ADCY10

Adenylate cyclase 10 (soluble)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4CLF​, 4CLK​, 4CLL​, 4CLP​, 4CLS​, 4CLT​, 4CLU​, 4CLW​, 4CLY​, 4CLZ​, 4CM0​, 4CM2​, 4OYA​, 4OYB​, 4OYI​, 4OYM​, 4OYO​, 4OYP​, 4OYW​, 4OYX​, 4OYZ​, 4OZ2​, 4OZ3​, 4UST​, 4USU​, 4USV​, 4USW​
Identifiers
Symbols	ADCY10 ; HCA2; SAC; SACI; Sacy; hsAC
External IDs	OMIM: 605205 MGI: 2660854 HomoloGene: 10188 ChEMBL: 5854 GeneCards: ADCY10 Gene
EC number	4.6.1.1
Gene ontology Molecular function • magnesium ion binding • adenylate cyclase activity • ATP binding • manganese ion binding • ATPase binding Cellular component • cytoplasm • cytosol • cytoskeleton • plasma membrane • axon • dendrite • growth cone • neuronal cell body • apical part of cell • basal part of cell • perinuclear region of cytoplasm Biological process • cAMP biosynthetic process • spermatogenesis • intracellular signal transduction • positive regulation of apoptotic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	55811	271639
Ensembl	ENSG00000143199	ENSMUSG00000026567
UniProt	Q96PN6	Q8C0T9
RefSeq (mRNA)	NM_001167749	NM_173029
RefSeq (protein)	NP_001161221	NP_766617
Location (UCSC)	Chr 1: 167.81 – 167.91 Mb	Chr 1: 165.49 – 165.58 Mb
PubMed search

Adenylyl cyclase 10 also known as ADCY10 is an enzyme that, in humans, is encoded by the ADCY10 gene.^[1]

Function

The protein encoded by this gene belongs to a distinct class of mammalian adenylyl cyclase that is soluble and insensitive to G protein or forskolin regulation. It is localized in the cytoplasm and is thought to function as a general bicarbonate sensor throughout the body. It may also play an important role in the generation of cAMP in spermatozoa, implying possible roles in sperm maturation through the epididymis, capacitation, hypermotility, and/or the acrosome reaction.^[2]

Clinical significance

Mutations in the ADCY10 gene are associated with an increased risk of adsorptive hypercalciuria.^[1]

References

1. Reed BY, Heller HJ, Gitomer WL, Pak CY (November 1999). "Mapping a gene defect in absorptive hypercalciuria to chromosome 1q23.3-q24". J. Clin. Endocrinol. Metab. 84 (11): 3907–13. doi:10.1210/jc.84.11.3907. PMID 10566627.
2. "Entrez Gene: ADCY10".

Further reading

• Wuttke MS, Buck J, Levin LR (2002). "Bicarbonate-regulated soluble adenylyl cyclase.". JOP 2 (4 Suppl): 154–8. PMID 11875252.
• Hukovic N, Panetta R, Kumar U; et al. (1998). "The cytoplasmic tail of the human somatostatin receptor type 5 is crucial for interaction with adenylyl cyclase and in mediating desensitization and internalization.". J. Biol. Chem. 273 (33): 21416–22. doi:10.1074/jbc.273.33.21416. PMID 9694905.
• Buck J, Sinclair ML, Schapal L; et al. (1999). "Cytosolic adenylyl cyclase defines a unique signaling molecule in mammals". Proc. Natl. Acad. Sci. U.S.A. 96 (1): 79–84. doi:10.1073/pnas.96.1.79. PMC 15096. PMID 9874775.
• Hayes JS, Lawler OA, Walsh MT, Kinsella BT (1999). "The prostacyclin receptor is isoprenylated. Isoprenylation is required for efficient receptor-effector coupling". J. Biol. Chem. 274 (34): 23707–18. doi:10.1074/jbc.274.34.23707. PMID 10446129.
• Sinclair ML, Wang XY, Mattia M; et al. (2000). "Specific expression of soluble adenylyl cyclase in male germ cells". Mol. Reprod. Dev. 56 (1): 6–11. doi:10.1002/(SICI)1098-2795(200005)56:1<6::AID-MRD2>3.0.CO;2-M. PMID 10737962.
• Chen Y, Cann MJ, Litvin TN; et al. (2000). "Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor". Science 289 (5479): 625–8. doi:10.1126/science.289.5479.625. PMID 10915626.
• Jaiswal BS, Conti M (2001). "Identification and functional analysis of splice variants of the germ cell soluble adenylyl cyclase". J. Biol. Chem. 276 (34): 31698–708. doi:10.1074/jbc.M011698200. PMID 11423534.
• Reed BY, Gitomer WL, Heller HJ; et al. (2002). "Identification and characterization of a gene with base substitutions associated with the absorptive hypercalciuria phenotype and low spinal bone density". J. Clin. Endocrinol. Metab. 87 (4): 1476–85. doi:10.1210/jc.87.4.1476. PMID 11932268.
• Zippin JH, Chen Y, Nahirney P; et al. (2003). "Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains". FASEB J. 17 (1): 82–4. doi:10.1096/fj.02-0598fje. PMID 12475901.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Litvin TN, Kamenetsky M, Zarifyan A; et al. (2003). "Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate". J. Biol. Chem. 278 (18): 15922–6. doi:10.1074/jbc.M212475200. PMID 12609998.
• Jaiswal BS, Conti M (2003). "Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa". Proc. Natl. Acad. Sci. U.S.A. 100 (19): 10676–81. doi:10.1073/pnas.1831008100. PMC 196863. PMID 12958208.
• Marjanovic JA, Li Z, Stojanovic A, Du X (2006). "Stimulatory roles of nitric-oxide synthase 3 and guanylyl cyclase in platelet activation". J. Biol. Chem. 280 (45): 37430–8. doi:10.1074/jbc.M506518200. PMID 16144836.
• Schmid A, Sutto Z, Nlend MC; et al. (2007). "Soluble Adenylyl Cyclase Is Localized to Cilia and Contributes to Ciliary Beat Frequency Regulation via Production of cAMP". J. Gen. Physiol. 130 (1): 99–109. doi:10.1085/jgp.200709784. PMC 2154360. PMID 17591988.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.