EPAD1_ORYSJ
ID EPAD1_ORYSJ Reviewed; 228 AA.
AC Q75GY0; A0A0P0W141; Q10FL6;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Non-specific lipid-transfer protein EPAD1 {ECO:0000305};
DE AltName: Full=Protein EXINE PATTERN DESIGNER 1 {ECO:0000303|PubMed:33093144};
DE Flags: Precursor;
GN Name=EPAD1 {ECO:0000303|PubMed:33093144};
GN OrderedLocusNames=Os03g0663900 {ECO:0000312|EMBL:BAS85619.1},
GN LOC_Os03g46110 {ECO:0000312|EMBL:ABF98043.1};
GN ORFNames=OSJNBa0034D21.11 {ECO:0000312|EMBL:AAS07321.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=30675653; DOI=10.1007/s00709-019-01349-3;
RA Ma T., Dong F., Luan D., Hu H., Zhao J.;
RT "Gene expression and localization of arabinogalactan proteins during the
RT development of anther, ovule, and embryo in rice.";
RL Protoplasma 256:909-922(2019).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 204-SER--SER-206.
RX PubMed=33093144; DOI=10.1105/tpc.20.00551;
RA Li H., Kim Y.J., Yang L., Liu Z., Zhang J., Shi H., Huang G., Persson S.,
RA Zhang D., Liang W.;
RT "Grass-specific EPAD1 is essential for pollen exine patterning in rice.";
RL Plant Cell 32:3961-3977(2020).
CC -!- FUNCTION: Plant non-specific lipid-transfer protein that binds
CC phospholipids in vitro (PubMed:33093144). Required for correct pollen
CC exine patterning by controlling the continuity and homogeneity of the
CC primexine distribution (PubMed:33093144).
CC {ECO:0000269|PubMed:33093144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33093144};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:33093144}. Note=Localizes
CC to the microspore plasma membrane. {ECO:0000269|PubMed:33093144}.
CC -!- TISSUE SPECIFICITY: Expressed in young panicles (PubMed:30675653).
CC Specifically expressed in pollen mother cells and young microspores
CC (PubMed:33093144). {ECO:0000269|PubMed:30675653,
CC ECO:0000269|PubMed:33093144}.
CC -!- DISRUPTION PHENOTYPE: Abnormal exine pattern of pollen grains and
CC complete male sterility. {ECO:0000269|PubMed:33093144}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAS85619.1; Type=Erroneous gene model prediction; 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; AC137991; AAS07321.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98043.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12750.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85619.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q75GY0; -.
DR STRING; 4530.OS03T0663900-00; -.
DR EnsemblPlants; Os03t0663900-00; Os03t0663900-00; Os03g0663900.
DR Gramene; Os03t0663900-00; Os03t0663900-00; Os03g0663900.
DR eggNOG; ENOG502R3EN; Eukaryota.
DR InParanoid; Q75GY0; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0010584; P:pollen exine formation; IMP:UniProtKB.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF14368; LTP_2; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipid-binding;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..228
FT /note="Non-specific lipid-transfer protein EPAD1"
FT /id="PRO_0000452251"
FT REGION 124..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..158
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 40..62
FT /evidence="ECO:0000250|UniProtKB:Q0IQK9"
FT DISULFID 63..105
FT /evidence="ECO:0000250|UniProtKB:Q0IQK9"
FT DISULFID 78..119
FT /evidence="ECO:0000250|UniProtKB:Q0IQK9"
FT MUTAGEN 204..206
FT /note="SSS->FFF: Prevents plama membrane localization; loss
FT of function."
FT /evidence="ECO:0000269|PubMed:33093144"
SQ SEQUENCE 228 AA; 22642 MW; B1014580238D2D6D CRC64;
MERSHLAVLL GLLAFAAGVP AAAAATAVEG AQAATAEASC EPSILATQVS LFCAPDMPTA
QCCEPVVASV DLGGGVPCLC RVAAEPQLII SGLNATHLLT LYAACGGLRP GGARLAAACE
GPAPPASIVT APPPPVAFRR KPPAREAPPP PPAAEKLSPP PQQHDDSDHN KRVGPLPRGS
PPPYAQSVPV GPAAAPPPPR SGASSSLQAP LAATTTIVAI TLIAAAQY
