SSY2_ARATH
ID SSY2_ARATH Reviewed; 792 AA.
AC Q9MAC8;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Starch synthase 2, chloroplastic/amyloplastic;
DE Short=AtSS2;
DE EC=2.4.1.21;
DE AltName: Full=Soluble starch synthase II;
DE Flags: Precursor;
GN Name=SS2; OrderedLocusNames=At3g01180; ORFNames=T4P13.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17217470; DOI=10.1111/j.1365-313x.2006.02968.x;
RA Roldan I., Wattebled F., Mercedes Lucas M., Delvalle D., Planchot V.,
RA Jimenez S., Perez R., Ball S., D'Hulst C., Merida A.;
RT "The phenotype of soluble starch synthase IV defective mutants of
RT Arabidopsis thaliana suggests a novel function of elongation enzymes in the
RT control of starch granule formation.";
RL Plant J. 49:492-504(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18811962; DOI=10.1186/1471-2229-8-96;
RA Zhang X., Szydlowski N., Delvalle D., D'Hulst C., James M.G., Myers A.M.;
RT "Overlapping functions of the starch synthases SSII and SSIII in
RT amylopectin biosynthesis in Arabidopsis.";
RL BMC Plant Biol. 8:96-96(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Involved in the synthesis of glycan chains within amylopectin
CC in leaves. Is required to produce chains with a degree of
CC polymerization of 12 to 25 (DP12-DP25). {ECO:0000269|PubMed:18811962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:17217470}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant growth under short day photopheriod
CC conditions and starch granules with alterated morphology.
CC {ECO:0000269|PubMed:18811962}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC008261; AAF26156.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73621.1; -; Genomic_DNA.
DR EMBL; AY054467; AAK96659.1; -; mRNA.
DR EMBL; BT002555; AAO00915.1; -; mRNA.
DR RefSeq; NP_186767.1; NM_110984.3.
DR AlphaFoldDB; Q9MAC8; -.
DR SMR; Q9MAC8; -.
DR BioGRID; 5628; 11.
DR IntAct; Q9MAC8; 10.
DR STRING; 3702.AT3G01180.1; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR iPTMnet; Q9MAC8; -.
DR PaxDb; Q9MAC8; -.
DR PRIDE; Q9MAC8; -.
DR ProteomicsDB; 228258; -.
DR EnsemblPlants; AT3G01180.1; AT3G01180.1; AT3G01180.
DR GeneID; 820294; -.
DR Gramene; AT3G01180.1; AT3G01180.1; AT3G01180.
DR KEGG; ath:AT3G01180; -.
DR Araport; AT3G01180; -.
DR TAIR; locus:2102102; AT3G01180.
DR eggNOG; ENOG502QT35; Eukaryota.
DR HOGENOM; CLU_009583_31_1_1; -.
DR InParanoid; Q9MAC8; -.
DR OMA; MPSRWEP; -.
DR OrthoDB; 732319at2759; -.
DR PhylomeDB; Q9MAC8; -.
DR UniPathway; UPA00152; -.
DR PRO; PR:Q9MAC8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAC8; baseline and differential.
DR Genevisible; Q9MAC8; AT.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0009011; F:starch synthase activity; IMP:UniProtKB.
DR GO; GO:0010021; P:amylopectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02095; glgA; 1.
PE 1: Evidence at protein level;
KW Amyloplast; Chloroplast; Glycosyltransferase; Plastid; Reference proteome;
KW Starch biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..792
FT /note="Starch synthase 2, chloroplastic/amyloplastic"
FT /id="PRO_0000419769"
FT REGION 105..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000250"
SQ SEQUENCE 792 AA; 87593 MW; F8C852E4119EF670 CRC64;
MASVAESSFP LLCQIKTQRR INSSTLRHSR VSYHDLPSGS LSFRSRSFVL GHRCKCVSRV
EASGSDDDEP EDALQATIDK SKKVLAMQRN LLHQIAERRK LVSSIKESTP DLDDAKASSK
QESASSVNAN TDATKKEIMD GDANGSVSPS TYGKSSLSKE PEAKTFSPST ESLKNRKQSS
ASVISSSPVT SPQKPSDVAT NGKPWSSVVA SSVDPPYKPS SVMTSPEKTS DPVTSPGKPS
KSRAGAFWSD PLPSYLTKAP QTSTMKTEKY VEKTPDVASS ETNEPGKDEE KPPPLAGANV
MNVILVAAEC APFSKTGGLG DVAGALPKSL ARRGHRVMVV VPRYAEYAEA KDLGVRKRYK
VAGQDMEVMY FHAFIDGVDF VFIDSPEFRH LSNNIYGGNR LDILKRMVLF CKAAVEVPWY
VPCGGVCYGD GNLAFIANDW HTALLPVYLK AYYRDHGIMK YTRSVLVIHN IAHQGRGPVD
DFSYVDLPSH YLDSFKLYDP VGGEHFNIFA AGLKAADRVL TVSHGYSWEV KTLEGGWGLH
NIINENDWKF RGIVNGIDTQ EWNPEFDTYL HSDDYTNYSL ENLHIGKPQC KAALQKELGL
PVRPDVPLIG FIGRLDHQKG VDLIAEAVPW MMSQDVQLVM LGTGRPDLEE VLRQMEHQYR
DKARGWVGFS VKTAHRITAG ADILLMPSRF EPCGLNQLYA MNYGTIPVVH AVGGLRDTVQ
QFDPYSETGL GWTFDSAEAG KLIHALGNCL LTYREYKESW EGLQRRGMTQ DLSWDNAAEK
YEEVLVAAKY HW
