ID AT1_ORYSJ Reviewed; 485 AA. AC Q7G4G7; DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 07-OCT-2020, entry version 112. DE RecName: Full=Acyl transferase 1 {ECO:0000305}; DE Short=OsAT1 {ECO:0000303|PubMed:17273822}; DE EC=2.3.1.- {ECO:0000305}; DE AltName: Full=Protein SPOTTED LEAF 18 {ECO:0000303|PubMed:17273822}; GN Name=AT1 {ECO:0000303|PubMed:17273822}; GN Synonyms=SPL18 {ECO:0000303|PubMed:17273822}; GN OrderedLocusNames=Os10g0195600 {ECO:0000312|EMBL:BAF26202.1}, GN LOC_Os10g11980 {ECO:0000312|EMBL:AAP52614.1}; GN ORFNames=OSJNBa0034E15.15 {ECO:0000312|EMBL:AAN05389.1}; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12791992; DOI=10.1126/science.1083523; RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M., RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.; RT "In-depth view of structure, activity, and evolution of rice chromosome RT 10."; RL Science 300:1566-1569(2003). RN [2] 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 [3] 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 [4] 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 [5] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17273822; DOI=10.1007/s11103-006-9130-y; RA Mori M., Tomita C., Sugimoto K., Hasegawa M., Hayashi N., Dubouzet J.G., RA Ochiai H., Sekimoto H., Hirochika H., Kikuchi S.; RT "Isolation and molecular characterization of a Spotted leaf 18 mutant by RT modified activation-tagging in rice."; RL Plant Mol. Biol. 63:847-860(2007). CC -!- FUNCTION: Involved in defense against pathogens. May contribute to CC disease resistance by potentiating disease resistance signaling, or CC producing phytoalexin-like secondary products. CC {ECO:0000269|PubMed:17273822}. CC -!- TISSUE SPECIFICITY: Highly expressed in young panicles. Expressed in CC leaf sheaths and panicles. {ECO:0000269|PubMed:17273822}. CC -!- MISCELLANEOUS: The gain-of-function mutants Spl18 (T-DNA tagging) show CC a lesion mimic phenotype, express constitutively PBZ1, accumulate the CC phytoalexins momilactone A and sakuranetin, and display enhanced CC resistance to rice blast fungus (M.oryzae). Plants over-expressing CC SPL18 show a lesion mimic phenotype and display enhanced resistance to CC bacterial blight (X. oryzae pv. oryzae). {ECO:0000269|PubMed:17273822}. CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}. 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; AC093612; AAX95735.1; -; Genomic_DNA. DR EMBL; AC105377; AAN05389.1; -; Genomic_DNA. DR EMBL; DP000086; AAP52614.1; -; Genomic_DNA. DR EMBL; AP008216; BAF26202.1; -; Genomic_DNA. DR EMBL; AP014966; BAT10210.1; -; Genomic_DNA. DR RefSeq; XP_015612859.1; XM_015757373.1. DR RefSeq; XP_015612860.1; XM_015757374.1. DR STRING; 4530.OS10T0195600-01; -. DR PaxDb; Q7G4G7; -. DR PRIDE; Q7G4G7; -. DR EnsemblPlants; Os10t0195600-01; Os10t0195600-01; Os10g0195600. DR GeneID; 4348247; -. DR Gramene; Os10t0195600-01; Os10t0195600-01; Os10g0195600. DR KEGG; osa:4348247; -. DR eggNOG; ENOG502QUSI; Eukaryota. DR HOGENOM; CLU_014546_2_2_1; -. DR InParanoid; Q7G4G7; -. DR KO; K19861; -. DR OMA; GRWNTHT; -. DR OrthoDB; 1130893at2759; -. DR Proteomes; UP000000763; Chromosome 10. DR Proteomes; UP000059680; Chromosome 10. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW. DR Gene3D; 3.30.559.10; -; 2. DR InterPro; IPR023213; CAT-like_dom_sf. DR InterPro; IPR003480; Transferase. DR Pfam; PF02458; Transferase; 1. PE 2: Evidence at transcript level; KW Acyltransferase; Plant defense; Reference proteome; Transferase. FT CHAIN 1..485 FT /note="Acyl transferase 1" FT /id="PRO_0000437774" FT COMPBIAS 210..251 FT /note="Ala-rich" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00001" FT ACT_SITE 172 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q8W1W9" SQ SEQUENCE 485 AA; 52218 MW; D56AF5DF3F289B5B CRC64; MVVTFTSRRS EPVLLRPARP TPRETKQLSD LDDQRTLRYY ETVVGFFRRC DGGAAGAVGA PADPAKAIRA ALAEALVYYY PVAGRLREVA DGGGAGNRLV VDCTAEGVVF VEADADVRLE DFGQPLLPPY PCVGELLCDA GDTRAVVGKP LLLMQVTQLK CGGFVLGFHI CHNIADGFGM AQLIMAIADL ARGEPAPTIL PVWRRDLLTA ARLGSGAVAR TPFASAAAAS ASASSPALQN GARRAAAAAD AMLSTPPDRM VVEYFLFGPR EVSYLRGQLP AHLADSTTVF ELLTAVMWRC RTAALGYGPD LRVRLMITMN ARGRWNAHTP LPRGFYGNAH VSPVAEAAAG DLLGRPLADT VELVRRTKRG MTRERMSAMV ETVAQLREWP PSSMDRVYEV SDIKWTTVNL LKFGWAEFAG GGIPLAGDLT SKLGSDHTRC KNSAGEVSTV VSMLLPRVAM ARFKKEMAVL LNKDDKKSLT IMSSL //