Reviewed, UniProtKB/Swiss-Prot Q9ZT82 (CALSC_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1780 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.3 Ref.4 Ref.5 Ref.6
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.3
Tissue specificity	Hihgly expressed in flowers. Expressed at low levels in roots, leaves, stems, cauline leaves and siliques. Ref.3 Ref.6
Induction	By salicylic acid (SA). Ref.3
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 Peronospora parasitica. Ref.6
Sequence similarities	Belongs to the glycosyltransferase 48 family.

Ontologies

Keywords
Biological process	Cell shape Cell wall biogenesis/degradation
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	1,3-beta-glucan biosynthetic process Inferred from electronic annotation. Source: InterPro callose deposition in cell wall during defense response 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 regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW response to fungus Inferred from mutant phenotype. Source: TAIR salicylic acid mediated signaling pathway Inferred from expression pattern. Source: TAIR
Cellular component	1,3-beta-glucan synthase complex Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1,3-beta-glucan synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1780	1780	Callose synthase 12		PRO_0000334584
Regions
	Topological domain	1 – 302	302	Cytoplasmic Potential
	Transmembrane	303 – 323	21	Potential
	Topological domain	324 – 348	25	Extracellular Potential
	Transmembrane	349 – 369	21	Potential
	Topological domain	370 – 386	17	Cytoplasmic Potential
	Transmembrane	387 – 407	21	Potential
	Topological domain	408 – 427	20	Extracellular Potential
	Transmembrane	428 – 448	21	Potential
	Topological domain	449 – 489	41	Cytoplasmic Potential
	Transmembrane	490 – 510	21	Potential
	Topological domain	511 – 542	32	Extracellular Potential
	Transmembrane	543 – 563	21	Potential
	Topological domain	564 – 1348	785	Cytoplasmic Potential
	Transmembrane	1349 – 1369	21	Potential
	Topological domain	1370 – 1394	25	Extracellular Potential
	Transmembrane	1395 – 1415	21	Potential
	Topological domain	1416 – 1421	6	Cytoplasmic Potential
	Transmembrane	1422 – 1442	21	Potential
	Topological domain	1443 – 1489	47	Extracellular Potential
	Transmembrane	1490 – 1510	21	Potential
	Topological domain	1511 – 1516	6	Cytoplasmic Potential
	Transmembrane	1517 – 1537	21	Potential
	Topological domain	1538 – 1588	51	Extracellular Potential
	Transmembrane	1589 – 1609	21	Potential
	Topological domain	1610 – 1620	11	Cytoplasmic Potential
	Transmembrane	1621 – 1641	21	Potential
	Topological domain	1642 – 1657	16	Extracellular Potential
	Transmembrane	1658 – 1678	21	Potential
	Topological domain	1679 – 1681	3	Cytoplasmic Potential
	Transmembrane	1682 – 1702	21	Potential
	Topological domain	1703 – 1728	26	Extracellular Potential
	Transmembrane	1729 – 1749	21	Potential
	Topological domain	1750 – 1780	31	Cytoplasmic Potential
	Compositional bias	50 – 54	5	Poly-Ala
	Compositional bias	1601 – 1604	4	Poly-Phe
Amino acid modifications
	Glycosylation	1712	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9ZT82-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: DD4F0BD3AE54DDD0	FASTA	1,780	206,912
	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

References

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[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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC005142 Genomic DNA. Translation: AAD15311.1. AF071527 Genomic DNA. Translation: AAD11597.1. AL161497 Genomic DNA. Translation: CAB77840.1.
IPI	IPI00544563.
PIR	A85045.
RefSeq	NP_192264.1.
UniGene	At.3956
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT48. Glycosyltransferase Family 48.
Proteomic databases
PRIDE	Q9ZT82.
Genome annotation databases
GeneID	825650.
GenomeReviews	Gene locus AT4G03550 in contig CT486007_GR.
KEGG	ath:AT4G03550.
NMPDR	fig|3702.1.peg.18188.
Organism-specific databases
TAIR	At4g03550.
Phylogenomic databases
OMA	Q9ZT82. IYLMDIQ.
Gene expression databases
ArrayExpress	Q9ZT82.
Family and domain databases
InterPro	IPR003440. Glyco_trans_48. [Graphical view]
Pfam	PF02364. Glucan_synthase. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CALSC_ARATH

Accession

Primary (citable) accession number: Q9ZT82

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 1, 1999
Last modified:	July 7, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)