FLO6_ORYSJ
ID FLO6_ORYSJ Reviewed; 529 AA.
AC Q10F03; B9FAN7; Q0DPI8; Q6AVV5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein FLOURY ENDOSPERM 6, chloroplastic {ECO:0000303|PubMed:24456533};
DE AltName: Full=SKIPa-interacting protein 4 {ECO:0000303|PubMed:19339499};
DE Flags: Precursor;
GN Name=FLO6 {ECO:0000303|PubMed:24456533};
GN Synonyms=SIP4 {ECO:0000303|PubMed:19339499};
GN OrderedLocusNames=Os03g0686900 {ECO:0000312|EMBL:BAS85812.1},
GN LOC_Os03g48170 {ECO:0000312|EMBL:ABF98262.1};
GN ORFNames=OsJ_12152 {ECO:0000312|EMBL:EEE59721.1},
GN OSJNBb0024N19.10 {ECO:0000312|EMBL:AAT85062.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH SKIPA.
RX PubMed=19339499; DOI=10.1073/pnas.0901940106;
RA Hou X., Xie K., Yao J., Qi Z., Xiong L.;
RT "A homolog of human ski-interacting protein in rice positively regulates
RT cell viability and stress tolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6410-6415(2009).
RN [8]
RP FUNCTION, INTERACTION WITH ISA1, SUBCELLULAR LOCATION, DOMAIN CBM, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24456533; DOI=10.1111/tpj.12444;
RA Peng C., Wang Y., Liu F., Ren Y., Zhou K., Lv J., Zheng M., Zhao S.,
RA Zhang L., Wang C., Jiang L., Zhang X., Guo X., Bao Y., Wan J.;
RT "FLOURY ENDOSPERM6 encodes a CBM48 domain-containing protein involved in
RT compound granule formation and starch synthesis in rice endosperm.";
RL Plant J. 77:917-930(2014).
CC -!- FUNCTION: Involved in compound starch granule formation and starch
CC synthesis in endosperm. May act as a regulatory scaffolding protein and
CC affect starch synthesis and compound starch granule formation through
CC direct interaction with isoamylase 1 (ISA1). Binds starch, amylopectin
CC and amylose through its C-terminal carbohydrate-binding domain (CBM) in
CC vitro. {ECO:0000269|PubMed:24456533}.
CC -!- SUBUNIT: Interacts with SKIPA (PubMed:19339499). Interacts with ISA1
CC (PubMed:24456533). {ECO:0000269|PubMed:19339499,
CC ECO:0000269|PubMed:24456533}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24456533}. Note=Localizes to granule-like
CC structures in chloroplasts. {ECO:0000269|PubMed:24456533}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and panicles. Expressed
CC at lower levels in roots and developing seeds.
CC {ECO:0000269|PubMed:24456533}.
CC -!- DOMAIN: Contains a C-terminal (448-529) carbohydrate-binding domain
CC (CBM). {ECO:0000305|PubMed:24456533}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in plant height. Reduced size of
CC the endosperm, reduced starch content of the endosperm and floury
CC (opaque) endosperm. {ECO:0000269|PubMed:24456533}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT85062.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF12850.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC092779; AAT85062.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF98262.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12850.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014959; BAS85812.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE59721.1; -; Genomic_DNA.
DR EMBL; AK287681; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015630691.1; XM_015775205.1.
DR AlphaFoldDB; Q10F03; -.
DR STRING; 4530.OS03T0686900-01; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR PaxDb; Q10F03; -.
DR PRIDE; Q10F03; -.
DR EnsemblPlants; Os03t0686900-01; Os03t0686900-01; Os03g0686900.
DR GeneID; 4333759; -.
DR Gramene; Os03t0686900-01; Os03t0686900-01; Os03g0686900.
DR KEGG; osa:4333759; -.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_020708_0_0_1; -.
DR OMA; LEGKMAM; -.
DR OrthoDB; 440758at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:2001066; F:amylopectin binding; IDA:UniProtKB.
DR GO; GO:2001070; F:starch binding; IDA:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; IMP:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..529
FT /note="Protein FLOURY ENDOSPERM 6, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000442182"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 400..452
FT /evidence="ECO:0000255"
FT COMPBIAS 39..57
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="T -> Y (in Ref. 5; EEE59721)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="E -> K (in Ref. 5; EEE59721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 57988 MW; 3DC4942DA88D0CF4 CRC64;
MLPLLLPLPV TPPPPLPSPT LTLAPASAPR RRLVLLAAAA PHHHHHHRRR RVYRRQRAAP
TQTRAPRRTL SASNAARGEE DLEEAIYEFM RRSDKPGAFP TRAELVAAGR ADLAAAVDAC
GGWLSLGWSS GGAEAGRASS SVGVHPDYPP EAGAAAAAGG ASDLAQGAVW ASSREAEASP
SGRQPETEEE ETETKFGTGL DGMLTRLQRE RERVRPPLPR SSDGAGGERD NVALMGQSGA
PSHSATGGRY TPKVPDNGNI HSYHPQNGAL EHNKSSKSLT NDAWRTWSLD KGGFSDFQAA
EIHSTNSRKS FRHDGLDILA QDDVHGPSNG VAVHDYDIND VDSERDDIHA RLQNLELDLT
AALHTLRSRF DKVISDMSEG DGAKAPNGLS DDWEFEETKV MQAQEELRSI RAKIAVLEGK
MALEIIEKNK IIEEKQRRLD EAEKALSELR TVYIVWSNPA SEVLLTGSFD GWTSQRRMER
SERGTFSLNL RLYPGRYEIK FIVDGVWRND PLRPLVSNNG HENNLLTVT
