DHS3_CAEEL
ID DHS3_CAEEL Reviewed; 309 AA.
AC A5JYX5; A5JYX4; A5JYX6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein dhs-3 {ECO:0000305};
DE AltName: Full=Alcohol dehydrogenase dhs-3 {ECO:0000255|PROSITE-ProRule:PRU10001};
DE EC=1.1.1.1 {ECO:0000255|PROSITE-ProRule:PRU10001};
GN Name=dhs-3 {ECO:0000312|WormBase:T02E1.5b};
GN ORFNames=T02E1.5 {ECO:0000312|WormBase:T02E1.5b};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=26121959; DOI=10.1016/j.bbalip.2015.06.004;
RA Vrablik T.L., Petyuk V.A., Larson E.M., Smith R.D., Watts J.L.;
RT "Lipidomic and proteomic analysis of Caenorhabditis elegans lipid droplets
RT and identification of ACS-4 as a lipid droplet-associated protein.";
RL Biochim. Biophys. Acta 1851:1337-1345(2015).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=26025681; DOI=10.1016/j.bbamcr.2015.05.020;
RA Na H., Zhang P., Chen Y., Zhu X., Liu Y., Liu Y., Xie K., Xu N., Yang F.,
RA Yu Y., Cichello S., Mak H.Y., Wang M.C., Zhang H., Liu P.;
RT "Identification of lipid droplet structure-like/resident proteins in
RT Caenorhabditis elegans.";
RL Biochim. Biophys. Acta 1853:2481-2491(2015).
CC -!- FUNCTION: May play a role in lipid droplet formation. May modulate
CC triglyceride levels. {ECO:0000269|PubMed:26025681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10001};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26025681,
CC ECO:0000269|PubMed:26121959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:T02E1.5b};
CC IsoId=A5JYX5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T02E1.5a};
CC IsoId=A5JYX5-2; Sequence=VSP_059213;
CC Name=c {ECO:0000312|WormBase:T02E1.5c};
CC IsoId=A5JYX5-3; Sequence=VSP_059212;
CC -!- TISSUE SPECIFICITY: Expressed in the intestine and vulva.
CC {ECO:0000269|PubMed:26025681}.
CC -!- DEVELOPMENTAL STAGE: Not expressed in embryos.
CC {ECO:0000269|PubMed:26025681}.
CC -!- DISRUPTION PHENOTYPE: Viable, but intestinal cells contain lipid
CC droplets that are reduced in size and that contained a reduced amount
CC of triglycerides as compared to wild-type.
CC {ECO:0000269|PubMed:26025681}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|RuleBase:RU000363}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284601; CAN86610.1; -; Genomic_DNA.
DR EMBL; BX284601; CAN86611.1; -; Genomic_DNA.
DR EMBL; BX284601; CAN86612.1; -; Genomic_DNA.
DR RefSeq; NP_001122508.1; NM_001129036.1. [A5JYX5-2]
DR RefSeq; NP_001122509.1; NM_001129037.2. [A5JYX5-1]
DR RefSeq; NP_001122510.1; NM_001129038.2. [A5JYX5-3]
DR AlphaFoldDB; A5JYX5; -.
DR SMR; A5JYX5; -.
DR STRING; 6239.T02E1.5b; -.
DR EPD; A5JYX5; -.
DR PaxDb; A5JYX5; -.
DR PeptideAtlas; A5JYX5; -.
DR EnsemblMetazoa; T02E1.5a.1; T02E1.5a.1; WBGene00000967. [A5JYX5-2]
DR EnsemblMetazoa; T02E1.5b.1; T02E1.5b.1; WBGene00000967. [A5JYX5-1]
DR EnsemblMetazoa; T02E1.5c.1; T02E1.5c.1; WBGene00000967. [A5JYX5-3]
DR GeneID; 172603; -.
DR KEGG; cel:CELE_T02E1.5; -.
DR UCSC; T02E1.5b; c. elegans.
DR CTD; 172603; -.
DR WormBase; T02E1.5a; CE41004; WBGene00000967; dhs-3. [A5JYX5-2]
DR WormBase; T02E1.5b; CE41005; WBGene00000967; dhs-3. [A5JYX5-1]
DR WormBase; T02E1.5c; CE41006; WBGene00000967; dhs-3. [A5JYX5-3]
DR eggNOG; KOG1201; Eukaryota.
DR GeneTree; ENSGT00970000196335; -.
DR InParanoid; A5JYX5; -.
DR OMA; MIKANHG; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; A5JYX5; -.
DR Reactome; R-CEL-193144; Estrogen biosynthesis.
DR Reactome; R-CEL-2187335; The retinoid cycle in cones (daylight vision).
DR Reactome; R-CEL-5365859; RA biosynthesis pathway.
DR Reactome; R-CEL-8964572; Lipid particle organization.
DR PRO; PR:A5JYX5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000967; Expressed in larva and 4 other tissues.
DR GO; GO:0005811; C:lipid droplet; IDA:WormBase.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; HEP:WormBase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid droplet; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..309
FT /note="Protein dhs-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000442221"
FT REGION 1..50
FT /note="Required for lipid droplet localization"
FT /evidence="ECO:0000269|PubMed:26025681"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_059212"
FT VAR_SEQ 1..40
FT /note="MPYVFLLSPQLEIASQWDGYYEKTFEVSDHVHKEIILKVS -> MQDILESV
FT VVTLHAICLLIISTIRNCFPMGWLLRKDVR (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_059213"
SQ SEQUENCE 309 AA; 33885 MW; D015E4EC1D2BC0B9 CRC64;
MPYVFLLSPQ LEIASQWDGY YEKTFEVSDH VHKEIILKVS GQTVLITGSG SGLGRLMAFE
FGKLGARLVL WDINEQGNKE TLKELEAMGV EAKAYTVDLS EYKEINRTAD LVKSEVGKVD
ILVNNAGIVT GKKLLQCPDE LMVKTVSVNT NALFFTTKNF LPGMLESNKG HIVTIASMAG
KCGVAGLVDY CASKHGAVGF NDSLASELYA LKKDVKTTVV CPIYINTGMF DGIATKWPTL
LPILSPEYVV DCIMEAVLTD RAFLAIPKFS YIFIALAGLL PTEVLNLYGD HFGITHSMDH
FKGRQSRQA
