ID   SPSA4_ARATH             Reviewed;        1050 AA.
AC   F4JLK2; O82624; Q56Z77; Q570L0; Q680C9; Q9SN30;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   02-JUN-2021, entry version 70.
DE   RecName: Full=Probable sucrose-phosphate synthase 4;
DE            EC=2.4.1.14;
DE   AltName: Full=Sucrose phosphate synthase 4F;
DE            Short=AtSPS4F;
DE   AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase;
GN   Name=SPS4; Synonyms=SPSC; OrderedLocusNames=At4g10120; ORFNames=F28M11.40;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   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   [4]
RP   GENE FAMILY.
RX   PubMed=16876912; DOI=10.1016/j.jplph.2006.04.014;
RA   Lutfiyya L.L., Xu N., D'Ordine R.L., Morrell J.A., Miller P.W., Duff S.M.;
RT   "Phylogenetic and expression analysis of sucrose phosphate synthase
RT   isozymes in plants.";
RL   J. Plant Physiol. 164:923-933(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   INDUCTION BY COLD.
RX   PubMed=21309792; DOI=10.1111/j.1365-3040.2010.02265.x;
RA   Sun J., Zhang J., Larue C.T., Huber S.C.;
RT   "Decrease in leaf sucrose synthesis leads to increased leaf starch turnover
RT   and decreased RuBP regeneration-limited photosynthesis but not Rubisco-
RT   limited photosynthesis in Arabidopsis null mutants of SPSA1.";
RL   Plant Cell Environ. 34:592-604(2011).
CC   -!- FUNCTION: Plays a role in photosynthetic sucrose synthesis by
CC       catalyzing the rate-limiting step of sucrose biosynthesis from UDP-
CC       glucose and fructose- 6-phosphate. Involved in the regulation of carbon
CC       partitioning in the leaves of plants. May regulate the synthesis of
CC       sucrose and therefore play a major role as a limiting factor in the
CC       export of photoassimilates out of the leaf. Plays a role for sucrose
CC       availability that is essential for plant growth and fiber elongation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + UDP-alpha-D-glucose = H(+) +
CC         sucrose 6(F)-phosphate + UDP; Xref=Rhea:RHEA:22172,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.14;
CC   -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC       moderated by concentration of metabolites and light. {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC       fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: By cold (at protein level). {ECO:0000269|PubMed:21309792}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB39764.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78135.1; 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; AF096373; AAC62812.1; -; Genomic_DNA.
DR   EMBL; AL049487; CAB39764.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161516; CAB78135.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82844.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82845.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67156.1; -; Genomic_DNA.
DR   EMBL; AK175938; BAD43701.1; -; mRNA.
DR   EMBL; AK220698; BAD93789.1; -; mRNA.
DR   EMBL; AK220923; BAD94390.1; -; mRNA.
DR   EMBL; AK221092; BAD94960.1; -; mRNA.
DR   EMBL; AK230012; BAF01835.1; -; mRNA.
DR   PIR; T01981; T01981.
DR   PIR; T04062; T04062.
DR   RefSeq; NP_001031609.1; NM_001036532.3.
DR   RefSeq; NP_001329003.1; NM_001340652.1.
DR   RefSeq; NP_192750.2; NM_117080.5.
DR   STRING; 3702.AT4G10120.2; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; F4JLK2; -.
DR   PaxDb; F4JLK2; -.
DR   PRIDE; F4JLK2; -.
DR   ProteomicsDB; 228368; -.
DR   EnsemblPlants; AT4G10120.1; AT4G10120.1; AT4G10120.
DR   EnsemblPlants; AT4G10120.2; AT4G10120.2; AT4G10120.
DR   EnsemblPlants; AT4G10120.3; AT4G10120.3; AT4G10120.
DR   GeneID; 826603; -.
DR   Gramene; AT4G10120.1; AT4G10120.1; AT4G10120.
DR   Gramene; AT4G10120.2; AT4G10120.2; AT4G10120.
DR   Gramene; AT4G10120.3; AT4G10120.3; AT4G10120.
DR   KEGG; ath:AT4G10120; -.
DR   Araport; AT4G10120; -.
DR   TAIR; locus:2124680; AT4G10120.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_009583_24_0_1; -.
DR   InParanoid; F4JLK2; -.
DR   OrthoDB; 101620at2759; -.
DR   BRENDA; 2.4.1.14; 399.
DR   UniPathway; UPA00371; UER00545.
DR   PRO; PR:F4JLK2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JLK2; baseline and differential.
DR   Genevisible; F4JLK2; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0016157; F:sucrose synthase activity; IEA:InterPro.
DR   GO; GO:0046524; F:sucrose-phosphate synthase activity; IMP:TAIR.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16419; HAD_SPS; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006380; SPP_N.
DR   InterPro; IPR044161; SPS.
DR   InterPro; IPR035659; SPS_C.
DR   InterPro; IPR012819; SPS_pln.
DR   InterPro; IPR000368; Sucrose_synth.
DR   PANTHER; PTHR46039; PTHR46039; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   Pfam; PF00862; Sucrose_synth; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..1050
FT                   /note="Probable sucrose-phosphate synthase 4"
FT                   /id="PRO_0000413640"
FT   REGION          134..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   CONFLICT        276
FT                   /note="G -> D (in Ref. 3; BAD43701/BAD94390/BAD94960/
FT                   BAF01835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="L -> M (in Ref. 3; BAD94390/BAD94960/BAF01835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        603
FT                   /note="A -> V (in Ref. 3; BAD94390/BAD94960/BAF01835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        869
FT                   /note="E -> G (in Ref. 3; BAD94390/BAD94960/BAF01835)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1050 AA;  118878 MW;  4A835AA97C2D069B CRC64;
     MARNDWINSY LEAILDVGTS KKKRFESNSK IVQKLGDINS KDHQEKVFGD MNGKDHQEKV
     FSPIKYFVEE VVNSFDESDL YKTWIKVIAT RNTRERSNRL ENICWRIWHL ARKKKQIVWD
     DGVRLSKRRI EREQGRNDAE EDLLSELSEG EKDKNDGEKE KSEVVTTLEP PRDHMPRIRS
     EMQIWSEDDK SSRNLYIVLI SMHGLVRGEN MELGRDSDTG GQVKYVVELA RALANTEGVH
     RVDLLTRQIS SPEVDYSYGE PVEMLSCPPE GSDSCGSYII RIPCGSRDKY IPKESLWPHI
     PEFVDGALNH IVSIARSLGE QVNGGKPIWP YVIHGHYADA GEVAAHLAGA LNVPMVLTGH
     SLGRNKFEQL LQQGRITRED IDRTYKIMRR IEAEEQSLDA AEMVVTSTRQ EIDAQWGLYD
     GFDIKLERKL RVRRRRGVSC LGRYMPRMVV IPPGMDFSYV LTQDSQEPDG DLKSLIGPDR
     NQIKKPVPPI WSEIMRFFSN PHKPTILALS RPDHKKNVTT LVKAFGECQP LRELANLVLI
     LGNRDDIEEM PNSSSVVLMN VLKLIDQYDL YGQVAYPKHH KQSEVPDIYR LAAKTKGVFI
     NPALVEPFGL TLIEAAAYGL PIVATRNGGP VDIVKALNNG LLVDPHDQQA ISDALLKLVA
     NKHLWAECRK NGLKNIHRFS WPEHCRNYLS HVEHCRNRHP TSSLDIMKVP EELTSDSLRD
     VDDISLRFST EGDFTLNGEL DAGTRQKKLV DAISQMNSMK GCSAAIYSPG RRQMLFVVAV
     DSYDDNGNIK ANLNEIIKNM IKAADLTSGK GKIGFVLASG SSLQEVVDIT QKNLINLEDF
     DAIVCNSGSE IYYPWRDMMV DADYETHVEY KWPGESIRSV ILRLICTEPA AEDDITEYAS
     SCSTRCYAIS VKQGVKTRRV DDLRQRLRMR GLRCNIVYTH AATRLNVIPL CASRIQALRY
     LSIRWGIDMS KTVFFLGEKG DTDYEDLLGG LHKTIILKGV VGSDSEKLLR SEENFKREDA
     VPQESPNISY VKENGGSQEI MSTLEAYGIK
//