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Q9MAC8 (SSY2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

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

Names and origin

Protein namesRecommended name:
Starch synthase 2, chloroplastic/amyloplastic
Short name=AtSS2
EC=2.4.1.21
Alternative name(s):
Soluble starch synthase II
Gene names
Name:SS2
Ordered Locus Names:At3g01180
ORF Names:T4P13.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length792 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the synthesis of glycan chains within amylopectin in leaves. Is required to produce chains with a degree of polymerization of 12 to 25 (DP12-DP25). Ref.5

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

Plastid › chloroplast. Plastid › amyloplast Probable HAMAP-Rule MF_00484.

Tissue specificity

Expressed in roots, leaves and flowers. Ref.4

Disruption phenotype

Reduced plant growth under short day photopheriod conditions and starch granules with alterated morphology. Ref.5

Sequence similarities

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

Ontologies

Keywords
   Biological processStarch biosynthesis
   Cellular componentAmyloplast
Chloroplast
Plastid
   DomainTransit peptide
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processamylopectin biosynthetic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

starch biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

   Molecular_functionstarch synthase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5555Chloroplast Potential
Chain56 – 792737Starch synthase 2, chloroplastic/amyloplastic HAMAP-Rule MF_00484
PRO_0000419769

Regions

Compositional bias146 – 24297Ser-rich HAMAP-Rule MF_00484

Sites

Binding site3151ADP-glucose By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9MAC8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F8C852E4119EF670

FASTA79287,593
        10         20         30         40         50         60 
MASVAESSFP LLCQIKTQRR INSSTLRHSR VSYHDLPSGS LSFRSRSFVL GHRCKCVSRV 

        70         80         90        100        110        120 
EASGSDDDEP EDALQATIDK SKKVLAMQRN LLHQIAERRK LVSSIKESTP DLDDAKASSK 

       130        140        150        160        170        180 
QESASSVNAN TDATKKEIMD GDANGSVSPS TYGKSSLSKE PEAKTFSPST ESLKNRKQSS 

       190        200        210        220        230        240 
ASVISSSPVT SPQKPSDVAT NGKPWSSVVA SSVDPPYKPS SVMTSPEKTS DPVTSPGKPS 

       250        260        270        280        290        300 
KSRAGAFWSD PLPSYLTKAP QTSTMKTEKY VEKTPDVASS ETNEPGKDEE KPPPLAGANV 

       310        320        330        340        350        360 
MNVILVAAEC APFSKTGGLG DVAGALPKSL ARRGHRVMVV VPRYAEYAEA KDLGVRKRYK 

       370        380        390        400        410        420 
VAGQDMEVMY FHAFIDGVDF VFIDSPEFRH LSNNIYGGNR LDILKRMVLF CKAAVEVPWY 

       430        440        450        460        470        480 
VPCGGVCYGD GNLAFIANDW HTALLPVYLK AYYRDHGIMK YTRSVLVIHN IAHQGRGPVD 

       490        500        510        520        530        540 
DFSYVDLPSH YLDSFKLYDP VGGEHFNIFA AGLKAADRVL TVSHGYSWEV KTLEGGWGLH 

       550        560        570        580        590        600 
NIINENDWKF RGIVNGIDTQ EWNPEFDTYL HSDDYTNYSL ENLHIGKPQC KAALQKELGL 

       610        620        630        640        650        660 
PVRPDVPLIG FIGRLDHQKG VDLIAEAVPW MMSQDVQLVM LGTGRPDLEE VLRQMEHQYR 

       670        680        690        700        710        720 
DKARGWVGFS VKTAHRITAG ADILLMPSRF EPCGLNQLYA MNYGTIPVVH AVGGLRDTVQ 

       730        740        750        760        770        780 
QFDPYSETGL GWTFDSAEAG KLIHALGNCL LTYREYKESW EGLQRRGMTQ DLSWDNAAEK 

       790 
YEEVLVAAKY HW

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
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: TISSUE SPECIFICITY.
[5]"Overlapping functions of the starch synthases SSII and SSIII in amylopectin biosynthesis in Arabidopsis."
Zhang X., Szydlowski N., Delvalle D., D'Hulst C., James M.G., Myers A.M.
BMC Plant Biol. 8:96-96(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC008261 Genomic DNA. Translation: AAF26156.1.
CP002686 Genomic DNA. Translation: AEE73621.1.
AY054467 mRNA. Translation: AAK96659.1.
BT002555 mRNA. Translation: AAO00915.1.
IPIIPI00531533.
RefSeqNP_186767.1. NM_110984.2.
UniGeneAt.18317.

3D structure databases

ProteinModelPortalQ9MAC8.
SMRQ9MAC8. Positions 301-787.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9MAC8. 10 interactions.
STRING3702.AT3G01180.1-P.

Protein family/group databases

CAZyGT5. Glycosyltransferase Family 5.

Proteomic databases

PaxDbQ9MAC8.
PRIDEQ9MAC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G01180.1; AT3G01180.1; AT3G01180.
GeneID820294.
KEGGath:AT3G01180.

Organism-specific databases

TAIRAt3g01180.

Phylogenomic databases

eggNOGCOG0297.
HOGENOMHOG000294940.
InParanoidQ9MAC8.
KOK00703.
OMAECAPFSK.
PhylomeDBQ9MAC8.
ProtClustDBCLSN2684979.

Enzyme and pathway databases

UniPathwayUPA00152.

Gene expression databases

GenevestigatorQ9MAC8.

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 nameSSY2_ARATH
AccessionPrimary (citable) accession number: Q9MAC8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: October 1, 2000
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents