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OLEG_PINMS
ID   OLEG_PINMS              Reviewed;         138 AA.
AC   A0A060L102;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-SEP-2014, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Oleosin G {ECO:0000303|PubMed:24954070, ECO:0000312|EMBL:AIC74543.1};
OS   Pinus massoniana (Chinese red pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=88730;
RN   [1] {ECO:0000312|EMBL:AIC74543.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 93-106; 95-106; 109-121 AND
RP   122-130, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Megagametophyte {ECO:0000303|PubMed:24954070};
RX   PubMed=24954070; DOI=10.1016/j.plaphy.2014.05.015;
RA   Pasaribu B., Chung T.Y., Chen C.S., Wang S.L., Jiang P.L., Tzen J.T.;
RT   "Identification of caleosin and two oleosin isoforms in oil bodies of pine
RT   megagametophytes.";
RL   Plant Physiol. Biochem. 82:142-150(2014).
CC   -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:24954070}.
CC       Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
CC       Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water
CC       interface. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in megagametophytes (at protein level).
CC       {ECO:0000269|PubMed:24954070}.
CC   -!- DOMAIN: The proline-knot motif may be involved in targeting to lipid
CC       bodies. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; KJ415242; AIC74543.1; -; mRNA.
DR   AlphaFoldDB; A0A060L102; -.
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   InterPro; IPR000136; Oleosin.
DR   PANTHER; PTHR33203; PTHR33203; 1.
DR   Pfam; PF01277; Oleosin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipid droplet; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:C3S7F0"
FT   CHAIN           2..138
FT                   /note="Oleosin G"
FT                   /id="PRO_0000449962"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           47..58
FT                   /note="Proline-knot"
FT                   /evidence="ECO:0000305|PubMed:24954070"
SQ   SEQUENCE   138 AA;  14717 MW;  D22A3BD434F9B97C CRC64;
     MQKIHDHTPN PTQILGFITL FVSGAVLLFL TGLTLTGTVV GLVVLTPVLI FFSPILIPLA
     TVLFVAVAGF LSAGGFGLAA LSAISWLYNY IKGRHPPGAD QIDYARMRIA DTATHVKDYA
     REYGGYLQSK IQDAAPGA
 
 
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