SPSA4_ARATH
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 25-MAY-2022, entry version 73.
DE RecName: Full=Sucrose-phosphate synthase 4 {ECO:0000303|PubMed:16876912};
DE EC=2.4.1.14 {ECO:0000250|UniProtKB:P31927};
DE AltName: Full=Sucrose phosphate synthase 4F {ECO:0000303|PubMed:16876912};
DE Short=AtSPS4F {ECO:0000303|PubMed:16876912};
DE AltName: Full=Sucrose phosphate synthase C {ECO:0000303|PubMed:21309792};
DE AltName: Full=UDP-glucose-fructose-phosphate glucosyltransferase {ECO:0000303|PubMed:21309792};
GN Name=SPS4 {ECO:0000303|PubMed:16876912};
GN Synonyms=SPSC {ECO:0000303|PubMed:21309792};
GN OrderedLocusNames=At4g10120 {ECO:0000312|Araport:AT4G10120};
GN ORFNames=F28M11.40 {ECO:0000312|EMBL:CAB39764.1};
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=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.
RC STRAIN=cv. Columbia;
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 (By similarity). Involved in the
CC regulation of carbon partitioning in the leaves of plants (By
CC similarity). May regulate the synthesis of sucrose and therefore play a
CC major role as a limiting factor in the export of photoassimilates out
CC of the leaf (By similarity). Plays a role for sucrose availability that
CC is essential for plant growth and fiber elongation (By similarity).
CC {ECO:0000250|UniProtKB:Q94BT0}.
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 Evidence={ECO:0000250|UniProtKB:P31927};
CC -!- ACTIVITY REGULATION: Activity is regulated by phosphorylation and
CC moderated by concentration of metabolites and light.
CC {ECO:0000250|UniProtKB:P31928}.
CC -!- PATHWAY: Glycan biosynthesis; sucrose biosynthesis; sucrose from D-
CC fructose 6-phosphate and UDP-alpha-D-glucose: step 1/2.
CC {ECO:0000250|UniProtKB:P31927}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250|UniProtKB:P31927}.
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};
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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; 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 AlphaFoldDB; F4JLK2; -.
DR SMR; F4JLK2; -.
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:0016157; F:sucrose synthase activity; IEA:InterPro.
DR GO; GO:0046524; F:sucrose-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0005986; P:sucrose biosynthetic process; IGI:TAIR.
DR CDD; cd16419; HAD_SPS; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR036412; HAD-like_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="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
