SSY4_ARATH
ID SSY4_ARATH Reviewed; 1040 AA.
AC Q0WVX5; O49727;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable starch synthase 4, chloroplastic/amyloplastic {ECO:0000305};
DE Short=AtSS4 {ECO:0000303|PubMed:17217470};
DE EC=2.4.1.21 {ECO:0000269|PubMed:19666739};
DE AltName: Full=Soluble starch synthase IV {ECO:0000303|PubMed:17217470};
DE Short=SSIV {ECO:0000303|PubMed:17217470};
DE Flags: Precursor;
GN Name=SS4 {ECO:0000303|PubMed:17217470};
GN OrderedLocusNames=At4g18240 {ECO:0000312|Araport:AT4G18240};
GN ORFNames=T9A21.90 {ECO:0000312|EMBL:CAB78826.1};
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17217470; DOI=10.1111/j.1365-313x.2006.02968.x;
RA Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V.,
RA Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.;
RT "The phenotype of soluble starch synthase IV defective mutants of
RT Arabidopsis thaliana suggests a novel function of elongation enzymes in the
RT control of starch granule formation.";
RL Plant J. 49:492-504(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19666739; DOI=10.1105/tpc.109.066522;
RA Szydlowski N., Ragel P., Raynaud S., Lucas M.M., Roldan I., Montero M.,
RA Munoz F.J., Ovecka M., Bahaji A., Planchot V., Pozueta-Romero J.,
RA D'Hulst C., Merida A.;
RT "Starch granule initiation in Arabidopsis requires the presence of either
RT class IV or class III starch synthases.";
RL Plant Cell 21:2443-2457(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21645200; DOI=10.1111/j.1467-7652.2011.00626.x;
RA Gamez-Arjona F.M., Li J., Raynaud S., Baroja-Fernandez E., Munoz F.J.,
RA Ovecka M., Ragel P., Bahaji A., Pozueta-Romero J., Merida A.;
RT "Enhancing the expression of starch synthase class IV results in increased
RT levels of both transitory and long-term storage starch.";
RL Plant Biotechnol. J. 9:1049-1060(2011).
RN [7]
RP INTERACTION WITH PTST2.
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: Probably involved in the priming of starch granule formation.
CC May play a regulatory role in the control of starch accumulation in
CC plastids. Is necessary and sufficient to establish the correct number
CC of starch granules observed in chloroplasts.
CC {ECO:0000269|PubMed:17217470, ECO:0000269|PubMed:19666739,
CC ECO:0000269|PubMed:21645200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC Evidence={ECO:0000269|PubMed:19666739};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with PTST2. {ECO:0000269|PubMed:28684429}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast
CC {ECO:0000269|PubMed:19666739, ECO:0000269|PubMed:21645200}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:17217470}.
CC -!- DISRUPTION PHENOTYPE: Severe reduced growth, reduced number of starch
CC granules, altered structure of starch granules.
CC {ECO:0000269|PubMed:17217470}.
CC -!- MISCELLANEOUS: Plants over-expressing SS4 have increased levels of
CC starch in leaves and display a higher growth rate than wild-type.
CC {ECO:0000305|PubMed:21645200}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021713; CAA16796.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161548; CAB78826.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84015.1; -; Genomic_DNA.
DR EMBL; AK226610; BAE98723.1; -; mRNA.
DR PIR; T04926; T04926.
DR RefSeq; NP_193558.3; NM_117934.4.
DR PDB; 6GNE; X-ray; 2.55 A; A/B=533-1040.
DR PDBsum; 6GNE; -.
DR AlphaFoldDB; Q0WVX5; -.
DR SMR; Q0WVX5; -.
DR BioGRID; 12843; 8.
DR STRING; 3702.AT4G18240.1; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR PaxDb; Q0WVX5; -.
DR PRIDE; Q0WVX5; -.
DR ProteomicsDB; 228261; -.
DR EnsemblPlants; AT4G18240.1; AT4G18240.1; AT4G18240.
DR GeneID; 827550; -.
DR Gramene; AT4G18240.1; AT4G18240.1; AT4G18240.
DR KEGG; ath:AT4G18240; -.
DR Araport; AT4G18240; -.
DR TAIR; locus:2141936; AT4G18240.
DR eggNOG; ENOG502QQTU; Eukaryota.
DR HOGENOM; CLU_007243_0_0_1; -.
DR InParanoid; Q0WVX5; -.
DR OMA; PLYWEIY; -.
DR OrthoDB; 166165at2759; -.
DR PhylomeDB; Q0WVX5; -.
DR BRENDA; 2.4.1.21; 399.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q0WVX5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WVX5; baseline and differential.
DR Genevisible; Q0WVX5; AT.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0009011; F:starch synthase activity; IMP:TAIR.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloplast; Chloroplast; Coiled coil; Glycosyltransferase;
KW Plastid; Reference proteome; Starch biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..1040
FT /note="Probable starch synthase 4,
FT chloroplastic/amyloplastic"
FT /id="PRO_0000419771"
FT REGION 43..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..466
FT /evidence="ECO:0000255"
FT COMPBIAS 68..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 556
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 593..607
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 610..621
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 624..632
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 649..666
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 672..677
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 678..682
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 684..691
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 717..721
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 727..730
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 733..736
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 747..754
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 756..761
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 763..770
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 772..775
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 779..784
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 798..800
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 803..805
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 819..832
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 843..849
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 856..868
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 872..878
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 882..894
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 895..897
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 899..904
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 909..918
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 920..924
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 934..940
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 944..950
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 951..956
FT /evidence="ECO:0007829|PDB:6GNE"
FT TURN 967..969
FT /evidence="ECO:0007829|PDB:6GNE"
FT STRAND 972..979
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 980..996
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 998..1009
FT /evidence="ECO:0007829|PDB:6GNE"
FT HELIX 1016..1031
FT /evidence="ECO:0007829|PDB:6GNE"
SQ SEQUENCE 1040 AA; 117747 MW; A89327E598D01165 CRC64;
MTTKLSSFCF LTHGLAGISC EREHGSSRRF FYLPSRRLVS TSCKMRQQRG FDSSKRQEVK
KGSPKPILSI NSGLQSNNDE ESDLENGSAD SVPSLKSDAE KGSSIHGSID MNHADENLEK
KDDIQTTEVT RRKSKTAKKK GESIHATIDI GHDDGKNLDN ITVPEVAKAL SLNKSEGEQI
SDGQFGELMT MIRSAEKNIL RLDEARATAL DDLNKILSDK EALQGEINVL EMKLSETDER
IKTAAQEKAH VELLEEQLEK LRHEMISPIE SDGYVLALSK ELETLKLENL SLRNDIEMLK
SELDSVKDTG ERVVVLEKEC SGLESSVKDL ESKLSVSQED VSQLSTLKIE CTDLWAKVET
LQLLLDRATK QAEQAVIVLQ QNQDLRNKVD KIEESLKEAN VYKESSEKIQ QYNELMQHKV
TLLEERLEKS DAEIFSYVQL YQESIKEFQE TLESLKEESK KKSRDEPVDD MPWDYWSRLL
LTVDGWLLEK KIASNDADLL RDMVWKKDRR IHDTYIDVKD KNERDAISAF LKLVSSPTSS
GLYVVHIAAE MAPVAKVGGL GDVVAGLGKA LQRKGHLVEI ILPKYDCMQY DRVRDLRALD
TVVESYFDGK LYKNKIWIGT VEGLPVHFIE PQHPSKFFWR GQFYGEQDDF RRFSYFSRAA
LELLLQSGKK PDIIHCHDWQ TAFVAPLYWD LYAPKGLDSA RICFTCHNFE YQGTASASEL
GSCGLDVNQL NRPDRMQDHS SGDRVNPVKG AIIFSNIVTT VSPTYAQEVR TAEGGKGLHS
TLNFHSKKFI GILNGIDTDS WNPATDPFLK AQFNAKDLQG KEENKHALRK QLGLSSAESR
RPLVGCITRL VPQKGVHLIR HAIYRTLELG GQFVLLGSSP VPHIQREFEG IEQQFKSHDH
VRLLLKYDEA LSHTIYAASD LFIIPSIFEP CGLTQMIAMR YGSIPIARKT GGLNDSVFDI
DDDTIPTQFQ NGFTFQTADE QGFNYALERA FNHYKKDEEK WMRLVEKVMS IDFSWGSSAT
QYEELYTRSV SRARAVPNRT
