WAT_DROME
ID WAT_DROME Reviewed; 517 AA.
AC Q8MS59; Q9VAR3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Fatty acyl-CoA reductase wat {ECO:0000305};
DE AltName: Full=Protein waterproof {ECO:0000303|PubMed:24183938};
DE EC=1.2.1.84 {ECO:0000269|PubMed:24183938};
GN Name=wat {ECO:0000303|PubMed:24183938};
GN ORFNames=CG1443 {ECO:0000312|FlyBase:FBgn0039620};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM50938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50938.1};
RC TISSUE=Larva {ECO:0000312|EMBL:AAM50938.1}, and
RC Pupae {ECO:0000312|EMBL:AAM50938.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=24183938; DOI=10.1016/j.ydbio.2013.10.022;
RA Jaspers M.H., Pflanz R., Riedel D., Kawelke S., Feussner I., Schuh R.;
RT "The fatty acyl-CoA reductase Waterproof mediates airway clearance in
RT Drosophila.";
RL Dev. Biol. 385:23-31(2014).
CC -!- FUNCTION: Catalyzes the reduction of saturated fatty acyl-CoA to fatty
CC alcohols. The preferred substrates are C24:0 and C26:0. Necessary for
CC the final stages of tracheal maturation, to facilitate the transition
CC from water-filled to gas-filled tubes. May help to maintain the
CC integrity of the outer hydrophobic envelope of the trachea.
CC {ECO:0000269|PubMed:24183938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain
CC primary fatty alcohol + CoA + 2 NADP(+); Xref=Rhea:RHEA:52716,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77396, ChEBI:CHEBI:83139; EC=1.2.1.84;
CC Evidence={ECO:0000269|PubMed:24183938};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000305|PubMed:24183938}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Detected in the tracheal system and hindgut from
CC embryonic stage 13 onwards (at protein level).
CC {ECO:0000269|PubMed:24183938}.
CC -!- DISRUPTION PHENOTYPE: Tracheal morphogenesis in embryos is grossly
CC normal. The tracheal tubes fail to fill with gas during the final
CC stages of maturation, and instead remain full of fluid. The hydrophobic
CC outer cuticle layer of the trachea appears to be disrupted and forms
CC membranous structures extending into the tracheal lumen.
CC {ECO:0000269|PubMed:24183938}.
CC -!- SIMILARITY: Belongs to the fatty acyl-CoA reductase family.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF56838.2; -; Genomic_DNA.
DR EMBL; AY119078; AAM50938.1; -; mRNA.
DR RefSeq; NP_651652.2; NM_143395.1.
DR AlphaFoldDB; Q8MS59; -.
DR IntAct; Q8MS59; 25.
DR STRING; 7227.FBpp0084714; -.
DR PaxDb; Q8MS59; -.
DR PRIDE; Q8MS59; -.
DR DNASU; 43420; -.
DR EnsemblMetazoa; FBtr0085345; FBpp0084714; FBgn0039620.
DR GeneID; 43420; -.
DR KEGG; dme:Dmel_CG1443; -.
DR UCSC; CG1443-RA; d. melanogaster.
DR CTD; 43420; -.
DR FlyBase; FBgn0039620; wat.
DR VEuPathDB; VectorBase:FBgn0039620; -.
DR eggNOG; KOG1221; Eukaryota.
DR GeneTree; ENSGT00390000006367; -.
DR HOGENOM; CLU_024661_0_2_1; -.
DR InParanoid; Q8MS59; -.
DR OMA; FAHCNMR; -.
DR OrthoDB; 815047at2759; -.
DR PhylomeDB; Q8MS59; -.
DR BRENDA; 1.2.1.84; 1994.
DR BioGRID-ORCS; 43420; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43420; -.
DR PRO; PR:Q8MS59; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039620; Expressed in crop (Drosophila) and 20 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0102965; F:alcohol-forming fatty acyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; ISS:FlyBase.
DR GO; GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IDA:FlyBase.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
DR GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IDA:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR CDD; cd09071; FAR_C; 1.
DR InterPro; IPR026055; FAR.
DR InterPro; IPR033640; FAR_C.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11011; PTHR11011; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF03015; Sterile; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Lipid biosynthesis; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Fatty acyl-CoA reductase wat"
FT /id="PRO_0000438526"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 59515 MW; 555C3FA9B454808B CRC64;
MDDPKIMNIM NGMKSLEDHC QLISDVKDES PMQMFYKDKG VFLTGGTGFF GKIIIEKLLR
VTEVGQIYLL IRTKKGKDAF ARIEDLFNDP VFAKMKQVNP KYRCQITIIS GDCSLPGLGI
SADERETIME NVNIVLHSAA TVRFDEKLKM AIAINVHGTK EIIKLAKEIV NLKALVHVST
AFAHCNMRHI QERFYSGTMS GENAFKLSEC LDEHTLNTLT PTIIKGYPNT YTFTKVLAEN
VVQQSAQNLP VTIFRPGIVI TTYREPVTGW IDNMYGPCGV IVGIGSGVLR VFTGDMDNKA
HIVPVDMCVN ALLASAWDIA RNKYETPPIY NYVPDAENMV TWRRYMEDGF EYGCDIPMRK
SIWYPRFTIV PHMWQYHILC FLYHTLPALV MDAIMVIIGK KPRMMKIYRK IHKLSNVLKY
FSSNEFRFDN DNVRKLTEKL DDRDKRLFAF DMRDLDWTNL FRVSLYGLRL YVVKDDPSNI
PESIKRYERL KVLHYTTLAV FYALAAWALY ALLKLFL
