ASAT1_ARATH
ID ASAT1_ARATH Reviewed; 345 AA.
AC Q9SV07;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acyl-CoA--sterol O-acyltransferase 1;
DE EC=2.3.1.-;
DE AltName: Full=Sterol O-acyltransferase 1;
GN Name=ASAT1; OrderedLocusNames=At3g51970; ORFNames=F4F15.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=15535861; DOI=10.1186/gb-2004-5-11-r85;
RA Honys D., Twell D.;
RT "Transcriptome analysis of haploid male gametophyte development in
RT Arabidopsis.";
RL Genome Biol. 5:R85.1-R85.13(2004).
RN [6]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=17885082; DOI=10.1104/pp.107.106278;
RA Chen Q., Steinhauer L., Hammerlindl J., Keller W., Zou J.;
RT "Biosynthesis of phytosterol esters: identification of a sterol o-
RT acyltransferase in Arabidopsis.";
RL Plant Physiol. 145:974-984(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19923239; DOI=10.1104/pp.109.145672;
RA Bouvier-Nave P., Berna A., Noiriel A., Compagnon V., Carlsson A.S.,
RA Banas A., Stymne S., Schaller H.;
RT "Involvement of the phospholipid sterol acyltransferase1 in plant sterol
RT homeostasis and leaf senescence.";
RL Plant Physiol. 152:107-119(2010).
CC -!- FUNCTION: Involved in the esterification of cycloartenol. Not
CC implicated in the formation of sterol esters in flowers or during seed
CC maturation. Has a substrate preference toward saturated fatty acyl
CC donors (16:0 > 18:0 > 16:1 > 18:1). Does not require triacyglycerols
CC (TAGs) as a fatty acyl donor, and is unable to acylate diacylglycerol
CC to produce TAG. {ECO:0000269|PubMed:17885082,
CC ECO:0000269|PubMed:19923239}.
CC -!- INTERACTION:
CC Q9SV07; P34791: CYP20-3; NbExp=3; IntAct=EBI-2025397, EBI-449385;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Increased expression during seed development and
CC as pollen development proceeded from uninucleate microspore to mature
CC pollen. {ECO:0000269|PubMed:15535861}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19923239}.
CC -!- SIMILARITY: Belongs to the wax synthase family. {ECO:0000305}.
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DR EMBL; AL049711; CAB41317.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78870.1; -; Genomic_DNA.
DR EMBL; BT010536; AAQ65159.1; -; mRNA.
DR EMBL; AK175140; BAD42903.1; -; mRNA.
DR PIR; T49076; T49076.
DR RefSeq; NP_190765.1; NM_115056.3.
DR AlphaFoldDB; Q9SV07; -.
DR IntAct; Q9SV07; 1.
DR STRING; 3702.AT3G51970.1; -.
DR PaxDb; Q9SV07; -.
DR PRIDE; Q9SV07; -.
DR EnsemblPlants; AT3G51970.1; AT3G51970.1; AT3G51970.
DR GeneID; 824360; -.
DR Gramene; AT3G51970.1; AT3G51970.1; AT3G51970.
DR KEGG; ath:AT3G51970; -.
DR Araport; AT3G51970; -.
DR TAIR; locus:2083780; AT3G51970.
DR eggNOG; ENOG502QSCR; Eukaryota.
DR HOGENOM; CLU_045902_0_0_1; -.
DR InParanoid; Q9SV07; -.
DR OMA; EGWWASH; -.
DR OrthoDB; 853289at2759; -.
DR PhylomeDB; Q9SV07; -.
DR BioCyc; ARA:AT3G51970-MON; -.
DR PRO; PR:Q9SV07; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SV07; baseline and differential.
DR Genevisible; Q9SV07; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0016127; P:sterol catabolic process; IMP:UniProtKB.
DR GO; GO:0034434; P:sterol esterification; IMP:UniProtKB.
DR InterPro; IPR044851; Wax_synthase.
DR InterPro; IPR032805; Wax_synthase_dom.
DR InterPro; IPR017088; Wax_synthase_Magnoliopsida.
DR PANTHER; PTHR31595; PTHR31595; 1.
DR Pfam; PF13813; MBOAT_2; 1.
DR PIRSF; PIRSF037006; Wax_synthase; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Steroid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..345
FT /note="Acyl-CoA--sterol O-acyltransferase 1"
FT /id="PRO_0000398823"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 345 AA; 39320 MW; EB71D09D3863BB38 CRC64;
MASFIKAWGL VIISLCYTFF IAKLVPKGIK RLILFFPVFL IFFIVPFLIY SLHLLGITAF
FIAWLANFKL LLFALGRGPL SSNHKPLSLP IFLAVSCLPI KIQLSPKPTK THSHEGSTEG
PLIYTIKAVF VVLIIKAYEY STKLPEKVVL TLYAIHIYFA LEIILAATAA AVRAMSDLEL
EPQFNKPYLA TSLQDFWGRR WNLMVTGILR PTVYEPSLQL FSVLGPNYSQ ILAAFGTFVV
SGIMHELIFF YMGRLRPDWK MMWFFLINGF CTTVEIAIKK TINGRWRFPK AISQVLTLTF
VMVTALWLFL PEFNRCNIVE KALDEYAAIG AFAVEVRRKL TAYLF
