PTST2_ARATH
ID PTST2_ARATH Reviewed; 532 AA.
AC Q9LFY0; Q8LPF2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein PTST homolog 2, chloroplastic {ECO:0000305};
DE AltName: Full=PROTEIN TARGETING TO STARCH homolog 2 {ECO:0000303|PubMed:28684429};
DE Flags: Precursor;
GN Name=PTST2 {ECO:0000303|PubMed:28684429};
GN OrderedLocusNames=At1g27070 {ECO:0000312|Araport:AT1G27070};
GN ORFNames=T7N9.13 {ECO:0000312|EMBL:AAF79876.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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, INTERACTION WITH PTST3 AND SS4, SUBCELLULAR LOCATION, AND
RP DISRUPTION 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 Binds and delivers suitable maltooligosaccharide substrates to starch
CC synthase 4 (SS4). {ECO:0000269|PubMed:28684429}.
CC -!- SUBUNIT: Interacts with PTST3 and SS4. {ECO:0000269|PubMed:28684429}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:28684429}.
CC -!- DOMAIN: Contains a C-terminal (456-532) 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=AAM26688.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC000348; AAF79876.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30776.1; -; Genomic_DNA.
DR EMBL; AY102120; AAM26688.1; ALT_FRAME; mRNA.
DR EMBL; BT000569; AAN18138.1; -; mRNA.
DR RefSeq; NP_174027.3; NM_102469.5.
DR AlphaFoldDB; Q9LFY0; -.
DR SMR; Q9LFY0; -.
DR STRING; 3702.AT1G27070.1; -.
DR iPTMnet; Q9LFY0; -.
DR PaxDb; Q9LFY0; -.
DR PRIDE; Q9LFY0; -.
DR ProteomicsDB; 226454; -.
DR EnsemblPlants; AT1G27070.1; AT1G27070.1; AT1G27070.
DR GeneID; 839596; -.
DR Gramene; AT1G27070.1; AT1G27070.1; AT1G27070.
DR KEGG; ath:AT1G27070; -.
DR Araport; AT1G27070; -.
DR TAIR; locus:2205819; AT1G27070.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_020708_1_1_1; -.
DR OMA; LEGKMAM; -.
DR OrthoDB; 440758at2759; -.
DR PhylomeDB; Q9LFY0; -.
DR PRO; PR:Q9LFY0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LFY0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:2001071; F:maltoheptaose binding; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:TAIR.
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..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..532
FT /note="Protein PTST homolog 2, chloroplastic"
FT /id="PRO_0000442180"
FT REGION 165..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..454
FT /evidence="ECO:0000255"
FT COMPBIAS 265..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 59199 MW; C0786243CE210B14 CRC64;
MVSINSGPIS SFVSRYSMID SDTLLHLSSF GSTFNPNYKA KACIRFARKV CGSTVLGFLE
VKPRKKSCCS RCNGVSRMCN KRNLGWDSEG SKDLETEILE FMKNSEKPGM FPSKKDLIRS
GRFDLVERIV NQGGWLSMGW DLDEQEEKVR VNENVTPQDL HIEKQLPNCN SPEMDKTLNH
GDLDLSSNLS SSTEQVESRN DSGIEGILTR LEKERNLSLG ISVRENGKSN GAMHDISPNG
SVPWSSRIVT ASEIQEVDGS RGSGEYAQSR YQGAKSVSGK PGLSDSPTSE TWRTWSMRRA
GFTDEDFEAA EISSSGLTGV KKDDTKKDSG DSMNGKDRIA SSSEDVNKTH IKHRLQQLQS
ELSSVLHSLR SPPDKVVTSK DSETTAGNLE NLSDDWEYKE NEIIHAQNKL RSTRAKLAVL
EGKMAMAIID AQRIVREKQR RIDHASRALR LLRTASIVWP NSASEVLLTG SFDGWSTQRK
MKKAENGVFS LSLKLYPGKY EIKFIVDGQW KVDPLRPIVT SGGYENNLLI IS
