AEX4_CAEEL
ID AEX4_CAEEL Reviewed; 234 AA.
AC G5EEN8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=t-SNARE protein aex-4 {ECO:0000305};
DE AltName: Full=Aboc, expulsion defective protein 4 {ECO:0000312|WormBase:T14G12.2};
GN Name=aex-4 {ECO:0000312|WormBase:T14G12.2};
GN Synonyms=tag-81 {ECO:0000312|WormBase:T14G12.2};
GN ORFNames=T14G12.2 {ECO:0000312|WormBase:T14G12.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:ACI04533.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18852466; DOI=10.1073/pnas.0803617105;
RA Mahoney T.R., Luo S., Round E.K., Brauner M., Gottschalk A., Thomas J.H.,
RA Nonet M.L.;
RT "Intestinal signaling to GABAergic neurons regulates a rhythmic behavior in
RT Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16350-16355(2008).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
CC -!- FUNCTION: t-SNARE protein which regulates the secretion of aex-5 from
CC intestinal cells. Involved in the defecation motor program, which is a
CC coordinated series of three muscle contractions that occurs every 45
CC seconds. {ECO:0000269|PubMed:18852466}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18852466}.
CC -!- TISSUE SPECIFICITY: Expressed in intestinal cells.
CC {ECO:0000269|PubMed:18852466}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defecation
CC abnormalities. {ECO:0000269|PubMed:18852466}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; FJ165552; ACI04533.1; -; mRNA.
DR EMBL; BX284606; CCD62368.1; -; Genomic_DNA.
DR PIR; T16877; T16877.
DR RefSeq; NP_508641.2; NM_076240.6.
DR AlphaFoldDB; G5EEN8; -.
DR SMR; G5EEN8; -.
DR STRING; 6239.T14G12.2; -.
DR PaxDb; G5EEN8; -.
DR EnsemblMetazoa; T14G12.2.1; T14G12.2.1; WBGene00006454.
DR GeneID; 188509; -.
DR KEGG; cel:CELE_T14G12.2; -.
DR CTD; 188509; -.
DR WormBase; T14G12.2; CE35769; WBGene00006454; aex-4.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_1416344_0_0_1; -.
DR InParanoid; G5EEN8; -.
DR OMA; CDTIEDE; -.
DR OrthoDB; 1701546at2759; -.
DR PhylomeDB; G5EEN8; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013026; RHOB GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR PRO; PR:G5EEN8; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006454; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:2000294; P:positive regulation of defecation; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:2000292; P:regulation of defecation; IGI:UniProtKB.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS50192; T_SNARE; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Membrane; Reference proteome; Repeat.
FT CHAIN 1..234
FT /note="t-SNARE protein aex-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438190"
FT DOMAIN 37..99
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 170..232
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
SQ SEQUENCE 234 AA; 27098 MW; 966A99FC7E677E92 CRC64;
MARKTIDSIP EPIALPTEET VQKRIKLKMV DLDAEIAKLN VQSLDSSIQM IRDIDQMNVD
AVQTTAALED QDEQLDKIEA NLSNVIDDLN VVSHNITAME HYCGCGFFRI LRAPFKYFRK
RERDIIKEEV LEKMTSPKLR RKEESNMMMF TNSSKRREST GDFMKRLTCD AIEDELERNL
MQIDQGLESV KNLAVDMHVQ LKLQEPKLNR IEELTETNDF VVEGVNDKVK KLLH
