位置:首页 > 蛋白库 > ELO3L_ARATH
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024