RIMS1

RIMS1

Available structures

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

Bgee

Human

Mouse (ortholog)

n/a

BioGPS


More reference expression data

Gene ontology
Molecular function	GTPase regulator activity metal ion binding protein binding transmembrane transporter binding RNA binding
Cellular component	cytosol membrane plasma 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 membrane 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 neurotransmitter secretion visual perception calcium-ion regulated exocytosis exocytosis 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 protein-containing complex assembly acrosomal vesicle exocytosis
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


22999


116837

Ensembl


ENSG00000079841


ENSMUSG00000041670

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

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

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

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]

Clinical significance

Mutations of the gene cause cone-rod dystrophy 7.

Interactions

RIMS1 has been shown to interact with:

References

^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1".
^ ^a ^b 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.
^ 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.
^ ^a ^b 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. S2CID 155875.
^ 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.
^ "Protein unc-13 homolog A". UniProt.
^ 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.

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. S2CID 155875.
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. Bibcode:2002Natur.415..321S. doi:10.1038/415321a. PMID 11797009. S2CID 4424128.
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. Bibcode:2002PNAS...9914464W. 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. Bibcode:2004PNAS..10112130B. 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. S2CID 25242611.
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.

v t e PDB gallery
1zub: Solution Structure of the RIM1alpha PDZ Domain in Complex with an ELKS1b C-terminal Peptide 2css: Solution structure of the PDZ domain of human KIAA0340 protein

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This page was last edited on 27 May 2022, at 12:55

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Function

Clinical significance

Interactions

References

Further reading