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Q0WVX5 (SSY4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable starch synthase 4, chloroplastic/amyloplastic

Short name=AtSS4
EC=2.4.1.21
Alternative name(s):
Soluble starch synthase IV
Gene names
Name:SS4
Ordered Locus Names:At4g18240
ORF Names:T9A21.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1040 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.4 Ref.5 Ref.6

Catalytic activity

ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1). HAMAP-Rule MF_00484

Pathway

Glycan biosynthesis; starch biosynthesis. HAMAP-Rule MF_00484

Subcellular location

Plastidchloroplast. Plastidamyloplast Ref.5 Ref.6.

Tissue specificity

Expressed in leaves and flowers. Ref.4

Disruption phenotype

Severe reduced growth, reduced number of starch granules, altered structure of starch granules. Ref.4

Miscellaneous

Plants over-expressing SS4 have increased levels of starch in leaves and display a higher growth rate than wild-type (Ref.6).

Sequence similarities

Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.

Sequence caution

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

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

Ontologies

Keywords
   Biological processStarch biosynthesis
   Cellular componentAmyloplast
Chloroplast
Plastid
   DomainCoiled coil
Transit peptide
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processstarch biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

starch metabolic process

Inferred from mutant phenotype Ref.4. Source: TAIR

   Cellular_componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

   Molecular_functionstarch synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Chloroplast Potential
Chain43 – 1040998Probable starch synthase 4, chloroplastic/amyloplastic HAMAP-Rule MF_00484
PRO_0000419771

Regions

Coiled coil187 – 466280 Potential

Sites

Binding site5561ADP-glucose By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0WVX5 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A89327E598D01165

FASTA1,040117,747
        10         20         30         40         50         60 
MTTKLSSFCF LTHGLAGISC EREHGSSRRF FYLPSRRLVS TSCKMRQQRG FDSSKRQEVK 

        70         80         90        100        110        120 
KGSPKPILSI NSGLQSNNDE ESDLENGSAD SVPSLKSDAE KGSSIHGSID MNHADENLEK 

       130        140        150        160        170        180 
KDDIQTTEVT RRKSKTAKKK GESIHATIDI GHDDGKNLDN ITVPEVAKAL SLNKSEGEQI 

       190        200        210        220        230        240 
SDGQFGELMT MIRSAEKNIL RLDEARATAL DDLNKILSDK EALQGEINVL EMKLSETDER 

       250        260        270        280        290        300 
IKTAAQEKAH VELLEEQLEK LRHEMISPIE SDGYVLALSK ELETLKLENL SLRNDIEMLK 

       310        320        330        340        350        360 
SELDSVKDTG ERVVVLEKEC SGLESSVKDL ESKLSVSQED VSQLSTLKIE CTDLWAKVET 

       370        380        390        400        410        420 
LQLLLDRATK QAEQAVIVLQ QNQDLRNKVD KIEESLKEAN VYKESSEKIQ QYNELMQHKV 

       430        440        450        460        470        480 
TLLEERLEKS DAEIFSYVQL YQESIKEFQE TLESLKEESK KKSRDEPVDD MPWDYWSRLL 

       490        500        510        520        530        540 
LTVDGWLLEK KIASNDADLL RDMVWKKDRR IHDTYIDVKD KNERDAISAF LKLVSSPTSS 

       550        560        570        580        590        600 
GLYVVHIAAE MAPVAKVGGL GDVVAGLGKA LQRKGHLVEI ILPKYDCMQY DRVRDLRALD 

       610        620        630        640        650        660 
TVVESYFDGK LYKNKIWIGT VEGLPVHFIE PQHPSKFFWR GQFYGEQDDF RRFSYFSRAA 

       670        680        690        700        710        720 
LELLLQSGKK PDIIHCHDWQ TAFVAPLYWD LYAPKGLDSA RICFTCHNFE YQGTASASEL 

       730        740        750        760        770        780 
GSCGLDVNQL NRPDRMQDHS SGDRVNPVKG AIIFSNIVTT VSPTYAQEVR TAEGGKGLHS 

       790        800        810        820        830        840 
TLNFHSKKFI GILNGIDTDS WNPATDPFLK AQFNAKDLQG KEENKHALRK QLGLSSAESR 

       850        860        870        880        890        900 
RPLVGCITRL VPQKGVHLIR HAIYRTLELG GQFVLLGSSP VPHIQREFEG IEQQFKSHDH 

       910        920        930        940        950        960 
VRLLLKYDEA LSHTIYAASD LFIIPSIFEP CGLTQMIAMR YGSIPIARKT GGLNDSVFDI 

       970        980        990       1000       1010       1020 
DDDTIPTQFQ NGFTFQTADE QGFNYALERA FNHYKKDEEK WMRLVEKVMS IDFSWGSSAT 

      1030       1040 
QYEELYTRSV SRARAVPNRT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04926.
RefSeqNP_193558.3. NM_117934.4.
UniGeneAt.46236.

3D structure databases

ProteinModelPortalQ0WVX5.
SMRQ0WVX5. Positions 544-1026.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G18240.1-P.

Proteomic databases

PRIDEQ0WVX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G18240.1; AT4G18240.1; AT4G18240.
GeneID827550.
KEGGath:AT4G18240.

Organism-specific databases

TAIRAT4G18240.

Phylogenomic databases

InParanoidQ0WVX5.
OMALVGCITR.
PhylomeDBQ0WVX5.
ProtClustDBPLN02939.

Enzyme and pathway databases

UniPathwayUPA00152.

Gene expression databases

GenevestigatorQ0WVX5.

Family and domain databases

HAMAPMF_00484. Glycogen_synth.
InterProIPR001296. Glyco_trans_1.
IPR011835. Glycogen/starch_synth.
IPR013534. Starch_synth_cat_dom.
[Graphical view]
PfamPF08323. Glyco_transf_5. 1 hit.
PF00534. Glycos_transf_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR02095. glgA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSSY4_ARATH
AccessionPrimary (citable) accession number: Q0WVX5
Secondary accession number(s): O49727
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: September 5, 2006
Last modified: March 19, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names