AHO3_CAEEL
ID AHO3_CAEEL Reviewed; 332 AA.
AC Q21221;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Alpha/beta hydrolase domain-containing protein aho-3 {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:Q8VCV1};
DE AltName: Full=Abnormal hunger orientation protein 3 {ECO:0000312|WormBase:K04G2.2};
GN Name=aho-3 {ECO:0000312|WormBase:K04G2.2};
GN ORFNames=K04G2.2 {ECO:0000312|WormBase:K04G2.2};
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|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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF CYS-34; CYS-35; LEU-36; CYS-38; CYS-39; SER-191; ASP-256
RP AND HIS-285.
RX PubMed=22512337; DOI=10.1111/j.1365-2443.2012.01594.x;
RA Nishio N., Mohri-Shiomi A., Nishida Y., Hiramatsu N., Kodama-Namba E.,
RA Kimura K.D., Kuhara A., Mori I.;
RT "A novel and conserved protein AHO-3 is required for thermotactic
RT plasticity associated with feeding states in Caenorhabditis elegans.";
RL Genes Cells 17:365-386(2012).
CC -!- FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC proteins (By similarity). Acts in sensory neurons including AWC to
CC regulate starvation-induced thermotaxis plasticity and salt learning
CC behavior. {ECO:0000250|UniProtKB:Q8VCV1, ECO:0000269|PubMed:22512337}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:Q8VCV1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:22512337};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000305|PubMed:22512337}. Cytoplasmic vesicle membrane
CC {ECO:0000305|PubMed:22512337}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q7M759}; Cytoplasmic side
CC {ECO:0000305|PubMed:22512337}. Note=In neurons, localizes to the
CC sensory endings and to cytoplasmic punctate structures.
CC {ECO:0000269|PubMed:22512337}.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of neurons including AIY,
CC HSN, ADF, AFD, AWC, AWB and NSM, hypodermis, pharyngeal muscle and
CC intestine. {ECO:0000269|PubMed:22512337}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and adults.
CC {ECO:0000269|PubMed:22512337}.
CC -!- PTM: Palmitoylated on cysteine residues located in a cysteine cluster
CC at the N-terminus which promotes membrane localization and localization
CC to sensory neuron endings. {ECO:0000305|PubMed:22512337}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.
CC {ECO:0000305}.
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DR EMBL; BX284601; CAB00039.2; -; Genomic_DNA.
DR PIR; T23321; T23321.
DR RefSeq; NP_492210.2; NM_059809.6.
DR AlphaFoldDB; Q21221; -.
DR SMR; Q21221; -.
DR STRING; 6239.K04G2.2; -.
DR ESTHER; caeel-K04G2.2; ABHD17-depalmitoylase.
DR MEROPS; S09.A81; -.
DR EPD; Q21221; -.
DR PaxDb; Q21221; -.
DR PeptideAtlas; Q21221; -.
DR EnsemblMetazoa; K04G2.2.1; K04G2.2.1; WBGene00045192.
DR GeneID; 172585; -.
DR KEGG; cel:CELE_K04G2.2; -.
DR UCSC; K04G2.2; c. elegans.
DR CTD; 172585; -.
DR WormBase; K04G2.2; CE37533; WBGene00045192; aho-3.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000155854; -.
DR HOGENOM; CLU_029375_5_4_1; -.
DR InParanoid; Q21221; -.
DR OMA; NDIVCMY; -.
DR OrthoDB; 629316at2759; -.
DR PhylomeDB; Q21221; -.
DR Reactome; R-CEL-9648002; RAS processing.
DR PRO; PR:Q21221; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00045192; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071683; C:sensory dendrite; IDA:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IMP:UniProtKB.
DR GO; GO:0042595; P:behavioral response to starvation; IMP:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Reference proteome.
FT CHAIN 1..332
FT /note="Alpha/beta hydrolase domain-containing protein aho-
FT 3"
FT /id="PRO_0000443110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
FT ACT_SITE 256
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 285
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MUTAGEN 34
FT /note="C->S: No defect in starvation-induced thermotaxis
FT plasticity. Impaired starvation-induced thermotaxis
FT plasticity and loss of localization to neuronal sensory
FT endings, when associated with S-35; S-38 and S-39."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 35
FT /note="C->S: No defect in starvation-induced thermotaxis
FT plasticity. Impaired starvation-induced thermotaxis
FT plasticity, when associated with S-34; S-38 and S-39 or S-
FT 36; S-38 and S-39. Loss of localization to neuronal sensory
FT endings, when associated with S-34; S-38 and S-39."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 36
FT /note="L->S: No defect in starvation-induced thermotaxis
FT plasticity. Impaired starvation-induced thermotaxis
FT plasticity, when associated with S-35; S-38 and S-39."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 38
FT /note="C->S: No defect in starvation-induced thermotaxis
FT plasticity. Impaired starvation-induced thermotaxis
FT plasticity, when associated with S-34; S-35 and S-39 or S-
FT 35; S-36 and S-39. Loss of localization to neuronal sensory
FT endings, when associated with S-34; S-35 and S-39."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 39
FT /note="C->S: No defect in starvation-induced thermotaxis
FT plasticity. Impaired starvation-induced thermotaxis
FT plasticity, when associated with S-34; S-35 and S-38 or S-
FT 35; S-36 and S-38. Loss of localization to neuronal sensory
FT endings, when associated with S-34; S-35 and S-38."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 191
FT /note="S->A: Impaired starvation-induced thermotaxis
FT plasticity."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 256
FT /note="D->N: Impaired starvation-induced thermotaxis
FT plasticity."
FT /evidence="ECO:0000269|PubMed:22512337"
FT MUTAGEN 285
FT /note="H->A: Impaired starvation-induced thermotaxis
FT plasticity."
FT /evidence="ECO:0000269|PubMed:22512337"
SQ SEQUENCE 332 AA; 35999 MW; 2D2F6DB0BE25945C CRC64;
MSSGAPSGSS MSSTPGSPPP RAGGPNSVSF KDLCCLFCCP PFPSSIVSKL AFMPPEPSYT
ITEDNKLVLI EGRAAWPHQE VDMANCVEMR ITRTRRRNRV ACTMIRPLPN SHFTLLFSHG
NAVDLGQMTS FLYGLGFHLN CNVFSYDYSG YGCSTGKPSE KNLYADITAA FELLKSEFGV
PKEKIILYGQ SIGTVPSVDL ASREDLAALV LHSPLMSGMR VAFPGTTTTW CCDAFPSIEK
VPRVKCPTLV IHGTDDEVID FSHGVSIYER CPTSVEPLWV PGAGHNDVEL HAAYLERLRS
FIDMEASAIR VTAPITNATS TNSRTISNGT SS
