AEX1_CAEEL
ID AEX1_CAEEL Reviewed; 1009 AA.
AC G5EEU3;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=C2 domain-containing protein aex-1 {ECO:0000305};
GN Name=aex-1 {ECO:0000303|PubMed:2323555, ECO:0000312|WormBase:D2030.10a};
GN ORFNames=D2030.10 {ECO:0000312|WormBase:D2030.10a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAL82897.1};
RN [1] {ECO:0000312|EMBL:AAL82897.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11804572; DOI=10.1016/s0896-6273(01)00587-6;
RA Doi M., Iwasaki K.;
RT "Regulation of retrograde signaling at neuromuscular junctions by the novel
RT C2 domain protein AEX-1.";
RL Neuron 33:249-259(2002).
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).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2323555; DOI=10.1093/genetics/124.4.855;
RA Thomas J.H.;
RT "Genetic analysis of defecation in Caenorhabditis elegans.";
RL Genetics 124:855-872(1990).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19028454; DOI=10.1016/j.bbrc.2008.11.064;
RA Yamashita M., Iwasaki K., Doi M.;
RT "The non-neuronal syntaxin SYN-1 regulates defecation behavior and neural
RT activity in C. elegans through interaction with the Munc13-like protein
RT AEX-1.";
RL Biochem. Biophys. Res. Commun. 378:404-408(2009).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25849533; DOI=10.1371/journal.pone.0124515;
RA Sheng M., Hosseinzadeh A., Muralidharan S.V., Gaur R., Selstam E., Tuck S.;
RT "Aberrant fat metabolism in Caenorhabditis elegans mutants with defects in
RT the defecation motor program.";
RL PLoS ONE 10:E0124515-E0124515(2015).
CC -!- FUNCTION: Involved in retrograde signaling from post-synaptic cells to
CC pre-synaptic neurons, probably by regulating vesicle exocytosis in
CC post-synaptic cells (PubMed:11804572, PubMed:2323555, PubMed:19028454).
CC Acts in muscles, to regulate the localization of synaptic vesicle
CC fusion protein unc-13 likely during vesicle exocytosis and thus
CC regulate retrograde signaling at the neuromuscular junction (NMJ)
CC (PubMed:11804572). Regulates anterior body muscle contractions (aBOC)
CC and the expulsion steps during the defecation motor program (DMP)
CC (PubMed:11804572, PubMed:2323555, PubMed:19028454). Probably by
CC regulating DMP, plays a homeostatic role in the uptake of triglycerides
CC (PubMed:25849533). Regulates locomotion (PubMed:11804572).
CC {ECO:0000269|PubMed:11804572, ECO:0000269|PubMed:19028454,
CC ECO:0000269|PubMed:2323555, ECO:0000269|PubMed:25849533}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, body wall muscles and some
CC amphid neurons. {ECO:0000269|PubMed:11804572}.
CC -!- DISRUPTION PHENOTYPE: Severely constipated due to absent or weak
CC anterior body muscle (aBOC) and intestinal contractions during the
CC defecation cycle (PubMed:11804572, PubMed:2323555). Reduced uptake and
CC accumulation of triglycerides (PubMed:25849533). Locomotion defects
CC characterized by mild body thrashing (PubMed:11804572). Partially
CC resistant to paralysis induced by acetylcholine esterase inhibitor
CC aldicarb (PubMed:2323555, PubMed:19028454). Reduced enrichment of unc-
CC 13 at presynaptic active sites of neuromuscular junctions
CC (PubMed:11804572). {ECO:0000269|PubMed:11804572,
CC ECO:0000269|PubMed:19028454, ECO:0000269|PubMed:2323555,
CC ECO:0000269|PubMed:25849533}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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DR EMBL; AF324832; AAL82897.1; -; mRNA.
DR EMBL; BX284601; CAA98122.2; -; Genomic_DNA.
DR PIR; T20361; T20361.
DR RefSeq; NP_740891.1; NM_170901.3.
DR AlphaFoldDB; G5EEU3; -.
DR STRING; 6239.D2030.10a; -.
DR PaxDb; G5EEU3; -.
DR EnsemblMetazoa; D2030.10a.1; D2030.10a.1; WBGene00000084.
DR GeneID; 172519; -.
DR KEGG; cel:CELE_D2030.10; -.
DR CTD; 172519; -.
DR WormBase; D2030.10a; CE30740; WBGene00000084; aex-1.
DR eggNOG; ENOG502T2S0; Eukaryota.
DR GeneTree; ENSGT00730000110939; -.
DR HOGENOM; CLU_297037_0_0_1; -.
DR InParanoid; G5EEU3; -.
DR OMA; TACESEV; -.
DR OrthoDB; 204670at2759; -.
DR PhylomeDB; G5EEU3; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EEU3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000084; Expressed in adult organism and 2 other tissues.
DR ExpressionAtlas; G5EEU3; baseline and differential.
DR GO; GO:0070382; C:exocytic vesicle; ISS:WormBase.
DR GO; GO:0099503; C:secretory vesicle; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0060179; P:male mating behavior; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0014057; P:positive regulation of acetylcholine secretion, neurotransmission; IMP:WormBase.
DR GO; GO:2000294; P:positive regulation of defecation; IMP:UniProtKB.
DR GO; GO:1904731; P:positive regulation of intestinal lipid absorption; IMP:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; IMP:UniProtKB.
DR GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 2: Evidence at transcript level;
KW Exocytosis; Reference proteome.
FT CHAIN 1..1009
FT /note="C2 domain-containing protein aex-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439619"
FT DOMAIN 812..945
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
SQ SEQUENCE 1009 AA; 117153 MW; A042D9897BC0A626 CRC64;
MREEALESIC AALSISFTED PDHLESIIDR FSEIFKVKDH LNQLRKKCEK FQTFTLEIRP
VGSSNCTENV YAYIIESETC RQLELKPTGT TKLEIGSDKN VSLKFGLSQK KDSTTSKKGL
SRSASLLKKL KFSDKKNLDE LKISIFPLDI AVRKNINLGS GKSTLLEMKL IRNDHRNMIQ
CLEFDDFLEM TRSFHEWQAQ ISESELYDGS LGDPTFSMFY SIAFFFEIPS FVLKLTEMTC
FLVWDDEMKK LDERALADVS LKMTACESEV DLQHPLLSPA LSYLNDCTCN TIRCILVPFS
TEPFFPPVSP SRLKSINVAL KLIADICVLD VWDEFENLAN PSNFLSSELK KLLESSAERY
GESLKKQEFN ELCRTILNLW MSLSNESQPY YIFFHQFDIN YIGAAMLKLD KYLAESIQIS
LKCQLDLLNL RIPTELENFT KTTMRLFVTL RNLLNMVEAF HLPECQLFHF EEWFTDISVF
WTYSWREVTL QMVERTITLD EDGDSVKYGA RRPLPAGLYS FLCIQKGISD DLARLEFTFP
HHLVVCAASV VNIMCQNINA YARKLFSEAM RNHEEKASRL VRATNGIEQA MCFVEEGYRR
FAQFQRLEEY VDVDDLSAVR STSIRLLKST RDTCEIQVST LLSHFVNLKT DIVLKIAKNL
CADGKESNSG LKSYMRELAS SERIESILEC CYGLVDDVRC LLLPNCFKLS TQHFATSLEQ
QIRKNIRQKQ PAEYYSNIYV GFLNILIFKR LKQMYLKFQI ALKYIYEFLE IEDRKDIELL
SNLHLNSFST KDLILSYYDS LCEKIDRTRF GNAPHVDVHI SYVKMVDEDT ISIQIKLIKM
SPIEWIDVIS DRVDYFVRLE LFPKILFPSN KFESPTTNPM PQSTRPQWKQ LFEIRVPLEC
FFLRGACLAI SVFDHERFID RLVGRGFISL HSVPQASEEK PTQRLQVPLL PNDFSDQNNV
FYQLLKTRAC RDSIAKEFIE TRTRRHQRIR ALQHYIRINR NRVGHMLLG
