OLEH2_SESIN
ID OLEH2_SESIN Reviewed; 144 AA.
AC O04925;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Oleosin H2 {ECO:0000303|PubMed:12450125};
DE AltName: Full=Oleosin 15.5 kDa {ECO:0000303|PubMed:12450125, ECO:0000303|PubMed:9399587};
OS Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=4182 {ECO:0000312|EMBL:AAB58402.1};
RN [1] {ECO:0000312|EMBL:AAB58402.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Tainan 1 {ECO:0000303|PubMed:9399587};
RC TISSUE=Seed {ECO:0000303|PubMed:9399587};
RX PubMed=9399587; DOI=10.1093/oxfordjournals.jbchem.a021828;
RA Chen J.C., Lin R.H., Huang H.C., Tzen J.T.;
RT "Cloning, expression and isoform classification of a minor oleosin in
RT sesame oil bodies.";
RL J. Biochem. 122:819-824(1997).
RN [2]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12450125; DOI=10.1271/bbb.66.2146;
RA Tai S.S., Chen M.C., Peng C.C., Tzen J.T.;
RT "Gene family of oleosin isoforms and their structural stabilization in
RT sesame seed oil bodies.";
RL Biosci. Biotechnol. Biochem. 66:2146-2153(2002).
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000255|RuleBase:RU000540,
CC ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:9399587}. Membrane
CC {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein
CC {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins
CC exist at a monolayer lipid/water interface. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC {ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:9399587}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation. Expressed in
CC maturing seeds about 2 and half weeks after flowering. Expression
CC continues steadily thereafter until it decreases in the seed-drying
CC stage, reaching undetectable levels in mature seeds.
CC {ECO:0000269|PubMed:12450125}.
CC -!- DOMAIN: The proline-knot motif may be involved in the targeting to oil
CC bodies. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the oleosin family.
CC {ECO:0000255|RuleBase:RU000540}.
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; U97700; AAB58402.1; -; mRNA.
DR PIR; JC5703; JC5703.
DR AlphaFoldDB; O04925; -.
DR Proteomes; UP000504604; Genome assembly.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:UniProtKB.
DR GO; GO:0034389; P:lipid droplet organization; IC:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IC:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IEP:UniProtKB.
DR InterPro; IPR000136; Oleosin.
DR PANTHER; PTHR33203; PTHR33203; 1.
DR Pfam; PF01277; Oleosin; 1.
DR PROSITE; PS00811; OLEOSINS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lipid droplet; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:C3S7F0"
FT CHAIN 2..144
FT /note="Oleosin H2"
FT /id="PRO_0000449964"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 124..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 61..72
FT /note="Proline-knot"
FT /evidence="ECO:0000305|PubMed:12450125"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:C3S7F0"
SQ SEQUENCE 144 AA; 15446 MW; 43E6C011C29B7CF7 CRC64;
MADEPHDQRP TDVIKSYLPE KGPSTSQVLA VVTLFPLGAV LLCLAGLILT GTIIGLAVAT
PLFVIFSPIL VPAALTIALA VTGFLTSGAF GITALSSISW LLNYVRRMRG SLPEQLDHAR
RRVQETVGQK TREAGQRSQD VIRP