CALSB_ARATH
ID CALSB_ARATH Reviewed; 1768 AA.
AC Q9S9U0; Q949N5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Callose synthase 11;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 1;
GN Name=CALS11; Synonyms=GSL1; OrderedLocusNames=At4g04970; ORFNames=T32N4.8;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1361-1768.
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 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 [5]
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: Required the formation of the callose wall separating the
CC tetraspores (interstitial wall), but not for the callose wall
CC surrounding the pollen mother cells (peripheral wall). Functionally
CC redudant to CALS12 (GSL5). During plant growth and development, callose
CC is found as a transitory component of the cell plate in dividing cells,
CC is a major component of pollen mother cell walls and pollen tubes, and
CC is found as a structural component of plasmodesmatal canals.
CC {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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16021399}.
CC -!- DISRUPTION PHENOTYPE: Plants develop collapsed and inviable pollen
CC grains. {ECO:0000269|PubMed:16021399}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; AF162444; AAD48971.1; -; Genomic_DNA.
DR EMBL; AL161502; CAB81039.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82451.1; -; Genomic_DNA.
DR EMBL; AY050990; AAK93667.2; -; mRNA.
DR PIR; E85062; E85062.
DR RefSeq; NP_567278.1; NM_116736.2.
DR AlphaFoldDB; Q9S9U0; -.
DR STRING; 3702.AT4G04970.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9S9U0; -.
DR PaxDb; Q9S9U0; -.
DR PRIDE; Q9S9U0; -.
DR ProteomicsDB; 222795; -.
DR EnsemblPlants; AT4G04970.1; AT4G04970.1; AT4G04970.
DR GeneID; 825838; -.
DR Gramene; AT4G04970.1; AT4G04970.1; AT4G04970.
DR KEGG; ath:AT4G04970; -.
DR Araport; AT4G04970; -.
DR TAIR; locus:2138396; AT4G04970.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_1_1_1; -.
DR InParanoid; Q9S9U0; -.
DR OMA; PRCEDAK; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9S9U0; -.
DR BioCyc; ARA:AT4G04970-MON; -.
DR PRO; PR:Q9S9U0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S9U0; baseline and differential.
DR Genevisible; Q9S9U0; AT.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEP: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 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;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1768
FT /note="Callose synthase 11"
FT /id="PRO_0000334583"
FT TOPO_DOM 1..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..1341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1363..1386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1387..1407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1408..1413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1414..1434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1435..1481
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1482..1502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1503..1508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1509..1529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1530..1583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1584..1604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1605..1612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1613..1633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1634..1649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1650..1670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1671..1673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1674..1694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1695..1719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1720..1740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1741..1768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1768 AA; 205526 MW; 1F7C5E0CF74EFF0C CRC64;
MRRQRPSVAT ARDAPSLEVY NIIPIHDFLT EHPSLRYPEV RAAAAALRIV GDLPKPPFAD
FTPRMDLMDW LGLLFGFQID NVRNQRENLV LHLANSQMRL QPPPRHPDGL DPTVLRRFRK
KLLRNYTNWC SFLGVRCHVT SPIQSRHQTN AVLNLRRELL YVALYLLIWG ESANLRFMPE
CLCYIFHHMA MELNKVLAGE FDDMTGMPYW PSFSGDCAFL KSVVMPIYKT VKTEVESSNN
GTKPHSAWRN YDDINEYFWS KRALKSLKWP LDYTSNFFDT TPKSSRVGKT GFVEQRSFWN
VYRSFDRLWI LLLLYLQAAI IVATSDVKFP WQDRDVEVAL LTVFISWAGL RLLQSVLDAS
TQYSLVSRET YWLFIRLTLK FVVAVAWTVL FSVFYARIWS QKNKDGVWSR AANERVVTFL
KVVFVYVIPE LLALVLFIVP CIRNWVEELN LGVVYFLTWW FYSKTFVGRG MREGLVDNVK
YTLFWIIVLA TKFIFSYFLQ IRPLIAPTRA LLNLKDATYN WHEFFGSTHR IAVGMLWLPV
ILVYLMDLQI WYSIYSSLVG ATIGLFSHLG EIRNIDQLRL RFQFFSSAMQ FNLKPEEHLL
SPKATMLKKA RDAIHRLKLR YGIGQPFNKI ESSQVEATWF ALIWNEIILT FREEDLISDR
EVELLELPPN CWNIRVIRWP CFLLCNELLL ALSQANELCD APDHWLWSKI CSSEYRRCAV
MEAFDSIKFV ILKIVKNGTE EESILNRLFM EIDENVENEK ITEVYKLTVL LRIHEKLISL
LERLMDPEKK VFRIVNILQA LYELCAWEFP KTRRSTPQLR QLGLAPISLE ADTELLFVNA
INLPPLDDVV FYRQIRRVHT ILTSRDPMHN VPKNIEARER LAFFSNSLFM TMPQAPSVEK
MMAFSVLTPY YDEEVMYRQE MLRAENEDGI STLFYLQRIY EDEWVNFLER MRREGAENEN
DIWSKKVRDL RLWASYRGQT LSRTVRGMMY YYSALKKLAF LDSASEMDIR MGTQIAPEAR
RSYYTNDGGD NTLQPTPSQE ISRMASGITH LLKGSEYGSA MMKFTYVVAC QVYGQHKARG
DHRAEEILFL MKNHDALRIA YVDEVDLGRG EVEYYSVLVK FDQQLQREVE IYRIRLPGPL
KLGEGKPENQ NHALIFTRGD AIQTIDMNQD NHFEEALKMR NLLESFKTYY GIRKPTILGV
REKVFTGSVS SLAWFMSAQE TSFVTLGQRV LANPLKVRMH YGHPDVFDRF WFVPRGGISK
ASRVINISED IFAGFNCTLR GGNVTHHEYI QVGKGRDVGL NQISMFEAKV ASGNGEQALS
RDVYRLGHRL DFFRMLSFFY TTVGYYFNTM LIVFTVYAFL WGRLYLALSG VEKIAKDRSS
SNEALGAILN QQFIIQLGLF TALPMILENS LERGFLPAVW DFITMQLQLA SFFYTFSMGT
RTHYFGRTIL HGGAKYRATG RGFVVEHKKF AENYRLYART HFIKAIELAI ILLVYAAYSP
LAKSSFVYIL MTISSWFLIT SWIISPFLFN PSGFDWLKTV NDFDDFIAWL WSRGGLFTKA
DQSWFTWWNE EQEHLKTTGV WGKLLEIILD LRFFFFQYSI VYHLRIAENR TSIGVYLISW
GCIIGIVAIY ITTIYAQKRY SVKEHIKYRF IQFLVILLTV LVVVMMLQFT KLTVVDLLIS
LLAFVPTGWG LISIAQVLKP FLLSTVVWDT VISVARFYDL FFGLIVMAPV ALLSWLPGFQ
NMQTRILFNE AFSRGLQISI ILAGKKST
