OLEO5_ARATH
ID OLEO5_ARATH Reviewed; 183 AA.
AC Q9SS98;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Oleosin 5;
GN OrderedLocusNames=At3g01570; ORFNames=F4P13.12;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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).
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 -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; AC009325; AAF01542.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73689.1; -; Genomic_DNA.
DR EMBL; AY059936; AAL24418.1; -; mRNA.
DR EMBL; AY081655; AAM10217.1; -; mRNA.
DR RefSeq; NP_186806.1; NM_111023.3.
DR AlphaFoldDB; Q9SS98; -.
DR SMR; Q9SS98; -.
DR BioGRID; 6439; 3.
DR IntAct; Q9SS98; 1.
DR STRING; 3702.AT3G01570.1; -.
DR PaxDb; Q9SS98; -.
DR PRIDE; Q9SS98; -.
DR ProteomicsDB; 250966; -.
DR EnsemblPlants; AT3G01570.1; AT3G01570.1; AT3G01570.
DR GeneID; 821106; -.
DR Gramene; AT3G01570.1; AT3G01570.1; AT3G01570.
DR KEGG; ath:AT3G01570; -.
DR Araport; AT3G01570; -.
DR TAIR; locus:2084223; AT3G01570.
DR eggNOG; ENOG502S1R0; Eukaryota.
DR HOGENOM; CLU_101983_1_1_1; -.
DR InParanoid; Q9SS98; -.
DR OMA; DVRTHSH; -.
DR OrthoDB; 1510479at2759; -.
DR PhylomeDB; Q9SS98; -.
DR PRO; PR:Q9SS98; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SS98; baseline and differential.
DR Genevisible; Q9SS98; 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; IBA:GO_Central.
DR GO; GO:0010344; P:seed oilbody biogenesis; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR InterPro; IPR000515; MetI-like.
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 Lipid droplet; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..183
FT /note="Oleosin 5"
FT /id="PRO_0000108131"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Polar"
FT /evidence="ECO:0000250"
FT REGION 40..113
FT /note="Hydrophobic"
FT /evidence="ECO:0000250"
FT REGION 144..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 19755 MW; 56B1C3C6F18AC6DD CRC64;
MADVRTHSHQ LQVHPQRQHE GGIKVLYPQS GPSSTQVLAV FVGVPIGGTL LTIAGLTLAG
SVIGLMLAFP LFLIFSPVIV PAAFVIGLAM TGFLASGAIG LTGLSSMSWV LNYIRRAGQH
IPEELEEAKH RLADMAEYVG QRTKDAGQTI EDKAHDVREA KTFDVRDRDT TKGTHNVRDT
KTT
