RIC19_CAEEL
ID RIC19_CAEEL Reviewed; 430 AA.
AC P91124;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Resistance to inhibitors of cholinesterase protein 19;
DE AltName: Full=ICA1 homolog;
GN Name=ric-19 {ECO:0000312|WormBase:C32E8.7};
GN ORFNames=C32E8.7 {ECO:0000312|WormBase:C32E8.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11029035; DOI=10.1091/mbc.11.10.3277;
RA Pilon M., Peng X.-R., Spence A.M., Plasterk R.H.A., Dosch H.-M.;
RT "The diabetes autoantigen ICA69 and its Caenorhabditis elegans homologue,
RT ric-19, are conserved regulators of neuroendocrine secretion.";
RL Mol. Biol. Cell 11:3277-3288(2000).
RN [3]
RP FUNCTION, INTERACTION WITH TBC-8, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22654674; DOI=10.1371/journal.pgen.1002722;
RA Hannemann M., Sasidharan N., Hegermann J., Kutscher L.M., Koenig S.,
RA Eimer S.;
RT "TBC-8, a putative RAB-2 GAP, regulates dense core vesicle maturation in
RT Caenorhabditis elegans.";
RL PLoS Genet. 8:e1002722-e1002722(2012).
RN [4]
RP INTERACTION WITH RUND-1.
RX PubMed=24698274; DOI=10.1016/j.neuron.2014.02.017;
RA Ailion M., Hannemann M., Dalton S., Pappas A., Watanabe S., Hegermann J.,
RA Liu Q., Han H.F., Gu M., Goulding M.Q., Sasidharan N., Schuske K.,
RA Hullett P., Eimer S., Jorgensen E.M.;
RT "Two Rab2 interactors regulate dense-core vesicle maturation.";
RL Neuron 82:167-180(2014).
CC -!- FUNCTION: May be involved in neurotransmitter secretion
CC (PubMed:11029035). In association with the GTPase activator protein
CC tbc-8 activates rab-2 during dense core vesicle maturation in
CC cholinergic motoneurons (PubMed:22654674).
CC {ECO:0000269|PubMed:11029035, ECO:0000269|PubMed:22654674}.
CC -!- SUBUNIT: Interacts with the GTPase activator protein tbc-8; the
CC interaction is direct and may be required for the activation of rab-2
CC and dense vesicle maturation in cholinergic motoneurons
CC (PubMed:22654674). Interacts with rund-1 (PubMed:24698274).
CC {ECO:0000269|PubMed:22654674, ECO:0000269|PubMed:24698274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11029035}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:22654674}; Peripheral
CC membrane protein {ECO:0000269|PubMed:22654674}. Note=Co-localizes with
CC tbc-8 at cytoplasmic vesicle membranes in neurons.
CC {ECO:0000269|PubMed:22654674}.
CC -!- TISSUE SPECIFICITY: Expressed in all neurons (PubMed:11029035,
CC PubMed:22654674). Highly expressed in m2 pharyngeal neurons and some
CC pharyngeal interneurons (PubMed:11029035). Also expressed in the
CC excretory canal and the gland cells located just below the nerve ring
CC in the head (PubMed:11029035). {ECO:0000269|PubMed:11029035,
CC ECO:0000269|PubMed:22654674}.
CC -!- DISRUPTION PHENOTYPE: Mutants are resistant to aldicarb, an inhibitor
CC of acetylcholinesterase. {ECO:0000269|PubMed:11029035}.
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DR EMBL; BX284601; CCD66406.1; -; Genomic_DNA.
DR PIR; T25595; T25595.
DR RefSeq; NP_491216.2; NM_058815.4.
DR AlphaFoldDB; P91124; -.
DR BioGRID; 56251; 3.
DR STRING; 6239.C32E8.7; -.
DR iPTMnet; P91124; -.
DR EPD; P91124; -.
DR PaxDb; P91124; -.
DR PeptideAtlas; P91124; -.
DR EnsemblMetazoa; C32E8.7.1; C32E8.7.1; WBGene00004368.
DR GeneID; 191757; -.
DR KEGG; cel:CELE_C32E8.7; -.
DR UCSC; C32E8.7; c. elegans.
DR CTD; 191757; -.
DR WormBase; C32E8.7; CE39089; WBGene00004368; ric-19.
DR eggNOG; KOG3891; Eukaryota.
DR GeneTree; ENSGT00390000005530; -.
DR HOGENOM; CLU_037158_2_1_1; -.
DR InParanoid; P91124; -.
DR OMA; YVLTHYQ; -.
DR OrthoDB; 766523at2759; -.
DR PhylomeDB; P91124; -.
DR PRO; PR:P91124; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004368; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:1990502; P:dense core granule maturation; IMP:WormBase.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IGI:WormBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:0051049; P:regulation of transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR010504; AH_dom.
DR InterPro; IPR024114; Islet_autoAg_Ica1/Ica1-like.
DR PANTHER; PTHR10164; PTHR10164; 1.
DR Pfam; PF06456; Arfaptin; 1.
DR SMART; SM01015; Arfaptin; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS50870; AH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Membrane; Neurotransmitter transport;
KW Reference proteome; Transport.
FT CHAIN 1..430
FT /note="Resistance to inhibitors of cholinesterase protein
FT 19"
FT /id="PRO_0000097331"
FT DOMAIN 56..260
FT /note="AH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00294"
FT REGION 279..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48906 MW; E238258E3389349A CRC64;
MAAQFYERNT SGMNADRFMT RLTDESTVNT MQRHYWTARQ FIRTKLGKKE DEHLEASDNE
LDTCLNLYRS VHGTSFQLLN NVDNYANFLL DETLVQNVLG KYLKEKGKID KTEAVGRILI
AVGRSLLFSS HRLNAARIGV STFYNKLSVF VERAIGDCSQ TIEAVQMCRT EYRGSLLWMK
KTSEELDPEV DGSMEKFREA QTTVKSNKER LDRLKTDTLQ KVDLLSASRS NLLSYVLTHY
QNELYEYYSK TSRAFETLAE NINCYNNYDF EILSHLATGT KPERERKSEK EESAKTSQPR
GNEEELKNLL FGRESPQFGE EEVQDESRSQ CDSPLIEDVD DERRKTGDLL DLESAASIAF
PIGPLATLFD TSSFVPPILP PPKPNAVSDD ILSLFDGNKA NSSGKEASAT TMDWQSLIDG
FDRENEDNLL
