OLEO2_ARATH
ID OLEO2_ARATH Reviewed; 199 AA.
AC Q39165; Q39164; Q41911;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Oleosin 21.2 kDa;
DE AltName: Full=Oleosin type 2;
GN OrderedLocusNames=At5g40420; ORFNames=MPO12.17;
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 STRAIN=cv. Columbia; TISSUE=Silique;
RX PubMed=8756608; DOI=10.1007/bf00021805;
RA Zou J., Brokx S.J., Taylor D.C.;
RT "Cloning of a cDNA encoding the 21.2 kDa oleosin isoform from Arabidopsis
RT thaliana and a study of its expression in a mutant defective in
RT diacylglycerol acyltransferase activity.";
RL Plant Mol. Biol. 31:429-433(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Silique;
RA Grellet F., Cooke R., Laudie M., Raynal M., Delseny 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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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] OF 1-111.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
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: In siliques, expression is first detected at stage
CC 7 when the siliques are green-brown. Expression then rises steadily to
CC reach a maximum at maturity. {ECO:0000269|PubMed:8756608}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; L40954; AAA87295.1; -; mRNA.
DR EMBL; X91956; CAA63022.1; -; mRNA.
DR EMBL; AB006702; BAB11599.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94546.1; -; Genomic_DNA.
DR EMBL; AY057590; AAL14385.1; -; mRNA.
DR EMBL; AY113011; AAM47319.1; -; mRNA.
DR EMBL; Z17657; CAA79025.1; -; mRNA.
DR PIR; S71253; S71253.
DR RefSeq; NP_198858.1; NM_123406.3.
DR AlphaFoldDB; Q39165; -.
DR BioGRID; 19291; 31.
DR IntAct; Q39165; 27.
DR STRING; 3702.AT5G40420.1; -.
DR iPTMnet; Q39165; -.
DR PaxDb; Q39165; -.
DR PRIDE; Q39165; -.
DR ProteomicsDB; 250807; -.
DR EnsemblPlants; AT5G40420.1; AT5G40420.1; AT5G40420.
DR GeneID; 834040; -.
DR Gramene; AT5G40420.1; AT5G40420.1; AT5G40420.
DR KEGG; ath:AT5G40420; -.
DR Araport; AT5G40420; -.
DR TAIR; locus:2170558; AT5G40420.
DR eggNOG; ENOG502S1R0; Eukaryota.
DR HOGENOM; CLU_101983_1_0_1; -.
DR InParanoid; Q39165; -.
DR OMA; GHETQGR; -.
DR OrthoDB; 1510479at2759; -.
DR PhylomeDB; Q39165; -.
DR PRO; PR:Q39165; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39165; baseline and differential.
DR Genevisible; Q39165; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0019915; P:lipid storage; IMP:TAIR.
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; IMP:TAIR.
DR InterPro; IPR000136; Oleosin.
DR PANTHER; PTHR33203; PTHR33203; 1.
DR Pfam; PF01277; Oleosin; 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..199
FT /note="Oleosin 21.2 kDa"
FT /id="PRO_0000108128"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..56
FT /note="Polar"
FT REGION 57..128
FT /note="Hydrophobic"
FT REGION 159..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:C3S7F1"
FT CONFLICT 93
FT /note="S -> A (in Ref. 6; CAA79025)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> G (in Ref. 2; CAA63022)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="R -> K (in Ref. 2; CAA63022)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="R -> G (in Ref. 2; CAA63022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 21279 MW; 0CC71620528F8BDF CRC64;
MADTHRVDRT DRHFQFQSPY EGGRGQGQYE GDRGYGGGGY KSMMPESGPS STQVLSLLIG
VPVVGSLLAL AGLLLAGSVI GLMVALPLFL LFSPVIVPAA LTIGLAMTGF LASGMFGLTG
LSSISWVMNY LRGTRRTVPE QLEYAKRRMA DAVGYAGQKG KEMGQHVQNK AQDVKQYDIS
KPHDTTTKGH ETQGRTTAA
