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Q9ZT82 (CALSC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Callose synthase 12
EC=2.4.1.34
Alternative name(s):
1,3-beta-glucan synthase
Protein GLUCAN SYNTHASE-LIKE 5
Protein POWDERY MILDEW RESISTANT 4
Gene names
Name:CALS12
Synonyms:GSL5, PMR4
Ordered Locus Names:At4g03550
ORF Names:F9H3.18, T5L23.4
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1780 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in sporophytic and gametophytic development. Required for normal leaf development. During pollen formation, required for the formation of the callose wall separating the tetraspores of the tetrad (interstitial wall), but not for the callose wall surrounding the pollen mother cells (peripheral wall). Functionally redudant to CALS11 (GSL1). May play a role later in pollen grain maturation. Required for callose formation induced by wounding and pathogen attack. May interfere with salicylic acid-induced signaling pathway during defense response. During plant growth and development, callose is found as a transitory component of the cell plate in dividing cells, is a major component of pollen mother cell walls and pollen tubes, and is found as a structural component of plasmodesmatal canals. Ref.4 Ref.5 Ref.6 Ref.7

Catalytic activity

UDP-glucose + ((1->3)-beta-D-glucosyl)(n) = UDP + ((1->3)-beta-D-glucosyl)(n+1).

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.4.

Tissue specificity

Hihgly expressed in flowers. Expressed at low levels in roots, leaves, stems, cauline leaves and siliques. Ref.4 Ref.7

Induction

By salicylic acid (SA). Ref.4

Disruption phenotype

Plants develop smaller leaves, and collapsed and inviable pollen grains. They are resistant to the biotrophic pathogens Erysiphe cichoracearum (powdery mildew), E.orontii and Hyaloperonospora parasitica. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 48 family.

Ontologies

Keywords
   Biological processCell shape
Cell wall biogenesis/degradation
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological process(1->3)-beta-D-glucan biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

defense response by callose deposition in cell wall

Inferred from mutant phenotype. Source: TAIR

defense response signaling pathway, resistance gene-dependent

Inferred from mutant phenotype. Source: TAIR

defense response to bacterium

Inferred from mutant phenotype. Source: TAIR

leaf morphogenesis

Inferred from mutant phenotype. Source: TAIR

leaf senescence

Inferred from mutant phenotype. Source: TAIR

pollen development

Inferred from genetic interaction Ref.7. Source: TAIR

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

reproduction

Inferred from genetic interaction Ref.7. Source: TAIR

response to fungus

Inferred from mutant phenotype. Source: TAIR

salicylic acid mediated signaling pathway

Inferred from expression pattern. Source: TAIR

   Cellular component1,3-beta-D-glucan synthase complex

Inferred from electronic annotation. Source: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasmodesma

Inferred from direct assay. Source: TAIR

   Molecular function1,3-beta-D-glucan synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17801780Callose synthase 12
PRO_0000334584

Regions

Topological domain1 – 302302Cytoplasmic Potential
Transmembrane303 – 32321Helical; Potential
Topological domain324 – 34825Extracellular Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 38617Cytoplasmic Potential
Transmembrane387 – 40721Helical; Potential
Topological domain408 – 42720Extracellular Potential
Transmembrane428 – 44821Helical; Potential
Topological domain449 – 48941Cytoplasmic Potential
Transmembrane490 – 51021Helical; Potential
Topological domain511 – 54232Extracellular Potential
Transmembrane543 – 56321Helical; Potential
Topological domain564 – 1348785Cytoplasmic Potential
Transmembrane1349 – 136921Helical; Potential
Topological domain1370 – 139425Extracellular Potential
Transmembrane1395 – 141521Helical; Potential
Topological domain1416 – 14216Cytoplasmic Potential
Transmembrane1422 – 144221Helical; Potential
Topological domain1443 – 148947Extracellular Potential
Transmembrane1490 – 151021Helical; Potential
Topological domain1511 – 15166Cytoplasmic Potential
Transmembrane1517 – 153721Helical; Potential
Topological domain1538 – 158851Extracellular Potential
Transmembrane1589 – 160921Helical; Potential
Topological domain1610 – 162011Cytoplasmic Potential
Transmembrane1621 – 164121Helical; Potential
Topological domain1642 – 165716Extracellular Potential
Transmembrane1658 – 167821Helical; Potential
Topological domain1679 – 16813Cytoplasmic Potential
Transmembrane1682 – 170221Helical; Potential
Topological domain1703 – 172826Extracellular Potential
Transmembrane1729 – 174921Helical; Potential
Topological domain1750 – 178031Cytoplasmic Potential
Compositional bias50 – 545Poly-Ala
Compositional bias1601 – 16044Poly-Phe

Amino acid modifications

Modified residue10531Phosphoserine Ref.8
Glycosylation17121N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZT82 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DD4F0BD3AE54DDD0

FASTA1,780206,912
        10         20         30         40         50         60 
MSLRHRTVPP QTGRPLAAEA VGIEEEPYNI IPVNNLLADH PSLRFPEVRA AAAALKTVGD 

        70         80         90        100        110        120 
LRRPPYVQWR SHYDLLDWLA LFFGFQKDNV RNQREHMVLH LANAQMRLSP PPDNIDSLDS 

       130        140        150        160        170        180 
AVVRRFRRKL LANYSSWCSY LGKKSNIWIS DRNPDSRREL LYVGLYLLIW GEAANLRFMP 

       190        200        210        220        230        240 
ECICYIFHNM ASELNKILED CLDENTGQPY LPSLSGENAF LTGVVKPIYD TIQAEIDESK 

       250        260        270        280        290        300 
NGTVAHCKWR NYDDINEYFW TDRCFSKLKW PLDLGSNFFK SRGKSVGKTG FVERRTFFYL 

       310        320        330        340        350        360 
YRSFDRLWVM LALFLQAAII VAWEEKPDTS SVTRQLWNAL KARDVQVRLL TVFLTWSGMR 

       370        380        390        400        410        420 
LLQAVLDAAS QYPLVSRETK RHFFRMLMKV IAAAVWIVAF TVLYTNIWKQ KRQDRQWSNA 

       430        440        450        460        470        480 
ATTKIYQFLY AVGAFLVPEI LALALFIIPW MRNFLEETNW KIFFALTWWF QGKSFVGRGL 

       490        500        510        520        530        540 
REGLVDNIKY STFWIFVLAT KFTFSYFLQV KPMIKPSKLL WNLKDVDYEW HQFYGDSNRF 

       550        560        570        580        590        600 
SVALLWLPVV LIYLMDIQIW YAIYSSIVGA VVGLFDHLGE IRDMGQLRLR FQFFASAIQF 

       610        620        630        640        650        660 
NLMPEEQLLN ARGFGNKFKD GIHRLKLRYG FGRPFKKLES NQVEANKFAL IWNEIILAFR 

       670        680        690        700        710        720 
EEDIVSDREV ELLELPKNSW DVTVIRWPCF LLCNELLLAL SQARELIDAP DKWLWHKICK 

       730        740        750        760        770        780 
NEYRRCAVVE AYDSIKHLLL SIIKVDTEEH SIITVFFQII NQSIQSEQFT KTFRVDLLPK 

       790        800        810        820        830        840 
IYETLQKLVG LVNDEETDSG RVVNVLQSLY EIATRQFFIE KKTTEQLSNE GLTPRDPASK 

       850        860        870        880        890        900 
LLFQNAIRLP DASNEDFYRQ VRRLHTILTS RDSMHSVPVN LEARRRIAFF SNSLFMNMPH 

       910        920        930        940        950        960 
APQVEKMMAF SVLTPYYSEE VVYSKEQLRN ETEDGISTLY YLQTIYADEW KNFKERMHRE 

       970        980        990       1000       1010       1020 
GIKTDSELWT TKLRDLRLWA SYRGQTLART VRGMMYYYRA LKMLAFLDSA SEMDIREGAQ 

      1030       1040       1050       1060       1070       1080 
ELGSVRNLQG ELGGQSDGFV SENDRSSLSR ASSSVSTLYK GHEYGTALMK FTYVVACQIY 

      1090       1100       1110       1120       1130       1140 
GSQKAKKEPQ AEEILYLMKQ NEALRIAYVD EVPAGRGETD YYSVLVKYDH QLEKEVEIFR 

      1150       1160       1170       1180       1190       1200 
VKLPGPVKLG EGKPENQNHA MIFTRGDAVQ TIDMNQDSYF EEALKMRNLL QEYNHYHGIR 

      1210       1220       1230       1240       1250       1260 
KPTILGVREH IFTGSVSSLA WFMSAQETSF VTLGQRVLAN PLKVRMHYGH PDVFDRFWFL 

      1270       1280       1290       1300       1310       1320 
SRGGISKASR VINISEDIFA GFNCTLRGGN VTHHEYIQVG KGRDVGLNQI SMFEAKVASG 

      1330       1340       1350       1360       1370       1380 
NGEQVLSRDV YRLGHRLDFF RMLSFFYTTV GFFFNTMMVI LTVYAFLWGR VYLALSGVEK 

      1390       1400       1410       1420       1430       1440 
SALADSTDTN AALGVILNQQ FIIQLGLFTA LPMIVEWSLE EGFLLAIWNF IRMQIQLSAV 

      1450       1460       1470       1480       1490       1500 
FYTFSMGTRA HYFGRTILHG GAKYRATGRG FVVEHKGFTE NYRLYARSHF VKAIELGLIL 

      1510       1520       1530       1540       1550       1560 
IVYASHSPIA KDSLIYIAMT ITSWFLVISW IMAPFVFNPS GFDWLKTVYD FEDFMNWIWY 

      1570       1580       1590       1600       1610       1620 
QGRISTKSEQ SWEKWWYEEQ DHLRNTGKAG LFVEIILVLR FFFFQYGIVY QLKIANGSTS 

      1630       1640       1650       1660       1670       1680 
LFVYLFSWIY IFAIFVLFLV IQYARDKYSA KAHIRYRLVQ FLLIVLAILV IVALLEFTHF 

      1690       1700       1710       1720       1730       1740 
SFIDIFTSLL AFIPTGWGIL LIAQTQRKWL KNYTIFWNAV VSVARMYDIL FGILIMVPVA 

      1750       1760       1770       1780 
FLSWMPGFQS MQTRILFNEA FSRGLRIMQI VTGKKSKGDV

« 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: 10617198] [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]"A cell plate-specific callose synthase and its interaction with phragmoplastin."
Hong Z., Delauney A.J., Verma D.P.S.
Plant Cell 13:755-768(2001) [PubMed: 11283334] [Abstract]
Cited for: GENE FAMILY AND NOMENCLATURE.
[4]"An Arabidopsis callose synthase."
Oestergaard L., Petersen M., Mattsson O., Mundy J.
Plant Mol. Biol. 49:559-566(2002) [PubMed: 12081364] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[5]"An Arabidopsis callose synthase, GSL5, is required for wound and papillary callose formation."
Jacobs A.K., Lipka V., Burton R.A., Panstruga R., Strizhov N., Schulze-Lefert P., Fincher G.B.
Plant Cell 15:2503-2513(2003) [PubMed: 14555698] [Abstract]
Cited for: FUNCTION.
[6]"Loss of a callose synthase results in salicylic acid-dependent disease resistance."
Nishimura M.T., Stein M., Hou B.-H., Vogel J.P., Edwards H., Somerville S.C.
Science 301:969-972(2003) [PubMed: 12920300] [Abstract]
Cited for: FUNCTION.
[7]"Two callose synthases, GSL1 and GSL5, play an essential and redundant role in plant and pollen development and in fertility."
Enns L.C., Kanaoka M.M., Torii K.U., Comai L., Okada K., Cleland R.E.
Plant Mol. Biol. 58:333-349(2005) [PubMed: 16021399] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, NOMENCLATURE, DISRUPTION PHENOTYPE.
[8]"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(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1053, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC005142 Genomic DNA. Translation: AAD15311.1.
AF071527 Genomic DNA. Translation: AAD11597.1.
AL161497 Genomic DNA. Translation: CAB77840.1.
CP002687 Genomic DNA. Translation: AEE82336.1.
IPIIPI00544563.
PIRA85045.
RefSeqNP_192264.1. NM_116593.3.
UniGeneAt.3956.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ZT82.

Protein family/group databases

CAZyGT48. Glycosyltransferase Family 48.

Proteomic databases

PRIDEQ9ZT82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G03550.1; AT4G03550.1; AT4G03550.
GeneID825650.
GenomeReviewsGene locus AT4G03550 in contig CT486007_GR.
KEGGath:AT4G03550.
NMPDRfig|3702.1.peg.18188.

Organism-specific databases

TAIRAt4g03550.

Phylogenomic databases

eggNOGKOG0916.
GeneTreeEPGT00070000028111.
HOGENOMHBG316390.
InParanoidQ9ZT82.
OMANIWISDR.
PhylomeDBQ9ZT82.
ProtClustDBCLSN2685951.

Gene expression databases

ArrayExpressQ9ZT82.
GenevestigatorQ9ZT82.

Family and domain databases

InterProIPR003440. Glyco_trans_48.
[Graphical view]
KOK11000.
PfamPF02364. Glucan_synthase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALSC_ARATH
AccessionPrimary (citable) accession number: Q9ZT82
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 67 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

SIMILARITY comments

Index of protein domains and families

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