UNC18_CAEEL
ID UNC18_CAEEL Reviewed; 673 AA.
AC P34815; Q26333; Q7JNZ2; Q7Z293;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Putative acetylcholine regulator unc-18;
DE AltName: Full=Uncoordinated protein 18;
GN Name=unc-18; Synonyms=lan-2; ORFNames=F27D9.1;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=1347782; DOI=10.1111/j.1471-4159.1992.tb11373.x;
RA Hosono R., Hekimi S., Kamiya Y., Sassa T., Murakami S., Nishiwaki K.,
RA Miwa J., Taketo A., Kodaira K.;
RT "The unc-18 gene encodes a novel protein affecting the kinetics of
RT acetylcholine metabolism in the nematode Caenorhabditis elegans.";
RL J. Neurochem. 58:1517-1525(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=8398155; DOI=10.1016/0896-6273(93)90080-b;
RA Gengyo-Ando K., Kamiya Y., Yamakawa A., Kodaira K., Nishiwaki K., Miwa J.,
RA Hori I., Hosono R.;
RT "The C. elegans unc-18 gene encodes a protein expressed in motor neurons.";
RL Neuron 11:703-711(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [4]
RP FUNCTION.
RX PubMed=17891142; DOI=10.1038/nn1981;
RA Van Buskirk C., Sternberg P.W.;
RT "Epidermal growth factor signaling induces behavioral quiescence in
RT Caenorhabditis elegans.";
RL Nat. Neurosci. 10:1300-1307(2007).
CC -!- FUNCTION: May participate in the axonal transport system and influences
CC the acetylcholine flow in motor neurons (PubMed:1347782,
CC PubMed:8398155). Probably by regulating neuronal transmission
CC downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and
CC upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the
CC decrease in pharyngeal pumping during the quiescent state that precedes
CC each larval molt (PubMed:17891142). {ECO:0000269|PubMed:1347782,
CC ECO:0000269|PubMed:17891142, ECO:0000269|PubMed:8398155}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c;
CC IsoId=P34815-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P34815-2; Sequence=VSP_020989, VSP_020990;
CC Name=b;
CC IsoId=P34815-3; Sequence=VSP_020989, VSP_020990, VSP_020991,
CC VSP_020992;
CC -!- TISSUE SPECIFICITY: Motor neurons and a limited number of neurons
CC constituting nerve ganglia. {ECO:0000269|PubMed:1347782,
CC ECO:0000269|PubMed:8398155}.
CC -!- DEVELOPMENTAL STAGE: Abundant at the early larval stage, decreased
CC amounts seen at the fourth larval and the adult stages.
CC {ECO:0000269|PubMed:1347782}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; S34207; AAB21818.1; -; Genomic_DNA.
DR EMBL; S66176; AAB28570.1; -; mRNA.
DR EMBL; FO080935; CCD67914.1; -; Genomic_DNA.
DR EMBL; FO080935; CCD67915.1; -; Genomic_DNA.
DR EMBL; FO080935; CCD67916.1; -; Genomic_DNA.
DR PIR; S36747; S36747.
DR RefSeq; NP_001024606.1; NM_001029435.3. [P34815-2]
DR AlphaFoldDB; P34815; -.
DR SMR; P34815; -.
DR BioGRID; 45954; 31.
DR STRING; 6239.F27D9.1c; -.
DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR EPD; P34815; -.
DR PaxDb; P34815; -.
DR PeptideAtlas; P34815; -.
DR PRIDE; P34815; -.
DR EnsemblMetazoa; F27D9.1a.1; F27D9.1a.1; WBGene00006757. [P34815-2]
DR GeneID; 181030; -.
DR KEGG; cel:CELE_F27D9.1; -.
DR UCSC; F27D9.1c; c. elegans. [P34815-1]
DR CTD; 181030; -.
DR WormBase; F27D9.1a; CE24927; WBGene00006757; unc-18. [P34815-2]
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000155127; -.
DR InParanoid; P34815; -.
DR OMA; RNQYKCA; -.
DR OrthoDB; 725424at2759; -.
DR PhylomeDB; P34815; -.
DR Reactome; R-CEL-114516; Disinhibition of SNARE formation.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-449836; Other interleukin signaling.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR PRO; PR:P34815; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006757; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:WormBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0016081; P:synaptic vesicle docking; IMP:WormBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Protein transport; Reference proteome; Transport.
FT CHAIN 1..673
FT /note="Putative acetylcholine regulator unc-18"
FT /id="PRO_0000206293"
FT VAR_SEQ 1..9
FT /note="MQNVKHSYL -> MSLKQIVGH (in isoform a and isoform b)"
FT /evidence="ECO:0000303|PubMed:8398155"
FT /id="VSP_020989"
FT VAR_SEQ 10..91
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000303|PubMed:8398155"
FT /id="VSP_020990"
FT VAR_SEQ 166..175
FT /note="IDKLIQDYCA -> VSFNLQKSLV (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020991"
FT VAR_SEQ 176..673
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020992"
SQ SEQUENCE 673 AA; 76733 MW; 20ADAD67642FA054 CRC64;
MQNVKHSYLA CSSSSCCQFF SLFLSLCHAE HQIQTLSPSF AYTLLIFALL VSDKSEIALL
SRHTHTYIFL PISSVHPSLE LLPFVVFMHM RKLLNDVIRP LKKGDGRSAW NVLIVDTLAM
RMLSSCCKMH NIMEEGITIV EDLNKRREPL PTLEAIYLIA PTAESIDKLI QDYCARNLYK
CAHVFFTEAC SDQLFSTLSK SAAARFIKTL KEINIAFTPY ESQVFNLDSP DTFFLYYNAQ
KQGGLTSNLE RIAEQIATVC ATLGEYPSLR YRADFERNVE LGHLVEQKLD AYKADDPSMG
EGADKARSQL IIIDRGYDAI TPLLHELTLQ AMCYDLLGIE NDVYKYETGG SDENLEKEVL
LDENDDLWVE MRHKHIAVVS QEVTKNLKKF SESKGNKGTM DSKSIKDLSM LIKRMPQHKK
ELNKFSTHIS LAEECMKQYQ QGVDKLCKVE QDLSTGIDAE GERVRDAMKL MVPLLIDPAV
RCEDRLRLIL LYILSKNGIT DENLNKLLQH ANISMADKET ITNAAYLGLN IVTDTGRKKT
WTPTKKERPH EQVYQSSRWV PVIKDIIEDA IDERLDTKHF PFLAGRQVNQ GYRAPASARY
GQWHKERGQQ SNYRSGPRLI IYIIGGVTFS EMRACYEVTA ARKPWEVVIG SDRIITPDKF
LTNLRDLNKP RDI
