PTST3_ARATH
ID PTST3_ARATH Reviewed; 598 AA.
AC F4KFB3; Q9LZE6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein PTST homolog 3, chloroplastic {ECO:0000305};
DE AltName: Full=PROTEIN TARGETING TO STARCH homolog 3 {ECO:0000303|PubMed:28684429};
DE Flags: Precursor;
GN Name=PTST {ECO:0000303|PubMed:28684429};
GN OrderedLocusNames=At5g03420 {ECO:0000312|Araport:AT5G03420};
GN ORFNames=F12E4_170 {ECO:0000312|EMBL:CAB83300.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 FUNCTION, INTERACTION WITH PTST2, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28684429; DOI=10.1105/tpc.17.00222;
RA Seung D., Boudet J., Monroe J., Schreier T.B., David L.C., Abt M., Lu K.J.,
RA Zanella M., Zeeman S.C.;
RT "Homologs of PROTEIN TARGETING TO STARCH control starch granule initiation
RT in Arabidopsis Leaves.";
RL Plant Cell 29:1657-1677(2017).
CC -!- FUNCTION: Involved in starch granule initiation in leaf chloroplasts.
CC {ECO:0000269|PubMed:28684429}.
CC -!- SUBUNIT: Interacts with PTST2. {ECO:0000269|PubMed:28684429}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:28684429}.
CC -!- DOMAIN: Contains a C-terminal (513-598) carbohydrate-binding domain
CC (CBM). {ECO:0000305|PubMed:28684429}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but leaf chloroplasts exhibit reduced number of starch
CC granules. {ECO:0000269|PubMed:28684429}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB83300.1; 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; AL162751; CAB83300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90601.1; -; Genomic_DNA.
DR PIR; T48365; T48365.
DR RefSeq; NP_195962.2; NM_120421.3.
DR AlphaFoldDB; F4KFB3; -.
DR SMR; F4KFB3; -.
DR PaxDb; F4KFB3; -.
DR PRIDE; F4KFB3; -.
DR ProteomicsDB; 224857; -.
DR EnsemblPlants; AT5G03420.1; AT5G03420.1; AT5G03420.
DR GeneID; 831846; -.
DR Gramene; AT5G03420.1; AT5G03420.1; AT5G03420.
DR KEGG; ath:AT5G03420; -.
DR Araport; AT5G03420; -.
DR TAIR; locus:2142669; AT5G03420.
DR eggNOG; ENOG502RRID; Eukaryota.
DR HOGENOM; CLU_040252_0_0_1; -.
DR OMA; SNNILRV; -.
DR OrthoDB; 885826at2759; -.
DR PRO; PR:F4KFB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KFB3; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0010581; P:regulation of starch biosynthetic process; IMP:TAIR.
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..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..598
FT /note="Protein PTST homolog 3, chloroplastic"
FT /id="PRO_0000442181"
FT REGION 129..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..516
FT /evidence="ECO:0000255"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 66571 MW; E3CDAD469934356E CRC64;
MATISQIPFS ISFPCFEFRK PSFYYHQPQL FVSYLNSTKK HSFICFACST KQTRVRKRVK
SNEELRSEIM QFVALAGLPE GHVPSMKELS AHGRVDLANI VRRRGYKFIK ELVANSGMEE
DCNELVADSE DNNTNIETGG SRACLEDSST DLSKEAEKQG SLSKDESSLA GVLSLENSFS
NLGDSNHSGE ITEKIFKIES VELNEIADIE NSSSEASVFA NHSQDLYDTS SCPDIEAGNV
SMTEDEEVND VDKDFSLTFD HYTSPTSNHY TSPDLNSIKH VDIATGSSYD LTSENTMTNV
ENFQNQQIDD IAANRSGSAD DSLVESEDND WMSGLSSCTS SIEEKTTRFI QNGYLDTVGA
DENDIPNESC PEESSETTKG GEYIGDSLGG PRIMSTPLNG SALALKEIIH ATEVNSSDRN
SDQRDGSVGL DTDPHHETRK RENQVEIDRL RFMLDQKELE LSRLKEQIEK EKLSLSVLQR
QAETEIQKAQ MLISEKEVEL QEAEESLSGL QEVVIEYCGD GNAVEVTGSF NGWQHRVGME
LQASKSIGKQ KCWSTLLWLY PGTYEIKFIV DGQWITDPQK DSVTRGHISN NILKVDSQ
