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OLNB2_BRANA
ID   OLNB2_BRANA             Reviewed;         183 AA.
AC   P29526; P81097;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Oleosin-B2;
DE   AltName: Full=Oleosin-C98;
DE   Contains:
DE     RecName: Full=Pollen coat protein B2;
DE   Flags: Fragment;
GN   Name=OlnB2; Synonyms=C98;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Anther;
RX   PubMed=8374615; DOI=10.1111/j.1365-313x.1993.00629.x;
RA   Roberts M.R., Hodge R., Ross J.H.E., Sorensen A., Murphy D.J., Draper J.,
RA   Scott R.;
RT   "Characterization of a new class of oleosins suggests a male gametophyte-
RT   specific lipid storage pathway.";
RL   Plant J. 3:629-636(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 104-120, AND FUNCTION.
RC   STRAIN=cv. Topas; TISSUE=Pollen;
RX   PubMed=9680961;
RA   Murphy D.J., Ross J.H.E.;
RT   "Biosynthesis, targeting and processing of oleosin-like proteins, which are
RT   major pollen coat components in Brassica napus.";
RL   Plant J. 13:1-16(1998).
CC   -!- FUNCTION: Many of the major pollen coat proteins are derived from
CC       endoproteolytic cleavage of oleosin-like proteins.
CC       {ECO:0000269|PubMed:9680961}.
CC   -!- SUBCELLULAR LOCATION: Lipid droplet. Membrane; Multi-pass membrane
CC       protein. Note=Surface of oil bodies. Oleosins exist at a monolayer
CC       lipid/water interface.
CC   -!- TISSUE SPECIFICITY: The full-length protein is found in the tapetal
CC       lipid bodies of immature anthers, the proteolytically cleaved C-
CC       terminal product is found on the coats of pollen grains. Not present in
CC       seeds. {ECO:0000269|PubMed:8374615}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing buds, until the pollen is
CC       near to maturity. {ECO:0000269|PubMed:8374615}.
CC   -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR   EMBL; X67142; CAA47623.1; -; mRNA.
DR   PIR; S24960; S24960.
DR   AlphaFoldDB; P29526; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012511; C:monolayer-surrounded lipid storage body; IEA:InterPro.
DR   GO; GO:0022414; P:reproductive process; IEA:UniProt.
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   Direct protein sequencing; Lipid droplet; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..183
FT                   /note="Oleosin-B2"
FT                   /id="PRO_0000108135"
FT   CHAIN           104..183
FT                   /note="Pollen coat protein B2"
FT                   /id="PRO_0000284379"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          <1..23
FT                   /note="Polar"
FT   REGION          24..95
FT                   /note="Hydrophobic"
FT   CONFLICT        108
FT                   /note="L -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   183 AA;  18149 MW;  198A5D3B6DF3045A CRC64;
     QASIFSRFFR MFSFIFPFVN VIKLIIASVT SLVCLAFSCV ALGGSAVALI VSTPLFIMFS
     PILVPATIAT TLLASGLMAG TTLGLTGIGL IMGLVRTAGG VSLLQSPLRK IIVNRIKARL
     GGGGGGSRLA RLKKILGLLN KLRGMGAGGA AAPAAEPAPA AEAAPAAEAA PAAAPAAAPA
     AAP
 
 
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