OLEO4_ARATH
ID OLEO4_ARATH Reviewed; 191 AA.
AC Q42431; Q42180; Q42229; Q8LDN9; Q96277;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Oleosin 20.3 kDa;
DE AltName: Full=Oleosin type 4;
GN Name=OL2; OrderedLocusNames=At3g27660; ORFNames=MGF10.7;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Silique;
RX PubMed=8756606; DOI=10.1007/bf00021803;
RA Kirik V., Koelle K., Balzer H.-J., Baeumlein H.;
RT "Two new oleosin isoforms with altered expression patterns in seeds of the
RT Arabidopsis mutant fus3.";
RL Plant Mol. Biol. 31:413-417(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RA Raynal M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-72 AND 114-191.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
CC -!- FUNCTION: May have a structural role to stabilize the lipid body during
CC desiccation of the seed by preventing coalescence of the oil. Probably
CC interacts with both lipid and phospholipid moieties of lipid bodies.
CC May also provide recognition signals for specific lipase anchorage in
CC lipolysis during seedling growth (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250}. Membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Surface
CC of oil bodies. Oleosins exist at a monolayer lipid/water interface (By
CC similarity). {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expression increases continuously throughout
CC embryonic development. {ECO:0000269|PubMed:8756606}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; Z54164; CAA90877.1; -; mRNA.
DR EMBL; X91918; CAA63011.1; -; mRNA.
DR EMBL; AB018114; BAB02690.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77349.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64789.1; -; Genomic_DNA.
DR EMBL; AY054540; AAK96731.1; -; mRNA.
DR EMBL; AY064657; AAL47366.1; -; mRNA.
DR EMBL; AY085886; AAM63098.1; -; mRNA.
DR EMBL; Z27260; CAA81771.1; -; mRNA.
DR EMBL; Z29859; CAA82822.1; -; mRNA.
DR PIR; S71286; S71286.
DR RefSeq; NP_001326794.1; NM_001338903.1.
DR RefSeq; NP_189403.1; NM_113682.4.
DR AlphaFoldDB; Q42431; -.
DR BioGRID; 7718; 2.
DR STRING; 3702.AT3G27660.1; -.
DR PaxDb; Q42431; -.
DR PRIDE; Q42431; -.
DR ProteomicsDB; 250905; -.
DR EnsemblPlants; AT3G27660.1; AT3G27660.1; AT3G27660.
DR EnsemblPlants; AT3G27660.2; AT3G27660.2; AT3G27660.
DR GeneID; 822388; -.
DR Gramene; AT3G27660.1; AT3G27660.1; AT3G27660.
DR Gramene; AT3G27660.2; AT3G27660.2; AT3G27660.
DR KEGG; ath:AT3G27660; -.
DR Araport; AT3G27660; -.
DR TAIR; locus:2089189; AT3G27660.
DR eggNOG; ENOG502S1R0; Eukaryota.
DR HOGENOM; CLU_101983_1_0_1; -.
DR OMA; GMKGKEM; -.
DR OrthoDB; 1510479at2759; -.
DR PhylomeDB; Q42431; -.
DR PRO; PR:Q42431; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42431; baseline and differential.
DR Genevisible; Q42431; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0050826; P:response to freezing; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IGI:TAIR.
DR GO; GO:0010344; P:seed oilbody biogenesis; IGI:TAIR.
DR InterPro; IPR000136; Oleosin.
DR PANTHER; PTHR33203; PTHR33203; 1.
DR Pfam; PF01277; Oleosin; 1.
DR PROSITE; PS00811; OLEOSINS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Lipid droplet; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:C3S7F1"
FT CHAIN 2..191
FT /note="Oleosin 20.3 kDa"
FT /id="PRO_0000108130"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 2..54
FT /note="Polar"
FT REGION 55..128
FT /note="Hydrophobic"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:C3S7F1"
FT CONFLICT 66
FT /note="L -> AI (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 127..132
FT /note="NYLRGT -> QLPPWA (in Ref. 7; CAA82822)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="L -> V (in Ref. 7; CAA82822)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> S (in Ref. 6; AAM63098)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="S -> P (in Ref. 2; CAA63011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 20313 MW; 75EA042B9595C23A CRC64;
MANVDRDRRV HVDRTDKRVH QPNYEDDVGF GGYGGYGAGS DYKSRGPSTN QILALIAGVP
IGGTLLTLAG LTLAGSVIGL LVSIPLFLLF SPVIVPAALT IGLAVTGILA SGLFGLTGLS
SVSWVLNYLR GTSDTVPEQL DYAKRRMADA VGYAGMKGKE MGQYVQDKAH EARETEFMTE
THEPGKARRG S
