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   19-MAR-2014, entry version 28.
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;
GN   ORFNames=F28M11.40;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Hayashizaki Y., 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.,
RA   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
RP   BY 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.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148, AND IDENTIFICATION
RP   BY 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
RT   turnover and decreased RuBP regeneration-limited photosynthesis but
RT   not Rubisco-limited photosynthesis in Arabidopsis null mutants of
RT   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
CC       UDP-glucose and fructose- 6-phosphate. Involved in the regulation
CC       of carbon partitioning in the leaves of plants. May regulate the
CC       synthesis of sucrose and therefore play a major role as a limiting
CC       factor in the export of photoassimilates out of the leaf. Plays a
CC       role for sucrose availability that is essential for plant growth
CC       and fiber elongation.
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + D-fructose 6-phosphate = UDP +
CC       sucrose 6(F)-phosphate.
CC   -!- ENZYME REGULATION: Activity is regulated by phosphorylation and
CC       moderated by concentration of metabolites and light (By
CC       similarity).
CC   -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from
CC       D-fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC   -!- SUBUNIT: Homodimer or homotetramer (By similarity).
CC   -!- INDUCTION: By cold (at protein level).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB39764.1; Type=Erroneous gene model prediction;
CC       Sequence=CAB78135.1; Type=Erroneous gene model prediction;
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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; 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_001036532.2.
DR   RefSeq; NP_192750.2; NM_117080.4.
DR   UniGene; At.27493; -.
DR   ProteinModelPortal; F4JLK2; -.
DR   SMR; F4JLK2; 218-698.
DR   STRING; 3702.AT4G10120.1-P; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   PRIDE; F4JLK2; -.
DR   EnsemblPlants; AT4G10120.1; AT4G10120.1; AT4G10120.
DR   EnsemblPlants; AT4G10120.2; AT4G10120.2; AT4G10120.
DR   GeneID; 826603; -.
DR   KEGG; ath:AT4G10120; -.
DR   TAIR; AT4G10120; -.
DR   eggNOG; COG0438; -.
DR   HOGENOM; HOG000009685; -.
DR   InParanoid; Q680C9; -.
DR   KO; K00696; -.
DR   OMA; LGRYMPR; -.
DR   UniPathway; UPA00371; UER00545.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0046524; F:sucrose-phosphate synthase activity; IMP:TAIR.
DR   GO; GO:0005986; P:sucrose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006380; Sucrose-P_synthase.
DR   InterPro; IPR012819; SucrsPsyn_pln.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR02468; sucrsPsyn_pln; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycosyltransferase; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN         1   1050       Probable sucrose-phosphate synthase 4.
FT                                /FTId=PRO_0000413640.
FT   MOD_RES     148    148       Phosphoserine.
FT   MOD_RES     180    180       Phosphoserine.
FT   CONFLICT    276    276       G -> D (in Ref. 3; BAD43701/BAD94390/
FT                                BAD94960/BAF01835).
FT   CONFLICT    461    461       L -> M (in Ref. 3; BAD94390/BAD94960/
FT                                BAF01835).
FT   CONFLICT    603    603       A -> V (in Ref. 3; BAD94390/BAD94960/
FT                                BAF01835).
FT   CONFLICT    869    869       E -> G (in Ref. 3; BAD94390/BAD94960/
FT                                BAF01835).
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
//