CALSC_ARATH
ID CALSC_ARATH Reviewed; 1780 AA.
AC Q9ZT82;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Callose synthase 12;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 5;
DE AltName: Full=Protein POWDERY MILDEW RESISTANT 4;
GN Name=CALS12; Synonyms=GSL5, PMR4; OrderedLocusNames=At4g03550;
GN ORFNames=F9H3.18, T5L23.4;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11283334; DOI=10.2307/3871338;
RA Hong Z., Delauney A.J., Verma D.P.S.;
RT "A cell plate-specific callose synthase and its interaction with
RT phragmoplastin.";
RL Plant Cell 13:755-768(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12081364; DOI=10.1023/a:1015558231400;
RA Oestergaard L., Petersen M., Mattsson O., Mundy J.;
RT "An Arabidopsis callose synthase.";
RL Plant Mol. Biol. 49:559-566(2002).
RN [5]
RP FUNCTION.
RX PubMed=14555698; DOI=10.1105/tpc.016097;
RA Jacobs A.K., Lipka V., Burton R.A., Panstruga R., Strizhov N.,
RA Schulze-Lefert P., Fincher G.B.;
RT "An Arabidopsis callose synthase, GSL5, is required for wound and papillary
RT callose formation.";
RL Plant Cell 15:2503-2513(2003).
RN [6]
RP FUNCTION.
RX PubMed=12920300; DOI=10.1126/science.1086716;
RA Nishimura M.T., Stein M., Hou B.-H., Vogel J.P., Edwards H.,
RA Somerville S.C.;
RT "Loss of a callose synthase results in salicylic acid-dependent disease
RT resistance.";
RL Science 301:969-972(2003).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=16021399; DOI=10.1007/s11103-005-4526-7;
RA Enns L.C., Kanaoka M.M., Torii K.U., Comai L., Okada K., Cleland R.E.;
RT "Two callose synthases, GSL1 and GSL5, play an essential and redundant role
RT in plant and pollen development and in fertility.";
RL Plant Mol. Biol. 58:333-349(2005).
CC -!- FUNCTION: Involved in sporophytic and gametophytic development.
CC Required for normal leaf development. During pollen formation, required
CC for the formation of the callose wall separating the tetraspores of the
CC tetrad (interstitial wall), but not for the callose wall surrounding
CC the pollen mother cells (peripheral wall). Functionally redudant to
CC CALS11 (GSL1). May play a role later in pollen grain maturation.
CC Required for callose formation induced by wounding and pathogen attack.
CC May interfere with salicylic acid-induced signaling pathway during
CC defense response. During plant growth and development, callose is found
CC as a transitory component of the cell plate in dividing cells, is a
CC major component of pollen mother cell walls and pollen tubes, and is
CC found as a structural component of plasmodesmatal canals.
CC {ECO:0000269|PubMed:12081364, ECO:0000269|PubMed:12920300,
CC ECO:0000269|PubMed:14555698, ECO:0000269|PubMed:16021399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12081364};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12081364}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed at low
CC levels in roots, leaves, stems, cauline leaves and siliques.
CC {ECO:0000269|PubMed:12081364, ECO:0000269|PubMed:16021399}.
CC -!- INDUCTION: By salicylic acid (SA). {ECO:0000269|PubMed:12081364}.
CC -!- DISRUPTION PHENOTYPE: Plants develop smaller leaves, and collapsed and
CC inviable pollen grains. They are resistant to the biotrophic pathogens
CC Erysiphe cichoracearum (powdery mildew), E.orontii and Hyaloperonospora
CC parasitica. {ECO:0000269|PubMed:16021399}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; AC005142; AAD15311.1; -; Genomic_DNA.
DR EMBL; AF071527; AAD11597.1; -; Genomic_DNA.
DR EMBL; AL161497; CAB77840.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82336.1; -; Genomic_DNA.
DR PIR; A85045; A85045.
DR RefSeq; NP_192264.1; NM_116593.4.
DR AlphaFoldDB; Q9ZT82; -.
DR SASBDB; Q9ZT82; -.
DR BioGRID; 10964; 3.
DR STRING; 3702.AT4G03550.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9ZT82; -.
DR PaxDb; Q9ZT82; -.
DR PRIDE; Q9ZT82; -.
DR ProteomicsDB; 222796; -.
DR EnsemblPlants; AT4G03550.1; AT4G03550.1; AT4G03550.
DR GeneID; 825650; -.
DR Gramene; AT4G03550.1; AT4G03550.1; AT4G03550.
DR KEGG; ath:AT4G03550; -.
DR Araport; AT4G03550; -.
DR TAIR; locus:2128786; AT4G03550.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_1_1_1; -.
DR InParanoid; Q9ZT82; -.
DR OMA; GKSNRFA; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9ZT82; -.
DR BioCyc; ARA:AT4G03550-MON; -.
DR PRO; PR:Q9ZT82; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZT82; baseline and differential.
DR Genevisible; Q9ZT82; AT.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0000003; P:reproduction; IGI:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IEP:TAIR.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1780
FT /note="Callose synthase 12"
FT /id="PRO_0000334584"
FT TOPO_DOM 1..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..348
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..1348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1349..1369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1370..1394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1416..1421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1422..1442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1443..1489
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1490..1510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1511..1516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1517..1537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1538..1588
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1589..1609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1610..1620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1621..1641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1642..1657
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1658..1678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1679..1681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1682..1702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1703..1728
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1729..1749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1750..1780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 1712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1780 AA; 206912 MW; DD4F0BD3AE54DDD0 CRC64;
MSLRHRTVPP QTGRPLAAEA VGIEEEPYNI IPVNNLLADH PSLRFPEVRA AAAALKTVGD
LRRPPYVQWR SHYDLLDWLA LFFGFQKDNV RNQREHMVLH LANAQMRLSP PPDNIDSLDS
AVVRRFRRKL LANYSSWCSY LGKKSNIWIS DRNPDSRREL LYVGLYLLIW GEAANLRFMP
ECICYIFHNM ASELNKILED CLDENTGQPY LPSLSGENAF LTGVVKPIYD TIQAEIDESK
NGTVAHCKWR NYDDINEYFW TDRCFSKLKW PLDLGSNFFK SRGKSVGKTG FVERRTFFYL
YRSFDRLWVM LALFLQAAII VAWEEKPDTS SVTRQLWNAL KARDVQVRLL TVFLTWSGMR
LLQAVLDAAS QYPLVSRETK RHFFRMLMKV IAAAVWIVAF TVLYTNIWKQ KRQDRQWSNA
ATTKIYQFLY AVGAFLVPEI LALALFIIPW MRNFLEETNW KIFFALTWWF QGKSFVGRGL
REGLVDNIKY STFWIFVLAT KFTFSYFLQV KPMIKPSKLL WNLKDVDYEW HQFYGDSNRF
SVALLWLPVV LIYLMDIQIW YAIYSSIVGA VVGLFDHLGE IRDMGQLRLR FQFFASAIQF
NLMPEEQLLN ARGFGNKFKD GIHRLKLRYG FGRPFKKLES NQVEANKFAL IWNEIILAFR
EEDIVSDREV ELLELPKNSW DVTVIRWPCF LLCNELLLAL SQARELIDAP DKWLWHKICK
NEYRRCAVVE AYDSIKHLLL SIIKVDTEEH SIITVFFQII NQSIQSEQFT KTFRVDLLPK
IYETLQKLVG LVNDEETDSG RVVNVLQSLY EIATRQFFIE KKTTEQLSNE GLTPRDPASK
LLFQNAIRLP DASNEDFYRQ VRRLHTILTS RDSMHSVPVN LEARRRIAFF SNSLFMNMPH
APQVEKMMAF SVLTPYYSEE VVYSKEQLRN ETEDGISTLY YLQTIYADEW KNFKERMHRE
GIKTDSELWT TKLRDLRLWA SYRGQTLART VRGMMYYYRA LKMLAFLDSA SEMDIREGAQ
ELGSVRNLQG ELGGQSDGFV SENDRSSLSR ASSSVSTLYK GHEYGTALMK FTYVVACQIY
GSQKAKKEPQ AEEILYLMKQ NEALRIAYVD EVPAGRGETD YYSVLVKYDH QLEKEVEIFR
VKLPGPVKLG EGKPENQNHA MIFTRGDAVQ TIDMNQDSYF EEALKMRNLL QEYNHYHGIR
KPTILGVREH IFTGSVSSLA WFMSAQETSF VTLGQRVLAN PLKVRMHYGH PDVFDRFWFL
SRGGISKASR VINISEDIFA GFNCTLRGGN VTHHEYIQVG KGRDVGLNQI SMFEAKVASG
NGEQVLSRDV YRLGHRLDFF RMLSFFYTTV GFFFNTMMVI LTVYAFLWGR VYLALSGVEK
SALADSTDTN AALGVILNQQ FIIQLGLFTA LPMIVEWSLE EGFLLAIWNF IRMQIQLSAV
FYTFSMGTRA HYFGRTILHG GAKYRATGRG FVVEHKGFTE NYRLYARSHF VKAIELGLIL
IVYASHSPIA KDSLIYIAMT ITSWFLVISW IMAPFVFNPS GFDWLKTVYD FEDFMNWIWY
QGRISTKSEQ SWEKWWYEEQ DHLRNTGKAG LFVEIILVLR FFFFQYGIVY QLKIANGSTS
LFVYLFSWIY IFAIFVLFLV IQYARDKYSA KAHIRYRLVQ FLLIVLAILV IVALLEFTHF
SFIDIFTSLL AFIPTGWGIL LIAQTQRKWL KNYTIFWNAV VSVARMYDIL FGILIMVPVA
FLSWMPGFQS MQTRILFNEA FSRGLRIMQI VTGKKSKGDV
