C85A1_ORYSJ
ID C85A1_ORYSJ Reviewed; 469 AA.
AC Q8GSQ1; Q10H45; Q84MZ2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cytochrome P450 85A1 {ECO:0000305};
DE Short=OsCYP85A1 {ECO:0000305};
DE AltName: Full=3-dehydroteasterone synthase {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE EC=1.14.14.- {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
DE AltName: Full=C6-oxidase {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE AltName: Full=Protein DWARF {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE Short=OsDWARF {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE AltName: Full=Teasterone synthase {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE EC=1.14.14.- {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
DE AltName: Full=Typhasterol synthase {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
DE EC=1.14.14.- {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
GN Name=CYP85A1 {ECO:0000305};
GN Synonyms=DWARF {ECO:0000303|PubMed:12427982, ECO:0000303|PubMed:12445121};
GN OrderedLocusNames=Os03g0602300 {ECO:0000305}, LOC_Os03g40540 {ECO:0000305};
GN ORFNames=OJ1519_A12.12 {ECO:0000312|EMBL:BAS85202.1},
GN OsJNBa0015G17.1 {ECO:0000312|EMBL:ABF97501.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, INDUCTION, MUTAGENESIS OF GLY-101 AND GLY-111, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Nipponbare;
RX PubMed=12445121; DOI=10.1046/j.1365-313x.2002.01438.x;
RA Hong Z., Ueguchi-Tanaka M., Shimizu-Sato S., Inukai Y., Fujioka S.,
RA Shimada Y., Takatsuto S., Agetsuma M., Yoshida S., Watanabe Y., Uozu S.,
RA Kitano H., Ashikari M., Matsuoka M.;
RT "Loss-of-function of a rice brassinosteroid biosynthetic enzyme, C-6
RT oxidase, prevents the organized arrangement and polar elongation of cells
RT in the leaves and stem.";
RL Plant J. 32:495-508(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12427982; DOI=10.1104/pp.007179;
RA Mori M., Nomura T., Ooka H., Ishizaka M., Yokota T., Sugimoto K., Okabe K.,
RA Kajiwara H., Satoh K., Yamamoto K., Hirochika H., Kikuchi S.;
RT "Isolation and characterization of a rice dwarf mutant with a defect in
RT brassinosteroid biosynthesis.";
RL Plant Physiol. 130:1152-1161(2002).
RN [8]
RP FUNCTION.
RX PubMed=18656444; DOI=10.1016/j.bbrc.2008.07.073;
RA Kim B.K., Fujioka S., Takatsuto S., Tsujimoto M., Choe S.;
RT "Castasterone is a likely end product of brassinosteroid biosynthetic
RT pathway in rice.";
RL Biochem. Biophys. Res. Commun. 374:614-619(2008).
CC -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC biosynthesis (PubMed:12427982, PubMed:12445121). May convert 6-
CC deoxoteasterone (6-deoxoTE) to teasterone (TE), 3-dehydro-6-
CC deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3-dehydroteasterone (3DT,
CC 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY)
CC (PubMed:12427982, PubMed:12445121). Involved in the organization and
CC elongation of the leaf and stem cells (PubMed:12427982,
CC PubMed:12445121). Not able to convert 6-deoxocastasterone (6-deoxoCS)
CC and castasterone (CS) to brassinolide (BL) (PubMed:18656444).
CC {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121,
CC ECO:0000269|PubMed:18656444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxyteasterone + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69959, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20716,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188499;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69960;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC teasterone; Xref=Rhea:RHEA:69963, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:26863, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:12427982,
CC ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69964;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxoteasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3-dehydro-6alpha-hydroxyteasterone + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69947,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69948;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6alpha-hydroxyteasterone + O2 + reduced [NADPH--
CC hemoprotein reductase] = 3-dehydroteasterone + H(+) + 2 H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69951,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188496;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69952;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxotyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6alpha-hydroxytyphasterol + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:69939, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20717,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:188495;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69940;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6alpha-hydroxytyphasterol + O2 + reduced [NADPH--hemoprotein
CC reductase] = H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase] +
CC typhasterol; Xref=Rhea:RHEA:69943, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:27173, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:188495; Evidence={ECO:0000269|PubMed:12427982,
CC ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69944;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--
CC hemoprotein reductase] = 3-dehydroteasterone + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:70039,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20000,
CC ChEBI:CHEBI:20710, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70040;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxoteasterone + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase] + teasterone; Xref=Rhea:RHEA:70043, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20716, ChEBI:CHEBI:26863,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70044;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-deoxotyphasterol + 2 O2 + 2 reduced [NADPH--hemoprotein
CC reductase] = 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein
CC reductase] + typhasterol; Xref=Rhea:RHEA:70035, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:27173,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70036;
CC Evidence={ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in all the tissues, but
CC preferentially in the leaf sheath. {ECO:0000269|PubMed:12445121}.
CC -!- INDUCTION: Down-regulated by brassinolide (BL) in the brassinosteroid-
CC deficient dwarf1 (brd1) mutant. {ECO:0000269|PubMed:12445121}.
CC -!- DISRUPTION PHENOTYPE: Plants show a range of abnormalities in organ
CC development and growth, with deficiency in the elongation of the stem
CC and leaves, skotomorphogenesis, root differentiation and reproductive
CC growth. Treatment with exogenous brassinolide (BL) rescues the abnormal
CC phenotype. {ECO:0000269|PubMed:12427982, ECO:0000269|PubMed:12445121}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB084385; BAC45000.1; -; mRNA.
DR EMBL; AC092778; AAP12898.1; -; Genomic_DNA.
DR EMBL; AC097276; AAT81671.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF97501.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12537.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85202.1; -; Genomic_DNA.
DR EMBL; AK072295; BAG92911.1; -; mRNA.
DR RefSeq; XP_015631644.1; XM_015776158.1.
DR AlphaFoldDB; Q8GSQ1; -.
DR SMR; Q8GSQ1; -.
DR STRING; 4530.OS03T0602300-01; -.
DR PaxDb; Q8GSQ1; -.
DR PRIDE; Q8GSQ1; -.
DR EnsemblPlants; Os03t0602300-01; Os03t0602300-01; Os03g0602300.
DR GeneID; 4333399; -.
DR Gramene; Os03t0602300-01; Os03t0602300-01; Os03g0602300.
DR KEGG; osa:4333399; -.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q8GSQ1; -.
DR OMA; WTATRDR; -.
DR OrthoDB; 574756at2759; -.
DR UniPathway; UPA00381; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q8GSQ1; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:Gramene.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IMP:Gramene.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:Gramene.
DR GO; GO:0009647; P:skotomorphogenesis; IMP:Gramene.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid biosynthesis; Heme; Iron; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..469
FT /note="Cytochrome P450 85A1"
FT /id="PRO_0000052172"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 419
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT MUTAGEN 101
FT /note="G->V: In brd1-3; dwarf and defective in
FT brassinosteroid biosynthesis."
FT /evidence="ECO:0000269|PubMed:12445121"
FT MUTAGEN 111
FT /note="G->V: In brd1-2; dwarf and defective in
FT brassinosteroid biosynthesis."
FT /evidence="ECO:0000269|PubMed:12445121"
SQ SEQUENCE 469 AA; 52822 MW; 24662A342BA96880 CRC64;
MVLVAIGVVV AAAVVVSSLL LRWNEVRYSR KRGLPPGTMG WPLFGETTEF LKQGPSFMKA
RRLRYGSVFR THILGCPTVV CMEAELNRRA LASEGRGFVP GYPQSMLDIL GRNNIAAVQG
PLHRAMRGAM LSLVRPAMIR SSLLPKIDAF MRSHLAAWSS SSSSAVVDIQ AKTKEMALLS
ALRQIAGVSA GPLSDALKAE LYTLVLGTIS LPINLPGTNY YQGFKARKKL VAMLEQMIAE
RRSSGQVHDD MLDALLTGVE GTREKLTDEQ IIDLIITLIY SGYETMSTTS MMAVKYLSDH
PKALEQLRKE HFDIRKGKAP EDAIDWNDFK SMTFTRAVIF ETLRLATVVN GLLRKTTQDV
EMNGYVIPKG WRIYVYTREI NYDPFLYPDP MTFNPWRWLE KNMESHPHFM LFGGGSRMCP
GKEVGTVEIA TFLHYFVTQY RWEEEGNNTI LKFPRVEAPN GLHIRVQDY
