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Q0WVX5

- SSY4_ARATH

UniProt

Q0WVX5 - SSY4_ARATH

Protein

Probable starch synthase 4, chloroplastic/amyloplastic

Gene

SS4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    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).

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. starch synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. starch biosynthetic process Source: UniProtKB-UniPathway
    2. starch metabolic process Source: TAIR

    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: Chromosome 4

    Organism-specific databases

    TAIRiAT4G18240.

    Subcellular locationi

    GO - Cellular componenti

    1. amyloplast Source: UniProtKB-SubCell
    2. chloroplast Source: TAIR

    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

    GenevestigatoriQ0WVX5.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G18240.1-P.

    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

    InParanoidiQ0WVX5.
    OMAiHSKKFIG.
    PhylomeDBiQ0WVX5.

    Family and domain databases

    HAMAPiMF_00484. Glycogen_synth.
    InterProiIPR001296. Glyco_trans_1.
    IPR011835. Glycogen/starch_synth.
    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

    MTTKLSSFCF LTHGLAGISC EREHGSSRRF FYLPSRRLVS TSCKMRQQRG     50
    FDSSKRQEVK KGSPKPILSI NSGLQSNNDE ESDLENGSAD SVPSLKSDAE 100
    KGSSIHGSID MNHADENLEK KDDIQTTEVT RRKSKTAKKK GESIHATIDI 150
    GHDDGKNLDN ITVPEVAKAL SLNKSEGEQI SDGQFGELMT MIRSAEKNIL 200
    RLDEARATAL DDLNKILSDK EALQGEINVL EMKLSETDER IKTAAQEKAH 250
    VELLEEQLEK LRHEMISPIE SDGYVLALSK ELETLKLENL SLRNDIEMLK 300
    SELDSVKDTG ERVVVLEKEC SGLESSVKDL ESKLSVSQED VSQLSTLKIE 350
    CTDLWAKVET LQLLLDRATK QAEQAVIVLQ QNQDLRNKVD KIEESLKEAN 400
    VYKESSEKIQ QYNELMQHKV TLLEERLEKS DAEIFSYVQL YQESIKEFQE 450
    TLESLKEESK KKSRDEPVDD MPWDYWSRLL LTVDGWLLEK KIASNDADLL 500
    RDMVWKKDRR IHDTYIDVKD KNERDAISAF LKLVSSPTSS GLYVVHIAAE 550
    MAPVAKVGGL GDVVAGLGKA LQRKGHLVEI ILPKYDCMQY DRVRDLRALD 600
    TVVESYFDGK LYKNKIWIGT VEGLPVHFIE PQHPSKFFWR GQFYGEQDDF 650
    RRFSYFSRAA LELLLQSGKK PDIIHCHDWQ TAFVAPLYWD LYAPKGLDSA 700
    RICFTCHNFE YQGTASASEL GSCGLDVNQL NRPDRMQDHS SGDRVNPVKG 750
    AIIFSNIVTT VSPTYAQEVR TAEGGKGLHS TLNFHSKKFI GILNGIDTDS 800
    WNPATDPFLK AQFNAKDLQG KEENKHALRK QLGLSSAESR RPLVGCITRL 850
    VPQKGVHLIR HAIYRTLELG GQFVLLGSSP VPHIQREFEG IEQQFKSHDH 900
    VRLLLKYDEA LSHTIYAASD LFIIPSIFEP CGLTQMIAMR YGSIPIARKT 950
    GGLNDSVFDI DDDTIPTQFQ NGFTFQTADE QGFNYALERA FNHYKKDEEK 1000
    WMRLVEKVMS IDFSWGSSAT QYEELYTRSV SRARAVPNRT 1040
    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.
    The sequence CAB78826.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T04926.
    RefSeqi NP_193558.3. NM_117934.4.
    UniGenei At.46236.

    3D structure databases

    ProteinModelPortali Q0WVX5.
    SMRi Q0WVX5. Positions 544-1026.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G18240.1-P.

    Proteomic databases

    PRIDEi Q0WVX5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G18240.1 ; AT4G18240.1 ; AT4G18240 .
    GeneIDi 827550.
    KEGGi ath:AT4G18240.

    Organism-specific databases

    TAIRi AT4G18240.

    Phylogenomic databases

    InParanoidi Q0WVX5.
    OMAi HSKKFIG.
    PhylomeDBi Q0WVX5.

    Enzyme and pathway databases

    UniPathwayi UPA00152 .

    Gene expression databases

    Genevestigatori Q0WVX5.

    Family and domain databases

    HAMAPi MF_00484. Glycogen_synth.
    InterProi IPR001296. Glyco_trans_1.
    IPR011835. Glycogen/starch_synth.
    IPR013534. Starch_synth_cat_dom.
    [Graphical view ]
    Pfami PF08323. Glyco_transf_5. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02095. glgA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 63 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