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OLNB3_BRANA
ID   OLNB3_BRANA             Reviewed;         424 AA.
AC   Q42626;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Oleosin-B3;
DE   Contains:
DE     RecName: Full=Pollen coat protein B3;
GN   Name=OlnB3 {ECO:0000303|PubMed:8653113};
GN   Synonyms=STA 41-2 {ECO:0000312|EMBL:AAA70400.1};
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:AAA70400.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Westar {ECO:0000312|EMBL:AAA70400.1};
RC   TISSUE=Tapetum {ECO:0000312|EMBL:AAA70400.1};
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 109-129, 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 109-128, 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; L33282; AAA70400.1; -; mRNA.
DR   PIR; T08093; T08093.
DR   RefSeq; NP_001303026.1; NM_001316097.1.
DR   AlphaFoldDB; Q42626; -.
DR   SMR; Q42626; -.
DR   EnsemblPlants; CDY68880; CDY68880; GSBRNA2T00080952001.
DR   GeneID; 106449581; -.
DR   Gramene; CDY68880; CDY68880; GSBRNA2T00080952001.
DR   KEGG; bna:106449581; -.
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; 3.
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..424
FT                   /note="Oleosin-B3"
FT                   /id="PRO_0000284754"
FT   CHAIN           109..424
FT                   /note="Pollen coat protein B3"
FT                   /evidence="ECO:0000269|PubMed:8653113"
FT                   /id="PRO_0000284755"
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          111..120
FT                   /note="1-1"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          121..130
FT                   /note="1-2"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          131..140
FT                   /note="1-3"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          141..150
FT                   /note="1-4"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          196..202
FT                   /note="2-1"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          203..209
FT                   /note="2-2"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          210..216
FT                   /note="2-3"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          217..223
FT                   /note="2-4"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          241..258
FT                   /note="3-1"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          259..276
FT                   /note="3-2"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          277..294
FT                   /note="3-3"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          301..318
FT                   /note="3-4"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          319..336
FT                   /note="3-5"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          337..354
FT                   /note="3-6"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          396..400
FT                   /note="4-1"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          401..405
FT                   /note="4-2"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          406..410
FT                   /note="4-3"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REPEAT          411..415
FT                   /note="4-4"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REGION          1..37
FT                   /note="Polar"
FT                   /evidence="ECO:0000255"
FT   REGION          38..119
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255"
FT   REGION          111..150
FT                   /note="4 X 10 AA tandem repeats of I-P-[EV]-S-I-K-P-S-N-
FT                   [IV]"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REGION          164..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..223
FT                   /note="4 X 7 AA tandem repeats of E-[SD]-[KT]-H-G-K-G"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REGION          241..354
FT                   /note="6 X 18 AA tandem repeats of [KR]-H-[EG]-[SG]-G-G-
FT                   [SA]-[PSA]-M-G-G-G-K-H-[GE]-S-[GV]-G"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   REGION          396..415
FT                   /note="4 X 5 AA tandem repeats of S-S-D-G-S"
FT                   /evidence="ECO:0000269|PubMed:7849761"
FT   COMPBIAS        164..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  42086 MW;  751C6D971FBBA6B0 CRC64;
     MRNEIQNETA QTDQTQGSMF SFFNLFPFLL PMFEVIKMVV ASVASVVYLG FAGVTLSGSA
     VALAVSTPLF IIFSPILLPA IAATTVLAAG LGSKKVAAAP AASPSLSLLG IPESIKPSNV
     IPESIKPSNI IPESIKPSNI IPVSIKPSNI KDKIKDTIGK VKNKIKAKQE EKSKGKSEDS
     SKGKGKSKGE DTTTDEDKHG KGESKHGKGE SKHGKGESTH GKGGKHGSEG SSMDEGKHGG
     KHGSGGSPMG GGKHGSGGKH ESGGSPMGGG KHGSGGKHES GGASMGGGKH ESVGKHGSGG
     KHESGGSPMG GGKHGSGGKH ESGGASMGGG KHGSGGRHEG GGSAMGGGKH GSGGKHGSEG
     KHGGEGSSMG KNSLSKNKKE FHYRGQAMDA SSTSESSDGS SSDGSSSDGS SSDGSSHGSG
     GKHI
 
 
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