Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Starch synthase 2, chloroplastic/amyloplastic

Gene

SS2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

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 sitei315 – 3151ADP-glucoseBy similarity

GO - Molecular functioni

  1. starch synthase activity Source: UniProtKB

GO - Biological processi

  1. amylopectin biosynthetic process Source: UniProtKB
  2. starch biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Starch biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00152.

Protein family/group databases

CAZyiGT5. Glycosyltransferase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Starch synthase 2, chloroplastic/amyloplastic (EC:2.4.1.21)
Short name:
AtSS2
Alternative name(s):
Soluble starch synthase II
Gene namesi
Name:SS2
Ordered Locus Names:At3g01180
ORF Names:T4P13.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G01180.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Amyloplast, Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Reduced plant growth under short day photopheriod conditions and starch granules with alterated morphology.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555ChloroplastSequence AnalysisAdd
BLAST
Chaini56 – 792737Starch synthase 2, chloroplastic/amyloplasticPRO_0000419769Add
BLAST

Proteomic databases

PaxDbiQ9MAC8.
PRIDEiQ9MAC8.

Expressioni

Tissue specificityi

Expressed in roots, leaves and flowers.1 Publication

Gene expression databases

ExpressionAtlasiQ9MAC8. baseline and differential.
GenevestigatoriQ9MAC8.

Interactioni

Protein-protein interaction databases

IntActiQ9MAC8. 10 interactions.
STRINGi3702.AT3G01180.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9MAC8.
SMRiQ9MAC8. Positions 294-785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi146 – 24297Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294940.
InParanoidiQ9MAC8.
KOiK00703.
OMAiRGPIDDF.
PhylomeDBiQ9MAC8.

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.

Q9MAC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVAESSFP LLCQIKTQRR INSSTLRHSR VSYHDLPSGS LSFRSRSFVL
60 70 80 90 100
GHRCKCVSRV EASGSDDDEP EDALQATIDK SKKVLAMQRN LLHQIAERRK
110 120 130 140 150
LVSSIKESTP DLDDAKASSK QESASSVNAN TDATKKEIMD GDANGSVSPS
160 170 180 190 200
TYGKSSLSKE PEAKTFSPST ESLKNRKQSS ASVISSSPVT SPQKPSDVAT
210 220 230 240 250
NGKPWSSVVA SSVDPPYKPS SVMTSPEKTS DPVTSPGKPS KSRAGAFWSD
260 270 280 290 300
PLPSYLTKAP QTSTMKTEKY VEKTPDVASS ETNEPGKDEE KPPPLAGANV
310 320 330 340 350
MNVILVAAEC APFSKTGGLG DVAGALPKSL ARRGHRVMVV VPRYAEYAEA
360 370 380 390 400
KDLGVRKRYK VAGQDMEVMY FHAFIDGVDF VFIDSPEFRH LSNNIYGGNR
410 420 430 440 450
LDILKRMVLF CKAAVEVPWY VPCGGVCYGD GNLAFIANDW HTALLPVYLK
460 470 480 490 500
AYYRDHGIMK YTRSVLVIHN IAHQGRGPVD DFSYVDLPSH YLDSFKLYDP
510 520 530 540 550
VGGEHFNIFA AGLKAADRVL TVSHGYSWEV KTLEGGWGLH NIINENDWKF
560 570 580 590 600
RGIVNGIDTQ EWNPEFDTYL HSDDYTNYSL ENLHIGKPQC KAALQKELGL
610 620 630 640 650
PVRPDVPLIG FIGRLDHQKG VDLIAEAVPW MMSQDVQLVM LGTGRPDLEE
660 670 680 690 700
VLRQMEHQYR DKARGWVGFS VKTAHRITAG ADILLMPSRF EPCGLNQLYA
710 720 730 740 750
MNYGTIPVVH AVGGLRDTVQ QFDPYSETGL GWTFDSAEAG KLIHALGNCL
760 770 780 790
LTYREYKESW EGLQRRGMTQ DLSWDNAAEK YEEVLVAAKY HW
Length:792
Mass (Da):87,593
Last modified:October 1, 2000 - v1
Checksum:iF8C852E4119EF670
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008261 Genomic DNA. Translation: AAF26156.1.
CP002686 Genomic DNA. Translation: AEE73621.1.
AY054467 mRNA. Translation: AAK96659.1.
BT002555 mRNA. Translation: AAO00915.1.
RefSeqiNP_186767.1. NM_110984.2.
UniGeneiAt.18317.

Genome annotation databases

EnsemblPlantsiAT3G01180.1; AT3G01180.1; AT3G01180.
GeneIDi820294.
KEGGiath:AT3G01180.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008261 Genomic DNA. Translation: AAF26156.1.
CP002686 Genomic DNA. Translation: AEE73621.1.
AY054467 mRNA. Translation: AAK96659.1.
BT002555 mRNA. Translation: AAO00915.1.
RefSeqiNP_186767.1. NM_110984.2.
UniGeneiAt.18317.

3D structure databases

ProteinModelPortaliQ9MAC8.
SMRiQ9MAC8. Positions 294-785.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9MAC8. 10 interactions.
STRINGi3702.AT3G01180.1-P.

Protein family/group databases

CAZyiGT5. Glycosyltransferase Family 5.

Proteomic databases

PaxDbiQ9MAC8.
PRIDEiQ9MAC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G01180.1; AT3G01180.1; AT3G01180.
GeneIDi820294.
KEGGiath:AT3G01180.

Organism-specific databases

TAIRiAT3G01180.

Phylogenomic databases

eggNOGiCOG0297.
HOGENOMiHOG000294940.
InParanoidiQ9MAC8.
KOiK00703.
OMAiRGPIDDF.
PhylomeDBiQ9MAC8.

Enzyme and pathway databases

UniPathwayiUPA00152.

Gene expression databases

ExpressionAtlasiQ9MAC8. baseline and differential.
GenevestigatoriQ9MAC8.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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.
    , 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(2002) [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(2006) [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  6. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSSY2_ARATH
AccessioniPrimary (citable) accession number: Q9MAC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2012
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.