DOC2B

Double C2-like domains, beta
Identifiers
Symbols	DOC2B;
External IDs	OMIM: 604568 MGI: 1100497 HomoloGene: 20796 GeneCards: DOC2B Gene
Gene Ontology Molecular function • transporter activity • calcium-dependent phospholipid binding • syntaxin binding Cellular component • cytoplasm • plasma membrane • synaptic vesicle • SNARE complex Biological process • exocytosis • protein localization • positive regulation of vesicle fusion • positive regulation of insulin secretion • positive regulation of calcium ion-dependent exocytosis • calcium ion-dependent exocytosis of neurotransmitter Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8447	13447
Ensembl	n/a	ENSMUSG00000020848
UniProt	Q14184	Q5SS41
RefSeq (mRNA)	NM_003585	NM_007873.2
RefSeq (protein)	NP_003576	NP_031899.2
Location (UCSC)	n/a	Chr 11: 75.58 – 75.61 Mb
PubMed search	[1]	[2]

Double C2-like domain-containing protein beta is a protein that in humans is encoded by the DOC2B gene.^[1][2]

There are at least two protein isoforms of the Double C2 protein, namely alpha (DOC2A) and beta (DOC2B), which contain two C2-like domains. DOC2A and DOC2B are encoded by different genes; these genes are at times confused with the unrelated DAB2 gene which was initially named DOC-2. Doc2b enhances Ca(2+)-dependent exocytosis in adipocytes,^[3] chromaffin cells of the adrenal gland^[4] and beta cells in the pancreas.^[5] In the central nervous system, Doc2b contributes to the spontaneous release of neurotransmitters by acting as a high-affinity Ca(2+) sensor for exocytosis of synaptic vesicles^[6]

References

1. ^ Orita S, Sasaki T, Naito A, Komuro R, Ohtsuka T, Maeda M, Suzuki H, Igarashi H, Takai Y (Feb 1995). "Doc2: a novel brain protein having two repeated C2-like domains". Biochem Biophys Res Commun 206 (2): 439–48. doi:10.1006/bbrc.1995.1062. PMID 7826360. 
2. ^ "Entrez Gene: DOC2B double C2-like domains, beta". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8447. 
3. ^ Fukuda N, Emoto M, Nakamori Y, Taguchi A, Miyamoto S, Uraki S, Oka Y, Tanizawa Y. (Feb 2009). "DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes". Diabetes 58 (2): 377–84. doi:10.2337/db08-0303. PMC 2628611. PMID 19033398. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2628611. 
4. ^ Friedrich R, Groffen AJ, Connell E, van Weering JR, Gutman O, Henis YI, Davletov B, Ashery U (Jul 2008). "DOC2B acts as a calcium switch and enhances vesicle fusion". J Neurosci 28 (27): 6794–806. doi:10.1523/JNEUROSCI.0538-08.2008. PMC 2673511. PMID 18596155. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2673511. 
5. ^ Miyazaki M, Emoto M, Fukuda N, Hatanaka M, Taguchi A, Miyamoto S, Tanizawa Y (Jul 2009). "DOC2b is a SNARE regulator of glucose-stimulated delayed insulin secretion". Biochem Biophys Res Commun 384 (4): 461–5. doi:10.1016/j.bbrc.2009.04.133. PMID 19410553. 
6. ^ Groffen AJ, Martens S, Díez Arazola R, Cornelisse LN, Lozovaya N, de Jong AP, Goriounova NA, Habets RL, Takai Y, Borst JG, Brose N, McMahon HT, Verhage M (Mar 2010). "Doc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter release". Science 327 (5973): 1614–8. doi:10.1126/science.1183765. PMC 2846320. PMID 20150444. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2846320. 

Further reading

• Cardoso C, Leventer RJ, Ward HL et al. (2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". Am. J. Hum. Genet. 72 (4): 918–30. doi:10.1086/374320. PMC 1180354. PMID 12621583. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1180354. 
• Duncan RR, Betz A, Shipston MJ et al. (1999). "Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo". J. Biol. Chem. 274 (39): 27347–50. doi:10.1074/jbc.274.39.27347. PMID 10488064. 
• Nagano F, Orita S, Sasaki T et al. (1998). "Interaction of Doc2 with tctex-1, a light chain of cytoplasmic dynein. Implication in dynein-dependent vesicle transport". J. Biol. Chem. 273 (46): 30065–8. doi:10.1074/jbc.273.46.30065. PMID 9804756. 
• Orita S, Naito A, Sakaguchi G et al. (1997). "Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery". J. Biol. Chem. 272 (26): 16081–4. doi:10.1074/jbc.272.26.16081. PMID 9195900. 
• Verhage M, de Vries KJ, Røshol H et al. (1997). "DOC2 proteins in rat brain: complementary distribution and proposed function as vesicular adapter proteins in early stages of secretion". Neuron 18 (3): 453–61. doi:10.1016/S0896-6273(00)81245-3. PMID 9115738. 
• Kojima T, Fukuda M, Aruga J, Mikoshiba K (1997). "Calcium-dependent phospholipid binding to the C2A domain of a ubiquitous form of double C2 protein (Doc2 beta)". J. Biochem. 120 (3): 671–6. PMID 8902635. 
• Sakaguchi G, Orita S, Maeda M et al. (1996). "Molecular cloning of an isoform of Doc2 having two C2-like domains". Biochem. Biophys. Res. Commun. 217 (3): 1053–61. doi:10.1006/bbrc.1995.2876. PMID 8554557. 

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