AYR1_SCHPO
ID AYR1_SCHPO Reviewed; 296 AA.
AC Q09851;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=NADPH-dependent 1-acyldihydroxyacetone phosphate reductase;
DE Short=ADR;
DE EC=1.1.1.101;
DE AltName: Full=1-acyl DHAP reductase;
DE AltName: Full=Acyl/alkyl DHAP reductase;
DE AltName: Full=Acylglycerone-phosphate reductase;
DE AltName: Full=Triacylglycerol lipase ayr1;
DE Short=TAG lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P40471};
GN Name=ayr1; ORFNames=SPAC23D3.11;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Can convert acyl and alkyl dihydroxyacetone-phosphate (DHAP)
CC into glycerolipids and ether lipids, respectively. Required for the
CC biosynthesis of phosphatidic acid via the DHAP pathway, where it
CC reduces 1-acyl DHAP to lysophosphatidic acid (LPA). Also has
CC triacylglycerol (TAG) lipase activity. Involved in the mobilization of
CC the non-polar storage lipids triacylglycerols (TAGs) from lipid
CC particles by hydrolysis of TAGs. Lipolysis of TAG by AYR1 is essential
CC for starvation-induced autophagy. Forms an NADPH-regulated cation-
CC selective channel in the mitochondrial outer membrane.
CC {ECO:0000250|UniProtKB:P40471}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + NADP(+) = 1-
CC hexadecanoylglycerone 3-phosphate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17341, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58303, ChEBI:CHEBI:58349;
CC EC=1.1.1.101; Evidence={ECO:0000250|UniProtKB:P40471};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + H(+) + NADPH = a 1-acyl-sn-
CC glycero-3-phosphate + NADP(+); Xref=Rhea:RHEA:33375,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57534, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:P40471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33376;
CC Evidence={ECO:0000250|UniProtKB:P40471};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:P40471};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P40471};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:P40471}.
CC Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole
CC {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus
CC {ECO:0000269|PubMed:16823372}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P40471}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91246.1; -; Genomic_DNA.
DR PIR; S62502; S62502.
DR RefSeq; NP_594548.1; NM_001019977.2.
DR AlphaFoldDB; Q09851; -.
DR SMR; Q09851; -.
DR BioGRID; 277991; 7.
DR STRING; 4896.SPAC23D3.11.1; -.
DR iPTMnet; Q09851; -.
DR MaxQB; Q09851; -.
DR PaxDb; Q09851; -.
DR EnsemblFungi; SPAC23D3.11.1; SPAC23D3.11.1:pep; SPAC23D3.11.
DR GeneID; 2541489; -.
DR KEGG; spo:SPAC23D3.11; -.
DR PomBase; SPAC23D3.11; ayr1.
DR VEuPathDB; FungiDB:SPAC23D3.11; -.
DR eggNOG; KOG1209; Eukaryota.
DR HOGENOM; CLU_010194_2_9_1; -.
DR InParanoid; Q09851; -.
DR OMA; LHAYSNT; -.
DR PhylomeDB; Q09851; -.
DR PRO; PR:Q09851; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0102566; F:1-acyl dihydroxyacetone phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000140; F:acylglycerone-phosphate reductase activity; ISO:PomBase.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:PomBase.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; NAD; NADP; Oxidoreductase;
KW Reference proteome; Vacuole.
FT CHAIN 1..296
FT /note="NADPH-dependent 1-acyldihydroxyacetone phosphate
FT reductase"
FT /id="PRO_0000054874"
FT MOTIF 11..15
FT /note="GXSXG"
FT /evidence="ECO:0000250|UniProtKB:P40471"
FT ACT_SITE 13
FT /note="Nucleophile; for lipase activity"
FT /evidence="ECO:0000250|UniProtKB:P40471"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 8..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 9..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 55..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 181..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 296 AA; 32731 MW; 91E33D2575F141FF CRC64;
MEAEKFVLIT GCSEGGIGNA LALKFHQEGF QVLATARQVE RMDNLTKAGL QTLKLDVTDE
DSVREVEQEV RKFTNGSLHY LINNAGAPCS APAIDLDIED VSKVMDVNFY GVIRMNKAFQ
HQLIRAKGTI VNVNSLVSYV PFAFNAAYNA SKAALLAYSN TLRIELAPFG VQVTSIMTGG
VQTKIQSKPL GTMTEAAIPE NSIYYPYRKL ILENRNPVEK FVTIEEFADA AYPQLVGRGR
WYQLFKPGVR PAQIWAGYMS SAGRVGSMLP VEVFSMSVRL IVKLPSTAVW RDHTVD
