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OLEH1_SESIN
ID   OLEH1_SESIN             Reviewed;         166 AA.
AC   Q9FUJ9;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Oleosin H1 {ECO:0000303|PubMed:12450125};
DE   AltName: Full=Allergen Ses i 4 {ECO:0000303|PubMed:16436145};
DE   AltName: Full=Oleosin 17 kDa {ECO:0000303|PubMed:12450125, ECO:0000303|PubMed:16436145};
DE   AltName: Allergen=Ses i 4.0101 {ECO:0000305};
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:AAG23840.1};
RN   [1] {ECO:0000312|EMBL:AAG23840.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Tainan 1 {ECO:0000303|PubMed:12450125};
RC   TISSUE=Seed {ECO:0000303|PubMed:12450125};
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).
RN   [2]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALLERGEN.
RX   PubMed=16436145; DOI=10.1111/j.1398-9995.2006.01013.x;
RA   Leduc V., Moneret-Vautrin D.A., Tzen J.T., Morisset M., Guerin L.,
RA   Kanny G.;
RT   "Identification of oleosins as major allergens in sesame seed allergic
RT   patients.";
RL   Allergy 61:349-356(2006).
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:16436145}. 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:16436145}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during seed maturation. Expressed in
CC       maturing seeds about 2 weeks after flowering. Expression continues
CC       steadily thereafter until it decreases in the seed-drying stage,
CC       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   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in all of
CC       the 32 patients tested allergic to sesame seeds.
CC       {ECO:0000269|PubMed:16436145}.
CC   -!- SIMILARITY: Belongs to the oleosin family.
CC       {ECO:0000255|RuleBase:RU000540}.
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DR   EMBL; AF302807; AAG23840.1; -; mRNA.
DR   RefSeq; NP_001292915.1; NM_001305986.1.
DR   AlphaFoldDB; Q9FUJ9; -.
DR   Allergome; 1440; Ses i 4.
DR   Allergome; 3474; Ses i 4.0101.
DR   EnsemblPlants; SIN_1007879.t; SIN_1007879.t.cds1; SIN_1007879.
DR   GeneID; 105177100; -.
DR   Gramene; SIN_1007879.t; SIN_1007879.t.cds1; SIN_1007879.
DR   KEGG; sind:105177100; -.
DR   OrthoDB; 1510479at2759; -.
DR   PhylomeDB; Q9FUJ9; -.
DR   Proteomes; UP000504604; Linkage group LG15.
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; Allergen; Lipid droplet; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:C3S7F0"
FT   CHAIN           2..166
FT                   /note="Oleosin H1"
FT                   /id="PRO_0000449963"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           73..84
FT                   /note="Proline-knot"
FT                   /evidence="ECO:0000305|PubMed:12450125"
FT   COMPBIAS        1..22
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:C3S7F0"
SQ   SEQUENCE   166 AA;  17373 MW;  6BDA3EB2671F3CA0 CRC64;
     MADRDRPHPH QIQVHPQHPH RYEGGVKSLL PQKGPSTTQI LAIITLLPIS GTLLCLAGIT
     LVGTLIGLAV ATPVFVIFSP VLVPAAILIA GAVTAFLTSG AFGLTGLSSL SWVLNSFRRA
     TGQGPLEYAK RGVQEGTLYV GEKTKQAGEA IKSTAKEGGR EGTART
 
 
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