FEY_ARATH
ID FEY_ARATH Reviewed; 376 AA.
AC F4JJR8; Q0WVF4; Q41248; Q9FQM0; Q9STP9; Q9T098;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Dehydrogenase/reductase SDR family member FEY {ECO:0000305};
DE EC=1.1.-.- {ECO:0000305};
DE AltName: Full=Protein FOREVER YOUNG {ECO:0000303|PubMed:7849756};
GN Name=FEY {ECO:0000303|PubMed:7849756}; Synonyms=FEY3 {ECO:0000305};
GN OrderedLocusNames=At4g27760 {ECO:0000312|Araport:AT4G27760};
GN ORFNames=T27E11.10 {ECO:0000312|EMBL:CAB43965.1}, T29A15 {ECO:0000305};
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 [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=7849756; DOI=10.1046/j.1365-313x.1994.6060835.x;
RA Callos J.D., DiRado M., Xu B., Behringer F.J., Link B.M., Medford J.I.;
RT "The forever young gene encodes an oxidoreductase required for proper
RT development of the Arabidopsis vegetative shoot apex.";
RL Plant J. 6:835-847(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RA Fu H., Song J., Du J., Jiang J., Park W.D.;
RT "Potato and tomato Forever Young genes contain class-I patatin-like
RT regulatory sequences.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Putative oxidoreductase (By similarity). Required for
CC vegetative shoot apex development, especially during leaf positioning
CC and for shoot apical meristem (SAM) maintenance (PubMed:7849756).
CC {ECO:0000250|UniProtKB:Q5RJY4, ECO:0000269|PubMed:7849756}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers and,
CC at lower levels, in siliques. {ECO:0000269|PubMed:7849756}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the development of the vegetative
CC shoot apex. Abnormal leaf positioning and impaired shoot apical
CC meristem (SAM) maintenance, leading to the death of most plants prior
CC to the end of vegetative development. {ECO:0000269|PubMed:7849756}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB33362.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB38288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB43965.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81426.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; S77418; AAB33362.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF217275; AAG44120.1; -; mRNA.
DR EMBL; AL035602; CAB38288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL078579; CAB43965.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81426.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85390.1; -; Genomic_DNA.
DR EMBL; AK226796; BAE98894.1; -; mRNA.
DR PIR; H85322; H85322.
DR PIR; T05881; T05881.
DR PIR; T09016; T09016.
DR RefSeq; NP_194506.4; NM_118915.6.
DR AlphaFoldDB; F4JJR8; -.
DR SMR; F4JJR8; -.
DR STRING; 3702.AT4G27760.1; -.
DR iPTMnet; F4JJR8; -.
DR PaxDb; F4JJR8; -.
DR PRIDE; F4JJR8; -.
DR ProteomicsDB; 230716; -.
DR EnsemblPlants; AT4G27760.1; AT4G27760.1; AT4G27760.
DR GeneID; 828890; -.
DR Gramene; AT4G27760.1; AT4G27760.1; AT4G27760.
DR KEGG; ath:AT4G27760; -.
DR Araport; AT4G27760; -.
DR TAIR; locus:2137772; AT4G27760.
DR eggNOG; KOG1208; Eukaryota.
DR HOGENOM; CLU_010194_44_2_1; -.
DR InParanoid; F4JJR8; -.
DR OMA; DMNMTSG; -.
DR OrthoDB; 921996at2759; -.
DR PRO; PR:F4JJR8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JJR8; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0010073; P:meristem maintenance; IMP:TAIR.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Acetylation; NAD; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..376
FT /note="Dehydrogenase/reductase SDR family member FEY"
FT /id="PRO_0000441878"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 61..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 156
FT /note="A -> E (in Ref. 5; BAE98894)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="K -> E (in Ref. 2; AAG44120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41481 MW; D70CD9E490BD4A03 CRC64;
MSDETTSSPS PAPAKKKQNL GWMEWMRGWS SVFGEILFQR ITASHLENPL PLPSVNDLTC
VVTGSTSGIG RETARQLAEA GAHVVMAVRN TKAAQELILQ WQNEWSGKGL PLNIEAMEID
LLSLDSVARF AEAFNARLGP LHVLINNAGM FAMGEAQKFS EEGYEQHMQV NHLAPALLSV
LLLPSLIRGS PSRIINVNSV MHSVGFVDPD DMNVVSGRRK YSSLIGYSSS KLAQIMFSSI
LFKKLPLETG VSVVCLSPGV VLTNVARDLS RILQALYAVI PYFIFSPQEG CRSSLFSATD
PQIPEYWETL KNDDWPVCPF ISQDCRPANP SEEAHNTETA QRVWKKTLEL VGLPLDAVEK
LIEGENIQCR YGAQHE
