PAP7_ARATH
ID PAP7_ARATH Reviewed; 273 AA.
AC Q5M755; F4KFC4; Q9FIC4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Fibrillin-5, chloroplastic {ECO:0000303|PubMed:21571574};
DE AltName: Full=Plastid-lipid-associated protein 7 {ECO:0000305};
DE Flags: Precursor;
GN Name=FBN5 {ECO:0000303|PubMed:21571574};
GN Synonyms=FIB5 {ECO:0000305}, PAP7 {ECO:0000305};
GN OrderedLocusNames=At5g09820 {ECO:0000312|Araport:AT5G09820};
GN ORFNames=MYH9.3 {ECO:0000312|EMBL:BAB09403.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21571574; DOI=10.1016/j.tplants.2011.03.014;
RA Singh D.K., McNellis T.W.;
RT "Fibrillin protein function: the tip of the iceberg?";
RL Trends Plant Sci. 16:432-441(2011).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
RN [7]
RP FUNCTION, INTERACTION WITH SPS1 AND SPS2, SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, AND DISRUPTION PHENOTYPE.
RX PubMed=26432861; DOI=10.1105/tpc.15.00707;
RA Kim E.H., Lee Y., Kim H.U.;
RT "Fibrillin 5 is essential for plastoquinone-9 biosynthesis by binding to
RT solanesyl diphosphate synthases in Arabidopsis.";
RL Plant Cell 27:2956-2971(2015).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=28751900; DOI=10.3389/fpls.2017.01197;
RA Kim E.H., Lee D.W., Lee K.R., Jung S.J., Jeon J.S., Kim H.U.;
RT "Conserved function of Fibrillin5 in the plastoquinone-9 biosynthetic
RT pathway in Arabidopsis and rice.";
RL Front. Plant Sci. 8:1197-1197(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=29741733; DOI=10.1093/pcp/pcy093;
RA Otsubo M., Ikoma C., Ueda M., Ishii Y., Tamura N.;
RT "Functional role of Fibrillin5 in acclimation to photooxidative stress.";
RL Plant Cell Physiol. 59:1670-1682(2018).
CC -!- FUNCTION: [Isoform 1]: Essential for plastoquinone-9 (PQ-9)
CC biosynthesis (PubMed:26432861, PubMed:29741733). Interacts with the
CC diphosphate synthases SPS1 and SPS2, and binds to the hydrophobic
CC solanesyl moiety, which is generated by SPS1 and SPS2, in FBN5-SPS
CC homodimeric complexes to stimulate the enzyme activity of SPS1 and SPS2
CC (PubMed:26432861). {ECO:0000269|PubMed:26432861,
CC ECO:0000269|PubMed:29741733}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with SPS1 and SPS2.
CC {ECO:0000269|PubMed:26432861}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22274653, ECO:0000269|PubMed:26432861,
CC ECO:0000269|PubMed:29741733}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=FBN5-B {ECO:0000303|PubMed:26432861}, FBN5
CC {ECO:0000303|PubMed:29741733};
CC IsoId=Q5M755-1; Sequence=Displayed;
CC Name=2; Synonyms=FBN5-A {ECO:0000303|PubMed:26432861}, FBN5-259
CC {ECO:0000303|PubMed:29741733};
CC IsoId=Q5M755-2; Sequence=VSP_060147, VSP_060148;
CC -!- TISSUE SPECIFICITY: Expressed in developing roots, developing leaves,
CC young stems and sepals. {ECO:0000269|PubMed:29741733}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality (PubMed:26432861,
CC PubMed:28751900). Severe reduced growth, strong reduction of levels of
CC plastoquinone-9 (PQ-9), and loss of plastochromanol-8 (PC-8) in leaves
CC when grown on MS medium supplemented with sucrose (PubMed:26432861,
CC PubMed:28751900). Severe decrease of photosynthetic performance and
CC higher levels of reactive oxygen species (ROS) under cold stress
CC (PubMed:26432861, PubMed:29741733). {ECO:0000269|PubMed:26432861,
CC ECO:0000269|PubMed:28751900, ECO:0000269|PubMed:29741733}.
CC -!- SIMILARITY: Belongs to the PAP/fibrillin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016893; BAB09403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91451.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91452.1; -; Genomic_DNA.
DR EMBL; BT020393; AAV91339.1; -; mRNA.
DR EMBL; AK228700; BAF00604.1; -; mRNA.
DR RefSeq; NP_001031862.1; NM_001036785.3. [Q5M755-1]
DR RefSeq; NP_001330170.1; NM_001343070.1.
DR RefSeq; NP_196544.3; NM_121019.5. [Q5M755-2]
DR AlphaFoldDB; Q5M755; -.
DR BioGRID; 16120; 2.
DR STRING; 3702.AT5G09820.2; -.
DR PaxDb; Q5M755; -.
DR PRIDE; Q5M755; -.
DR ProteomicsDB; 201634; -.
DR ProteomicsDB; 248637; -. [Q5M755-1]
DR EnsemblPlants; AT5G09820.1; AT5G09820.1; AT5G09820. [Q5M755-2]
DR EnsemblPlants; AT5G09820.2; AT5G09820.2; AT5G09820. [Q5M755-1]
DR GeneID; 830842; -.
DR Gramene; AT5G09820.1; AT5G09820.1; AT5G09820. [Q5M755-2]
DR Gramene; AT5G09820.2; AT5G09820.2; AT5G09820. [Q5M755-1]
DR KEGG; ath:AT5G09820; -.
DR Araport; AT5G09820; -.
DR TAIR; locus:2178133; AT5G09820.
DR eggNOG; ENOG502QRU1; Eukaryota.
DR HOGENOM; CLU_069245_2_0_1; -.
DR OMA; LTIRANY; -.
DR OrthoDB; 1286171at2759; -.
DR PhylomeDB; Q5M755; -.
DR PRO; PR:Q5M755; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5M755; baseline and differential.
DR Genevisible; Q5M755; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0010236; P:plastoquinone biosynthetic process; IMP:TAIR.
DR InterPro; IPR039633; PAP.
DR InterPro; IPR006843; PAP/fibrillin_dom.
DR PANTHER; PTHR31906; PTHR31906; 1.
DR Pfam; PF04755; PAP_fibrillin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome;
KW Stress response; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..273
FT /note="Fibrillin-5, chloroplastic"
FT /id="PRO_0000290211"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 250..259
FT /note="LDEDLQVGRD -> PFLIKIQNRN (in isoform 2)"
FT /id="VSP_060147"
FT VAR_SEQ 260..273
FT /note="Missing (in isoform 2)"
FT /id="VSP_060148"
SQ SEQUENCE 273 AA; 30531 MW; EFC60B87EBC74570 CRC64;
MTSNLFQPPS MAASRGAISR RTGNVKVLVS FTSSNGKTLS FSDNSFRLRP MFIGKVTEQS
SCSSPNEQQQ DEEQEQEQEE ITVSHIKEEL YEALKGINRG IFGVKSDKKT EIEGLVKLLE
CRNPTPEPTG ELDKIGGCWK LIYSTITVLG SKRTKLGLRD FVSLGDLLQQ IDIAQGKTVH
VLKFDVRGLN LLDGEFRIVA SFKISSKSSV EITYESSTIK PDQLMNIFRK NMDLLLGIFN
PEGLFEISYL DEDLQVGRDG KGNVFVLERI EKP
