RIMS1

Regulating synaptic membrane exocytosis protein 1 is a protein that in humans is encoded by the RIMS1 gene.[3][4][5]

RIMS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2CSS
Identifiers
Aliases	RIMS1, CORD7, RAB3IP2, RIM, RIM1, regulating synaptic membrane exocytosis 1
External IDs	OMIM: 606629 MGI: 2152971 HomoloGene: 128399 GeneCards: RIMS1
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0005083 GTPase regulator activity • metal ion binding • Rab GTPase binding • GO:0001948 protein binding • ion channel binding • RNA binding Cellular component • cytosol • membrane • cell membrane • synapse • presynaptic active zone • cell junction • presynaptic membrane • cytoskeleton of presynaptic active zone • presynaptic active zone cytoplasmic component Biological process • cell differentiation • response to stimulus • synaptic vesicle exocytosis • positive regulation of inhibitory postsynaptic potential • Lipid bilayer fusion • regulation of neurotransmitter secretion • secretion • glutamate secretion • positive regulation of gene expression • positive regulation of excitatory postsynaptic potential • positive regulation of dendrite extension • regulated exocytosis • intracellular protein transport • neurotransmitter transport • GO:0010554 neurotransmitter secretion • visual perception • calcium ion regulated exocytosis • exocytosis • GO:0048552 regulation of catalytic activity • regulation of membrane potential • calcium ion-regulated exocytosis of neurotransmitter • regulation of synaptic vesicle exocytosis • transport • regulation of synaptic plasticity • positive regulation of synaptic transmission • macromolecular complex assembly • acrosomal vesicle exocytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	22999	116837
Ensembl	n/a	n/a
UniProt	Q86UR5	Q99NE5
RefSeq (mRNA)	NM_001168407 NM_001168408 NM_001168409 NM_001168410 NM_001168411 NM_014989	NM_001012623 NM_001012624 NM_001012625 NM_053270 NM_183018
RefSeq (protein)	NP_001161879 NP_001161880 NP_001161881 NP_001161882 NP_001161883 NP_055804 NP_001337340 NP_001337341 NP_001337342 NP_001337343 NP_001337344 NP_001337345 NP_001337346 NP_001337347 NP_001337348 NP_001337349 NP_001337350 NP_001337351 NP_001337352 NP_001337353 NP_001337354 NP_001337355 NP_001337356 NP_001337357 NP_001337358 NP_001337359 NP_001337360 NP_001337361 NP_001337362 NP_001337363 NP_001337364 NP_001337365 NP_001337366 NP_001337367 NP_001337368 NP_001337369 NP_001337370 NP_001337371 NP_001337372 NP_001337373 NP_001337374 NP_001337375 NP_001337376 NP_001337377 NP_001337378 NP_001337379 NP_001337381 NP_001337383 NP_001337384 NP_001337385 NP_001337386 NP_001337387 NP_001337388 NP_001337389 NP_001337390 NP_001337391 NP_001337392 NP_001337393 NP_001337394 NP_001337395 NP_001337396 NP_001337397 NP_001337398 NP_001337399 NP_001337400 NP_001337401 NP_001337402 NP_001337403	NP_001012641 NP_001012642 NP_001012643 NP_444500 NP_898839
Location (UCSC)	n/a	n/a
PubMed search	[1]	[2]
Wikidata
View/Edit Human View/Edit Mouse

Function

RAB3A (MIM 179490), a member of the Ras superfamily of genes, is a synaptic vesicle protein that regulates synaptic vesicle exocytosis. MUNC13 (UNC13; MIM 605836) and its isoforms are required for priming synaptic vesicles for exocytosis. The RIM family of active zone proteins likely function as protein scaffolds that help regulate vesicle exocytosis during short-term plasticity.[supplied by OMIM][5]

Interactions

RIMS1 has been shown to interact with:

• ERC2,[6][7]
• RAB3A,[8][9]
• UNC13A,[10]
• UNC13B,[6][8] and
• YWHAH.[11]

References

1. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
2. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (September 1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
4. Coppola T, Magnin-Luthi S, Perret-Menoud V, Gattesco S, Schiavo G, Regazzi R (August 2001). "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin". J Biol Chem. 276 (35): 32756–62. doi:10.1074/jbc.M100929200. PMID 11438518.
5. "Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1".
6. Ohtsuka T, Takao-Rikitsu E, Inoue E, Inoue M, Takeuchi M, Matsubara K, Deguchi-Tawarada M, Satoh K, Morimoto K, Nakanishi H, Takai Y (August 2002). "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1". J. Cell Biol. 158 (3): 577–90. doi:10.1083/jcb.200202083. PMC 2173811. PMID 12163476.
7. Takao-Rikitsu E, Mochida S, Inoue E, Deguchi-Tawarada M, Inoue M, Ohtsuka T, Takai Y (January 2004). "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release". J. Cell Biol. 164 (2): 301–11. doi:10.1083/jcb.200307101. PMC 2172332. PMID 14734538.
8. Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/s0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654.
9. Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
10. "Protein unc-13 homolog A". UniProt.
11. Sun L, Bittner MA, Holz RW (October 2003). "Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus". J. Biol. Chem. 278 (40): 38301–9. doi:10.1074/jbc.M212801200. PMID 12871946.

Further reading

• Kelsell RE, Gregory-Evans K, Gregory-Evans CY, Holder GE, Jay MR, Weber BH, Moore AT, Bird AC, Hunt DM (1998). "Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q". Am. J. Hum. Genet. 63 (1): 274–9. doi:10.1086/301905. PMC 1377229. PMID 9634506.
• Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/S0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654.
• Liu X, Schrager JA, Lange GD, Marsh JW (2001). "HIV Nef-mediated cellular phenotypes are differentially expressed as a function of intracellular Nef concentrations". J. Biol. Chem. 276 (35): 32763–70. doi:10.1074/jbc.M101025200. PMID 11438519.
• Daiho T, Yamasaki K, Saino T, Kamidochi M, Satoh K, Iizuka H, Suzuki H (2001). "Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond". J. Biol. Chem. 276 (35): 32771–8. doi:10.1074/jbc.M101229200. PMID 11438520.
• Tsuji M, Inanami O, Kuwabara M (2001). "Induction of neurite outgrowth in PC12 cells by alpha -phenyl-N-tert-butylnitron through activation of protein kinase C and the Ras-extracellular signal-regulated kinase pathway". J. Biol. Chem. 276 (35): 32779–85. doi:10.1074/jbc.M101403200. PMID 11438521.
• Dierks H, Kolanus J, Kolanus W (2001). "Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain". J. Biol. Chem. 276 (40): 37472–81. doi:10.1074/jbc.M101502200. PMID 11438522.
• Schoch S, Castillo PE, Jo T, Mukherjee K, Geppert M, Wang Y, Schmitz F, Malenka RC, Südhof TC (2002). "RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone". Nature. 415 (6869): 321–6. doi:10.1038/415321a. PMID 11797009.
• Ohtsuka T, Takao-Rikitsu E, Inoue E, Inoue M, Takeuchi M, Matsubara K, Deguchi-Tawarada M, Satoh K, Morimoto K, Nakanishi H, Takai Y (2002). "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1". J. Cell Biol. 158 (3): 577–90. doi:10.1083/jcb.200202083. PMC 2173811. PMID 12163476.
• Wang Y, Liu X, Biederer T, Südhof TC (2002). "A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones". Proc. Natl. Acad. Sci. U.S.A. 99 (22): 14464–9. doi:10.1073/pnas.182532999. PMC 137906. PMID 12391317.
• Fukuda M (2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
• Wang Y, Südhof TC (2003). "Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins( small star, filled )". Genomics. 81 (2): 126–37. doi:10.1016/S0888-7543(02)00024-1. PMID 12620390.
• Johnson S, Halford S, Morris AG, Patel RJ, Wilkie SE, Hardcastle AJ, Moore AT, Zhang K, Hunt DM (2003). "Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7)". Genomics. 81 (3): 304–14. doi:10.1016/S0888-7543(03)00010-7. PMID 12659814.
• Sun L, Bittner MA, Holz RW (2003). "Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus". J. Biol. Chem. 278 (40): 38301–9. doi:10.1074/jbc.M212801200. PMID 12871946.
• Takao-Rikitsu E, Mochida S, Inoue E, Deguchi-Tawarada M, Inoue M, Ohtsuka T, Takai Y (2004). "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release". J. Cell Biol. 164 (2): 301–11. doi:10.1083/jcb.200307101. PMC 2172332. PMID 14734538.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Barragan I, Marcos I, Borrego S, Antiñolo G (2005). "Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa". Ophthalmic Res. 37 (2): 89–93. doi:10.1159/000084250. PMID 15746564.
• Sisodiya SM, Thompson PJ, Need A, Harris SE, Weale ME, Wilkie SE, Michaelides M, Free SL, Walley N, Gumbs C, Gerrelli D, Ruddle P, Whalley LJ, Starr JM, Hunt DM, Goldstein DB, Deary IJ, Moore AT (2007). "Genetic enhancement of cognition in a kindred with cone–rod dystrophy due to RIMS1 mutation". J. Med. Genet. 44 (6): 373–80. doi:10.1136/jmg.2006.047407. PMC 2740882. PMID 17237123.