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Protein

Probable starch synthase 4, chloroplastic/amyloplastic

Gene

SS4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Probably involved in the priming of starch granule formation. May play a regulatory role in the control of starch accumulation in plastids. Is necessary and sufficient to establish the correct number of starch granules observed in chloroplasts.3 Publications

Catalytic activityi

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1).

Pathway: starch biosynthesis

This protein is involved in the pathway starch biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway starch biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei556 – 5561ADP-glucoseBy similarity

GO - Molecular functioni

GO - Biological processi

  • starch biosynthetic process Source: UniProtKB-UniPathway
  • starch metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Starch biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00152.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable starch synthase 4, chloroplastic/amyloplastic (EC:2.4.1.21)
Short name:
AtSS4
Alternative name(s):
Soluble starch synthase IV
Gene namesi
Name:SS4
Ordered Locus Names:At4g18240
ORF Names:T9A21.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G18240.

Subcellular locationi

GO - Cellular componenti

  • amyloplast Source: UniProtKB-SubCell
  • chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Severe reduced growth, reduced number of starch granules, altered structure of starch granules.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242ChloroplastSequence AnalysisAdd
BLAST
Chaini43 – 1040998Probable starch synthase 4, chloroplastic/amyloplasticPRO_0000419771Add
BLAST

Proteomic databases

PRIDEiQ0WVX5.

Expressioni

Tissue specificityi

Expressed in leaves and flowers.1 Publication

Gene expression databases

ExpressionAtlasiQ0WVX5. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G18240.1.

Structurei

3D structure databases

ProteinModelPortaliQ0WVX5.
SMRiQ0WVX5. Positions 544-1026.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili187 – 466280Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

HOGENOMiHOG000082799.
InParanoidiQ0WVX5.
OMAiYGSIPIA.
PhylomeDBiQ0WVX5.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0WVX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTKLSSFCF LTHGLAGISC EREHGSSRRF FYLPSRRLVS TSCKMRQQRG
60 70 80 90 100
FDSSKRQEVK KGSPKPILSI NSGLQSNNDE ESDLENGSAD SVPSLKSDAE
110 120 130 140 150
KGSSIHGSID MNHADENLEK KDDIQTTEVT RRKSKTAKKK GESIHATIDI
160 170 180 190 200
GHDDGKNLDN ITVPEVAKAL SLNKSEGEQI SDGQFGELMT MIRSAEKNIL
210 220 230 240 250
RLDEARATAL DDLNKILSDK EALQGEINVL EMKLSETDER IKTAAQEKAH
260 270 280 290 300
VELLEEQLEK LRHEMISPIE SDGYVLALSK ELETLKLENL SLRNDIEMLK
310 320 330 340 350
SELDSVKDTG ERVVVLEKEC SGLESSVKDL ESKLSVSQED VSQLSTLKIE
360 370 380 390 400
CTDLWAKVET LQLLLDRATK QAEQAVIVLQ QNQDLRNKVD KIEESLKEAN
410 420 430 440 450
VYKESSEKIQ QYNELMQHKV TLLEERLEKS DAEIFSYVQL YQESIKEFQE
460 470 480 490 500
TLESLKEESK KKSRDEPVDD MPWDYWSRLL LTVDGWLLEK KIASNDADLL
510 520 530 540 550
RDMVWKKDRR IHDTYIDVKD KNERDAISAF LKLVSSPTSS GLYVVHIAAE
560 570 580 590 600
MAPVAKVGGL GDVVAGLGKA LQRKGHLVEI ILPKYDCMQY DRVRDLRALD
610 620 630 640 650
TVVESYFDGK LYKNKIWIGT VEGLPVHFIE PQHPSKFFWR GQFYGEQDDF
660 670 680 690 700
RRFSYFSRAA LELLLQSGKK PDIIHCHDWQ TAFVAPLYWD LYAPKGLDSA
710 720 730 740 750
RICFTCHNFE YQGTASASEL GSCGLDVNQL NRPDRMQDHS SGDRVNPVKG
760 770 780 790 800
AIIFSNIVTT VSPTYAQEVR TAEGGKGLHS TLNFHSKKFI GILNGIDTDS
810 820 830 840 850
WNPATDPFLK AQFNAKDLQG KEENKHALRK QLGLSSAESR RPLVGCITRL
860 870 880 890 900
VPQKGVHLIR HAIYRTLELG GQFVLLGSSP VPHIQREFEG IEQQFKSHDH
910 920 930 940 950
VRLLLKYDEA LSHTIYAASD LFIIPSIFEP CGLTQMIAMR YGSIPIARKT
960 970 980 990 1000
GGLNDSVFDI DDDTIPTQFQ NGFTFQTADE QGFNYALERA FNHYKKDEEK
1010 1020 1030 1040
WMRLVEKVMS IDFSWGSSAT QYEELYTRSV SRARAVPNRT
Length:1,040
Mass (Da):117,747
Last modified:September 5, 2006 - v1
Checksum:iA89327E598D01165
GO

Sequence cautioni

The sequence CAA16796.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78826.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021713 Genomic DNA. Translation: CAA16796.1. Sequence problems.
AL161548 Genomic DNA. Translation: CAB78826.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84015.1.
AK226610 mRNA. Translation: BAE98723.1.
PIRiT04926.
RefSeqiNP_193558.3. NM_117934.4.
UniGeneiAt.46236.

Genome annotation databases

EnsemblPlantsiAT4G18240.1; AT4G18240.1; AT4G18240.
GeneIDi827550.
KEGGiath:AT4G18240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021713 Genomic DNA. Translation: CAA16796.1. Sequence problems.
AL161548 Genomic DNA. Translation: CAB78826.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84015.1.
AK226610 mRNA. Translation: BAE98723.1.
PIRiT04926.
RefSeqiNP_193558.3. NM_117934.4.
UniGeneiAt.46236.

3D structure databases

ProteinModelPortaliQ0WVX5.
SMRiQ0WVX5. Positions 544-1026.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G18240.1.

Proteomic databases

PRIDEiQ0WVX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G18240.1; AT4G18240.1; AT4G18240.
GeneIDi827550.
KEGGiath:AT4G18240.

Organism-specific databases

TAIRiAT4G18240.

Phylogenomic databases

HOGENOMiHOG000082799.
InParanoidiQ0WVX5.
OMAiYGSIPIA.
PhylomeDBiQ0WVX5.

Enzyme and pathway databases

UniPathwayiUPA00152.

Miscellaneous databases

PROiQ0WVX5.

Gene expression databases

ExpressionAtlasiQ0WVX5. baseline and differential.

Family and domain databases

HAMAPiMF_00484. Glycogen_synth.
InterProiIPR001296. Glyco_trans_1.
IPR011835. GS/SS.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamiPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02095. glgA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation."
    Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V., Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.
    Plant J. 49:492-504(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  5. "Starch granule initiation in Arabidopsis requires the presence of either class IV or class III starch synthases."
    Szydlowski N., Ragel P., Raynaud S., Lucas M.M., Roldan I., Montero M., Munoz F.J., Ovecka M., Bahaji A., Planchot V., Pozueta-Romero J., D'Hulst C., Merida A.
    Plant Cell 21:2443-2457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Enhancing the expression of starch synthase class IV results in increased levels of both transitory and long-term storage starch."
    Gamez-Arjona F.M., Li J., Raynaud S., Baroja-Fernandez E., Munoz F.J., Ovecka M., Ragel P., Bahaji A., Pozueta-Romero J., Merida A.
    Plant Biotechnol. J. 9:1049-1060(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSSY4_ARATH
AccessioniPrimary (citable) accession number: Q0WVX5
Secondary accession number(s): O49727
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: September 5, 2006
Last modified: June 24, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants over-expressing SS4 have increased levels of starch in leaves and display a higher growth rate than wild-type.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.