ELO3L_ARATH
ID ELO3L_ARATH Reviewed; 289 AA.
AC Q9SYY4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Elongation of fatty acids protein 3-like;
DE Short=Protein ELO3-like;
DE EC=2.3.1.-;
DE AltName: Full=Protein HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 3;
DE AltName: Full=Very long-chain fatty acid condensing enzyme HOS3;
DE Short=VLCFA condensing enzyme HOS3;
GN Name=HOS3; OrderedLocusNames=At4g36830; ORFNames=AP22.81, C7A10.530;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=19529829; DOI=10.1093/mp/ssn085;
RA Quist T.M., Sokolchik I., Shi H., Joly R.J., Bressan R.A., Maggio A.,
RA Narsimhan M., Li X.;
RT "HOS3, an ELO-like gene, inhibits effects of ABA and implicates a S-1-
RT P/ceramide control system for abiotic stress responses in Arabidopsis
RT thaliana.";
RL Mol. Plant 2:138-151(2009).
CC -!- FUNCTION: Probable very long-chain fatty acid (VLCFA) elongase that
CC controls VLCFA composition and functions to inhibit abscisic acid
CC (ABA)-mediated stress responses, including regulation of stomatal
CC aperture, maintenance of primary root growth and inhibition of
CC germination. VLCFA pathway and products may function as signaling
CC components acting upstream of sphingosine-1-phosphate, ceramide and the
CC heterotrimeric G-protein complex, in lipid-mediated regulation of
CC abiotic stress signaling. {ECO:0000269|PubMed:19529829}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show decreased abscisic acid (ABA)-
CC induced inhibition of root growth and seed dormancy, and enhanced ABA-
CC mediated stomatal closure. {ECO:0000269|PubMed:19529829}.
CC -!- SIMILARITY: Belongs to the ELO family. {ECO:0000305}.
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DR EMBL; Z99708; CAB16818.1; -; Genomic_DNA.
DR EMBL; AL161590; CAB80349.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86707.1; -; Genomic_DNA.
DR EMBL; BT012601; AAT06420.1; -; mRNA.
DR EMBL; BT020336; AAV85691.1; -; mRNA.
DR PIR; H85434; H85434.
DR RefSeq; NP_195401.1; NM_119847.4.
DR AlphaFoldDB; Q9SYY4; -.
DR SMR; Q9SYY4; -.
DR BioGRID; 15117; 14.
DR IntAct; Q9SYY4; 14.
DR STRING; 3702.AT4G36830.1; -.
DR PaxDb; Q9SYY4; -.
DR PRIDE; Q9SYY4; -.
DR DNASU; 829836; -.
DR EnsemblPlants; AT4G36830.1; AT4G36830.1; AT4G36830.
DR GeneID; 829836; -.
DR Gramene; AT4G36830.1; AT4G36830.1; AT4G36830.
DR KEGG; ath:AT4G36830; -.
DR Araport; AT4G36830; -.
DR TAIR; locus:2115395; AT4G36830.
DR eggNOG; KOG3071; Eukaryota.
DR HOGENOM; CLU_048483_6_0_1; -.
DR InParanoid; Q9SYY4; -.
DR OMA; HIMKGGC; -.
DR PhylomeDB; Q9SYY4; -.
DR PRO; PR:Q9SYY4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SYY4; baseline and differential.
DR Genevisible; Q9SYY4; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IMP:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR GO; GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0034626; P:fatty acid elongation, polyunsaturated fatty acid; IBA:GO_Central.
DR GO; GO:0019367; P:fatty acid elongation, saturated fatty acid; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002076; ELO_fam.
DR PANTHER; PTHR11157; PTHR11157; 1.
DR Pfam; PF01151; ELO; 1.
PE 2: Evidence at transcript level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Stress response;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Elongation of fatty acids protein 3-like"
FT /id="PRO_0000430307"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 32782 MW; 1AD2B374FA7232F1 CRC64;
MSTALINSIT YFLSEHPYIV GFRWSNSQSW GSTWSFLFTS ISLYIAVSSS LHILLSAVRR
SNRSVPLGHI PEIHSLLMSI LSATIFAGIL LSAAAEIRDT RWLWRRSKTA TPLQWLLCFP
LGTRPSGRVF FWSYVFYLTR FLHMFRTIFA VLRSRRLAVS QLFCNSVMAF TSFLWLEFSQ
SYQILAILST TLVYSVVYGY RFWTGFGLPG SAFPSFVVNC QLVLVGCNLV SHAGVLTMHL
FKGGCNGIGA WGLNSVLNGA ILLLFLNFYV RMHSPMRRHI NKMNSQRNA