PTST_ARATH
ID PTST_ARATH Reviewed; 277 AA.
AC Q94AX2; F4KFV1;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein PTST, chloroplastic {ECO:0000303|PubMed:25710501};
DE AltName: Full=PROTEIN TARGETING TO STARCH {ECO:0000303|PubMed:25710501};
DE Flags: Precursor;
GN Name=PTST {ECO:0000303|PubMed:25710501}; Synonyms=PTST1 {ECO:0000305};
GN OrderedLocusNames=At5g39790 {ECO:0000312|Araport:AT5G39790};
GN ORFNames=MKM21.80 {ECO:0000312|EMBL:AB016876};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, DOMAIN, INDUCTION BY LIGHT, AND SUBCELLULAR LOCATION.
RX PubMed=19038037; DOI=10.1186/1471-2229-8-120;
RA Lohmeier-Vogel E.M., Kerk D., Nimick M., Wrobel S., Vickerman L.,
RA Muench D.G., Moorhead G.B.;
RT "Arabidopsis At5g39790 encodes a chloroplast-localized, carbohydrate-
RT binding, coiled-coil domain-containing putative scaffold protein.";
RL BMC Plant Biol. 8:120-120(2008).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP TRP-217 AND TRP-255, AND INTERACTION WITH GBSS1.
RC STRAIN=cv. Columbia;
RX PubMed=25710501; DOI=10.1371/journal.pbio.1002080;
RA Seung D., Soyk S., Coiro M., Maier B.A., Eicke S., Zeeman S.C.;
RT "PROTEIN TARGETING TO STARCH is required for localising GRANULE-BOUND
RT STARCH SYNTHASE to starch granules and for normal amylose synthesis in
RT Arabidopsis.";
RL PLoS Biol. 13:E1002080-E1002080(2015).
CC -!- FUNCTION: Involved in targeting GBSS1 to the starch granule
CC (PubMed:25710501). Was originally thought to be a carbohydrate-binding
CC scaffold protein, but it has been shown that it is mainly found as a
CC soluble protein and that interaction with GBSS1 is a pre-requisite for
CC subsequent starch granule binding (PubMed:19038037, PubMed:25710501).
CC Dissociation from starch as a function of pH, Mg(2+) concentration or
CC redox state is not observed (PubMed:19038037). Interacts primarily with
CC amylopectin and is required for amylose synthesis (PubMed:25710501).
CC {ECO:0000269|PubMed:19038037, ECO:0000269|PubMed:25710501}.
CC -!- SUBUNIT: Interacts with GBSS1. {ECO:0000269|PubMed:25710501}.
CC -!- INTERACTION:
CC Q94AX2; Q6NPM7: At3g60150; NbExp=2; IntAct=EBI-4430187, EBI-4426197;
CC Q94AX2; Q9MAQ0: GBSS1; NbExp=2; IntAct=EBI-4430187, EBI-2355339;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19038037, ECO:0000269|PubMed:25710501}. Note=The
CC vast majority of PTST is soluble and only a small amount is granule-
CC bound. No localization to the starch granules in the absence of GBSS1.
CC {ECO:0000269|PubMed:25710501}.
CC -!- INDUCTION: Circadian-regulation. Up-regulated during the day (at
CC protein level). {ECO:0000269|PubMed:19038037}.
CC -!- DOMAIN: Contains a C-terminal (199-277) carbohydrate-binding domain
CC (CBM). {ECO:0000269|PubMed:19038037}.
CC -!- DISRUPTION PHENOTYPE: 100-fold reduction of starch-bound GBSS1 protein
CC and production of amylose-free starch. {ECO:0000269|PubMed:25710501}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED94476.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED94476.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY045645; AAK74003.1; -; mRNA.
DR EMBL; AY059655; AAL31148.1; -; mRNA.
DR RefSeq; NP_568573.2; NM_123342.3.
DR AlphaFoldDB; Q94AX2; -.
DR SMR; Q94AX2; -.
DR DIP; DIP-61406N; -.
DR IntAct; Q94AX2; 4.
DR STRING; 3702.AT5G39790.1; -.
DR PaxDb; Q94AX2; -.
DR PRIDE; Q94AX2; -.
DR DNASU; 833975; -.
DR GeneID; 833975; -.
DR KEGG; ath:AT5G39790; -.
DR Araport; AT5G39790; -.
DR TAIR; locus:2167067; AT5G39790.
DR eggNOG; KOG1616; Eukaryota.
DR PhylomeDB; Q94AX2; -.
DR PRO; PR:Q94AX2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AX2; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009569; C:chloroplast starch grain; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:TAIR.
DR GO; GO:2001070; F:starch binding; IDA:UniProtKB.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IGI:TAIR.
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..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..277
FT /note="Protein PTST, chloroplastic"
FT /id="PRO_0000432836"
FT COILED 95..152
FT /evidence="ECO:0000255"
FT MUTAGEN 217
FT /note="W->A: Loss of binding to starch; when associated
FT with A-255."
FT /evidence="ECO:0000269|PubMed:25710501"
FT MUTAGEN 255
FT /note="W->A: Loss of binding to starch; when associated
FT with A-217."
FT /evidence="ECO:0000269|PubMed:25710501"
SQ SEQUENCE 277 AA; 31524 MW; E5D7C697F6B8464F CRC64;
MGCVPRIEFG CSSQSLTLSW NLRAWNLCRL NTISHFQKLP YPLVASTRKH YKNSLLLKRF
LVGVGTEESS LSEDLLDESL SRPLTSDELK SLLIDTERSK LVKKLSEANQ QNRFLKRQLK
TQEHEITNIK TELALMELEV QALVKLAEEI ANLGIPQGSR KISGKYIQSH LLSRLDAVQK
KMKEQIKGVE AAQSKEVHVF WIGMAESVQV MGSFDGWSQR EDLSPEYSAL FTKFSTTLFL
RPGRYEMKFL VDGEWQISPE FPTSGEGLME NNVLVVE
