OLNB4_BRANA
ID OLNB4_BRANA Reviewed; 377 AA.
AC Q42627;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Oleosin-B4;
DE Contains:
DE RecName: Full=Pollen coat protein B4;
GN Name=OlnB4 {ECO:0000303|PubMed:8653113};
GN Synonyms=STA 41-9 {ECO:0000312|EMBL:AAA70401.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAA70401.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Westar {ECO:0000312|EMBL:AAA70401.1};
RC TISSUE=Tapetum {ECO:0000312|EMBL:AAA70401.1};
RX PubMed=7849761; DOI=10.1046/j.1365-313x.1994.6060927.x;
RA Robert L.S., Gerster J., Allard S., Cass L., Simmonds J.;
RT "Molecular characterization of two Brassica napus genes related to oleosins
RT which are highly expressed in the tapetum.";
RL Plant J. 6:927-933(1994).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-10 AND 113-130, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Topas {ECO:0000269|PubMed:9680961};
RC TISSUE=Pollen {ECO:0000269|PubMed:9680961};
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).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 113-128, FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Topas {ECO:0000269|PubMed:8653113};
RC TISSUE=Pollen {ECO:0000269|PubMed:8653113};
RX PubMed=8653113; DOI=10.1046/j.1365-313x.1996.9050625.x;
RA Ross J.H.E., Murphy D.J.;
RT "Characterization of anther-expressed genes encoding a major class of
RT extracellular oleosin-like proteins in the pollen coat of Brassicaceae.";
RL Plant J. 9:625-637(1996).
CC -!- FUNCTION: Many of the major pollen coat proteins are derived from
CC endoproteolytic cleavage of oleosin-like proteins.
CC {ECO:0000269|PubMed:8653113, 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|UniProtKB:P29526}.
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. No expression
CC is detected in other flower organs, siliques or seedlings.
CC {ECO:0000269|PubMed:7849761, ECO:0000269|PubMed:9680961}.
CC -!- DEVELOPMENTAL STAGE: Only expressed in early developing buds and
CC anthers, mRNA is first detected in 2-3 mm buds, expression levels peak
CC in 4-5 mm buds and are absent in later stages of development.
CC {ECO:0000269|PubMed:7849761, ECO:0000269|PubMed:8653113,
CC ECO:0000269|PubMed:9680961}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000255}.
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DR EMBL; L33283; AAA70401.1; -; mRNA.
DR PIR; T08095; T08095.
DR RefSeq; NP_001302602.1; NM_001315673.1.
DR AlphaFoldDB; Q42627; -.
DR EnsemblPlants; CDX70048; CDX70048; GSBRNA2T00136147001.
DR GeneID; 106419230; -.
DR Gramene; CDX70048; CDX70048; GSBRNA2T00136147001.
DR KEGG; bna:106419230; -.
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; 2.
DR Pfam; PF01277; Oleosin; 1.
DR PROSITE; PS00811; OLEOSINS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lipid droplet; Membrane; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="Oleosin-B4"
FT /id="PRO_0000284756"
FT CHAIN 113..377
FT /note="Pollen coat protein B4"
FT /evidence="ECO:0000269|PubMed:8653113"
FT /id="PRO_0000284757"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 115..124
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 125..134
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 135..144
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 196..202
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 196..202
FT /note="2.1"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 204..208
FT /note="2-2; truncated"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 209..215
FT /note="2-3"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 216..222
FT /note="2-4"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 230..247
FT /note="3-1"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 260..277
FT /note="3-2"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 278..295
FT /note="3-3"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 296..313
FT /note="3-4"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 355..359
FT /note="4-1"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 360..363
FT /note="4-2; truncated"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REPEAT 364..368
FT /note="4-3"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REGION 1..37
FT /note="Polar"
FT /evidence="ECO:0000255"
FT REGION 38..133
FT /note="Hydrophobic"
FT /evidence="ECO:0000255"
FT REGION 115..144
FT /note="3 X 10 AA tandem repeats of I-P-E-[SG]-I-K-P-S-N-
FT [IV]"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REGION 158..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..222
FT /note="3 X 6 AA tandem repeats of E-[SD]-[KT]-H-G-[KS]-G"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REGION 230..313
FT /note="4 X 18 AA tandem repeats of K-H-E-S-G-G-[SA]-[PSA]-
FT M-G-G-G-K-H-G-S-[GE]-G"
FT /evidence="ECO:0000269|PubMed:7849761"
FT REGION 355..368
FT /note="3 X 5 AA tandem repeats of S-S-D-G-S"
FT /evidence="ECO:0000269|PubMed:7849761"
FT COMPBIAS 158..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 37647 MW; 5DC8BCEA234E1B12 CRC64;
MRNEIQNETA QTDQTQGSMF SFFNLFPFLL PMFEVIKMVV ASVASVVYLG FAGVTLSGSA
VALAVSTPLF IIFSPILLPA IAATTVLAAG LGGKKVAAAP EASPAASPSL SLLGIPESIK
PSNIIPESIK PSNIIPEGIK PSNIKDKIKD TIGKVKNKIK AKKEEKSKGK SEDSSKGKGK
SKGEDTTTDD DTTTDEDKHG SGAKHGKGES KHGKGESTHG KGGKHGSEGK HGSGGSSMGG
GKHGSGGKHE TGGKHGSGGK HESGGSPMGG GKHGSEGKHG SGGASMGGGK HGSGGKHESG
GSAMGGGKHG SGGKHGSEGK HGGEGSSMGK NSLSKKKKEF HYRGQAMDAS STSESSDGSS
DGSSSDGSSH GSGGKHI
