OLNB1_BRANA
ID OLNB1_BRANA Reviewed; 157 AA.
AC Q00650; Q39338; Q39352;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Oleosin-B1;
DE AltName: Full=Microspore-specific protein I3;
DE AltName: Full=Oleosin-B5;
DE Contains:
DE RecName: Full=Pollen coat protein B1;
DE AltName: Full=Pollen coat protein B5;
GN Name=OlnB1; Synonyms=I3, OlnB5, pol3;
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=Microspore;
RX PubMed=1863784; DOI=10.1007/bf00039509;
RA Roberts M.R., Robson F., Foster G.D., Draper J., Scott R.J.;
RT "A Brassica napus mRNA expressed specifically in developing microspores.";
RL Plant Mol. Biol. 17:295-299(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Anther;
RX PubMed=7766048; DOI=10.1007/bf00202607;
RA Roberts M.R., Hodge R., Scott R.;
RT "Brassica napus pollen oleosins possess a characteristic C-terminal
RT domain.";
RL Planta 195:469-470(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-12 AND 76-94, 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 {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 -!- 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. Highest
CC expression is in microspores entering and undergoing mitosis. No
CC expression is observed in male-sterile plants, green tissues or roots.
CC {ECO:0000269|PubMed:1863784}.
CC -!- DEVELOPMENTAL STAGE: Expressed after tetrad release, until the end of
CC the second pollen mitosis. Expressed in buds over 3 mm in length,
CC maximum expression is observed in 3-4 mm buds and decreases rapidly in
CC buds containing mature pollen. {ECO:0000269|PubMed:1863784}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40608.1; Type=Frameshift; Evidence={ECO:0000305};
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; X57332; CAA40608.1; ALT_FRAME; mRNA.
DR EMBL; X82019; CAA57544.1; -; mRNA.
DR EMBL; X82020; CAA57545.1; -; mRNA.
DR PIR; S16569; S16569.
DR PIR; S49448; S49448.
DR PIR; S50195; S50195.
DR AlphaFoldDB; Q00650; -.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid droplet; Membrane; Repeat; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9680961"
FT CHAIN 2..157
FT /note="Oleosin-B1"
FT /id="PRO_0000084122"
FT CHAIN 76..157
FT /note="Pollen coat protein B1"
FT /id="PRO_0000284880"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 119..122
FT /note="1"
FT REPEAT 123..126
FT /note="2"
FT REPEAT 127..130
FT /note="3"
FT REPEAT 131..134
FT /note="4"
FT REPEAT 135..138
FT /note="5"
FT REPEAT 139..142
FT /note="6"
FT REPEAT 143..146
FT /note="7"
FT REPEAT 147..150
FT /note="8"
FT REPEAT 151..154
FT /note="9"
FT REGION 2..20
FT /note="Polar"
FT REGION 21..138
FT /note="Hydrophobic"
FT REGION 119..122
FT /note="9 X 4 AA tandem repeats of P-[AR]-[AP]-[AKP]"
FT REGION 137..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12..13
FT /note="NA -> KP (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="S -> A (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="Q -> H (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="S -> A (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="R -> Q (in Ref. 1; CAA40608 and 2; CAA57544)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> A (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> K (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> E (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="R -> A (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> G (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> V (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..142
FT /note="PK -> AA (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> PKPAAAPSI (in Ref. 2; CAA57545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 15309 MW; A883168D99BEAC95 CRC64;
MGILRKKKHE RNASFKSVLT SILATQAATF LLLISGVSLA GTAAAFIATM PLFVVFSPIL
VPAGITTGLL TTGLAAAGGA GATAVTIILW LYKRATGKEP PAVLSKVLKK IIPGAAAAPR
AAPAAAPAAA PAAAPAAAPA PKPAAAPAPK PAAPPAL
