AEX2_CAEEL
ID AEX2_CAEEL Reviewed; 321 AA.
AC G5ECD9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=G-protein coupled receptor aex-2 {ECO:0000305};
DE AltName: Full=Aboc, expulsion defective protein 2 {ECO:0000312|WormBase:T14B1.2};
GN Name=aex-2 {ECO:0000312|WormBase:T14B1.2};
GN ORFNames=T14B1.2 {ECO:0000312|WormBase:T14B1.2};
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:ACI04534.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-174 AND ARG-232.
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).
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23583549; DOI=10.1016/j.cub.2013.03.049;
RA Wang H., Girskis K., Janssen T., Chan J.P., Dasgupta K., Knowles J.A.,
RA Schoofs L., Sieburth D.;
RT "Neuropeptide secreted from a pacemaker activates neurons to control a
RT rhythmic behavior.";
RL Curr. Biol. 23:746-754(2013).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-232.
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: G-protein coupled receptor for the nlp-40 neuropeptide
CC (PubMed:23583549). The activity of this receptor is mediated by G
CC proteins which activate adenylyl cyclase (PubMed:23583549). Plays a
CC role in the defecation motor program, which is a coordinated series of
CC three muscle contractions that occurs every 45 seconds
CC (PubMed:18852466, PubMed:23583549). Specifically, acts in GABAergic
CC neurons, such as AVL and DVB, to control the expulsion step of
CC defecation (PubMed:18852466, PubMed:23583549). Required for fatty acid
CC uptake and metabolism by intestinal cells and therefore regulates the
CC levels of triglycerides in the intestine (PubMed:25849533).
CC {ECO:0000269|PubMed:18852466, ECO:0000269|PubMed:23583549,
CC ECO:0000269|PubMed:25849533}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23583549};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium
CC {ECO:0000269|PubMed:18852466}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal muscle, anal depressor,
CC AVL and DVB GABAergic neurons, enteric muscles, the nerve ring, the
CC ventral nerve cord and head mesodermal cells.
CC {ECO:0000269|PubMed:18852466}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a mild
CC defecation defect. {ECO:0000269|PubMed:18852466}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; FJ165553; ACI04534.1; -; mRNA.
DR EMBL; BX284606; CAA86863.3; -; Genomic_DNA.
DR PIR; T21729; T21729.
DR RefSeq; NP_509626.2; NM_077225.5.
DR AlphaFoldDB; G5ECD9; -.
DR SMR; G5ECD9; -.
DR STRING; 6239.T14B1.2; -.
DR PaxDb; G5ECD9; -.
DR EnsemblMetazoa; T14B1.2.1; T14B1.2.1; WBGene00000085.
DR GeneID; 188491; -.
DR KEGG; cel:CELE_T14B1.2; -.
DR CTD; 188491; -.
DR WormBase; T14B1.2; CE31607; WBGene00000085; aex-2.
DR eggNOG; ENOG502S9TI; Eukaryota.
DR GeneTree; ENSGT00970000196027; -.
DR HOGENOM; CLU_872214_0_0_1; -.
DR InParanoid; G5ECD9; -.
DR OMA; DLLMCIV; -.
DR OrthoDB; 1075852at2759; -.
DR PhylomeDB; G5ECD9; -.
DR PRO; PR:G5ECD9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000085; Expressed in larva and 3 other tissues.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008188; F:neuropeptide receptor activity; IC:WormBase.
DR GO; GO:0010877; P:lipid transport involved in lipid storage; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA: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:2000292; P:regulation of defecation; IGI:UniProtKB.
DR InterPro; IPR039952; Aex-2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR21643; PTHR21643; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..321
FT /note="G-protein coupled receptor aex-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438189"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..76
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..90
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 133..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..175
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 222..242
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..254
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 9
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 88..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT MUTAGEN 174
FT /note="S->G: In sa1040; Defecation defect."
FT /evidence="ECO:0000269|PubMed:18852466"
FT MUTAGEN 232
FT /note="R->Q: In sa3; Defecation defect. Reduced fatty acid
FT uptake into the cytoplasm of intestinal cells and reduced
FT triglycerides in the intestine."
FT /evidence="ECO:0000269|PubMed:18852466,
FT ECO:0000269|PubMed:25849533"
SQ SEQUENCE 321 AA; 37742 MW; 2E6A321C98E82166 CRC64;
MNSTDIIANV TKPFVENLTL GETAFYISCG IVGTVFNALV LWIALTYINT EDKPRQIIVI
NMTVADLLMC IVYMKTRPWL SHFNLWLCHP YYVIIWTCQM CSCLNLVWLN VDKLIYIQFP
LHYYQIVNRK RLLWITAATW GGLYAMNIAL VTFLKITRGS CLGVSLNPYV YLLSPIFYVV
MILTSFSLSA LIYCIAHNLT HMEERQRSKL FRRLFFLFSS TLWTFFTCLP YRLLYLFSIF
CGETCQINNY YKTATNLFFR LLIVGIMINP VITIWTQRIY RLRLMRMFGR LRENSSTEVL
MVSNRRASER PPEHTPLRCD M
