APS2L_ARATH
ID APS2L_ARATH Reviewed; 476 AA.
AC F4I8U2; Q7YKW3; Q9SYK2;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Inactive glucose-1-phosphate adenylyltransferase small subunit 2, chloroplastic {ECO:0000303|PubMed:12748181};
DE AltName: Full=ADP-Glc pyrophosphorylase small subunit-like {ECO:0000303|PubMed:15347792};
DE AltName: Full=ADP-glucose pyrophosphorylase small subunit 2 {ECO:0000303|PubMed:12748181};
DE Short=ApS2 {ECO:0000303|PubMed:12748181};
DE Flags: Precursor;
GN Name=APS2 {ECO:0000303|PubMed:12748181};
GN OrderedLocusNames=At1g05610 {ECO:0000312|Araport:AT1G05610};
GN ORFNames=F3F20.6 {ECO:0000312|EMBL:AAD30613.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CAUTION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=12748181; DOI=10.1074/jbc.m304280200;
RA Crevillen P., Ballicora M.A., Merida A., Preiss J., Romero J.M.;
RT "The different large subunit isoforms of Arabidopsis thaliana ADP-glucose
RT pyrophosphorylase confer distinct kinetic and regulatory properties to the
RT heterotetrameric enzyme.";
RL J. Biol. Chem. 278:28508-28515(2003).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15347792; DOI=10.1104/pp.104.044347;
RA Smith S.M., Fulton D.C., Chia T., Thorneycroft D., Chapple A., Dunstan H.,
RA Hylton C., Zeeman S.C., Smith A.M.;
RT "Diurnal changes in the transcriptome encoding enzymes of starch metabolism
RT provide evidence for both transcriptional and posttranscriptional
RT regulation of starch metabolism in Arabidopsis leaves.";
RL Plant Physiol. 136:2687-2699(2004).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15598655; DOI=10.1074/jbc.m411713200;
RA Crevillen P., Ventriglia T., Pinto F., Orea A., Merida A., Romero J.M.;
RT "Differential pattern of expression and sugar regulation of Arabidopsis
RT thaliana ADP-glucose pyrophosphorylase-encoding genes.";
RL J. Biol. Chem. 280:8143-8149(2005).
CC -!- SUBUNIT: Heterotetramer. {ECO:0000269|PubMed:12748181}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:P55229}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in leaves,
CC inflorescences, fruits, and roots. {ECO:0000269|PubMed:15347792,
CC ECO:0000269|PubMed:15598655}.
CC -!- DEVELOPMENTAL STAGE: In leaves, mainly observed in starch-producing
CC tissues including the mesophyll and the vascular companions cells. In
CC flowers, detected in the stamens and pistil, as well as in the
CC receptacle. Also expressed in the embryo.
CC {ECO:0000269|PubMed:15598655}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
CC -!- CAUTION: No detectable activity. {ECO:0000269|PubMed:12748181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ536666; CAD60664.1; -; mRNA.
DR EMBL; AC007153; AAD30613.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27864.1; -; Genomic_DNA.
DR PIR; B86190; B86190.
DR RefSeq; NP_172052.2; NM_100441.3.
DR AlphaFoldDB; F4I8U2; -.
DR SMR; F4I8U2; -.
DR STRING; 3702.AT1G05610.1; -.
DR PaxDb; F4I8U2; -.
DR PRIDE; F4I8U2; -.
DR EnsemblPlants; AT1G05610.1; AT1G05610.1; AT1G05610.
DR GeneID; 837066; -.
DR Gramene; AT1G05610.1; AT1G05610.1; AT1G05610.
DR KEGG; ath:AT1G05610; -.
DR Araport; AT1G05610; -.
DR TAIR; locus:2032003; AT1G05610.
DR eggNOG; KOG1322; Eukaryota.
DR HOGENOM; CLU_029499_14_1_1; -.
DR OMA; LSSSKWW; -.
DR PRO; PR:F4I8U2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I8U2; baseline and differential.
DR Genevisible; F4I8U2; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..476
FT /note="Inactive glucose-1-phosphate adenylyltransferase
FT small subunit 2, chloroplastic"
FT /id="PRO_0000431762"
FT CONFLICT 222
FT /note="N -> K (in Ref. 1; CAD60664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53335 MW; 42A2818F581CAF75 CRC64;
MQISSSSFIT KFTNLHMVRS TSDHHQWRHN YNLKQLFIPN LSVSNSQHLP LNQSVAAIVF
GGGSDSELYP LTKTRSKGAI PIAANYRLID AVISNCINSG ITKIYAITQF NSTSLNSHLS
KAYSGFGLGK DRFVEVIAAY QSLEDQGWFQ GTADAIRRCL WVFEEFPVTE FLVLPGHHLY
KMDYKMLIED HRRSRADITI VGLSSVTDHD FGFGFMEVDS TNAVTRFTIK GQQDLISVAN
RTATRSDGTS SCSVPSAGIY VIGREQMVKL LRECLIKSKD LASEIIPGAI SEGMKVKAHM
FDGYWEDVRS IGAYYRANME SIKSYRFYDR QCPLYTMPRC LPPSSMSVAV ITNSIIGDGC
ILDKCVIRGS VVGMRTRIAD EVIVEDSIIV GSDIYEMEED VRRKGKEKKI EIRIGIGEKS
RIRRAIVDKN ARIGKNVMII NRDNVEEGNR EAQGYVIREG IIIILRNAVI PNDSIL
