystinyl aminopeptidase …   Medical dictionary DNPEP — Aspartyl aminopeptidase Identifiers Symbols DNPEP; ASPEP; DAP External IDs OMIM …   Wikipedia DPEP2 — dipeptidase 2 Identifiers Symbol DPEP2 Entrez 64174 HUGO …   Wikipedia 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”