CALS6_ARATH
ID CALS6_ARATH Reviewed; 1921 AA.
AC Q9LYS6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Putative callose synthase 6;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 11;
GN Name=CALS6; Synonyms=GSL11; OrderedLocusNames=At3g59100;
GN ORFNames=F17J16.150;
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 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.
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 [5]
RP NOMENCLATURE.
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: Probably involved in callose synthesis, but not required for
CC callose formation after wounding or pathogen attack. During plant
CC growth and development, callose is found as a transitory component of
CC the cell plate in dividing cells, is a major component of pollen mother
CC cell walls and pollen tubes, and is found as a structural component of
CC plasmodesmatal canals. {ECO:0000269|PubMed:14555698}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163527; CAB86938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79878.1; -; Genomic_DNA.
DR PIR; T47792; T47792.
DR RefSeq; NP_191469.3; NM_115772.4.
DR AlphaFoldDB; Q9LYS6; -.
DR SMR; Q9LYS6; -.
DR STRING; 3702.AT3G59100.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR PaxDb; Q9LYS6; -.
DR PRIDE; Q9LYS6; -.
DR ProteomicsDB; 240588; -.
DR EnsemblPlants; AT3G59100.1; AT3G59100.1; AT3G59100.
DR GeneID; 825079; -.
DR Gramene; AT3G59100.1; AT3G59100.1; AT3G59100.
DR KEGG; ath:AT3G59100; -.
DR Araport; AT3G59100; -.
DR TAIR; locus:2077720; AT3G59100.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; Q9LYS6; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9LYS6; -.
DR BioCyc; ARA:AT3G59100-MON; -.
DR PRO; PR:Q9LYS6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYS6; baseline and differential.
DR Genevisible; Q9LYS6; 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; IBA:GO_Central.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; -; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1921
FT /note="Putative callose synthase 6"
FT /id="PRO_0000334578"
FT TOPO_DOM 1..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..611
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..721
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..1484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1485..1505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1506..1540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1541..1561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1562..1564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1565..1585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1586..1628
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1629..1649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1650..1655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1656..1676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1677..1730
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1731..1751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1752..1759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1760..1780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1781..1796
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1797..1817
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1818..1823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1824..1844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1845..1867
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1868..1888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1889..1921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1921 AA; 223514 MW; F2CC970B984F9710 CRC64;
MEASSSGTAE LPRSLSRRAP SRATTMMIDR PNEDASAMDS ELVPSSLASI APILRVANEI
EKDNPRVAYL CRFHAFEKAH RMDATSSGRG VRQFKTYLLH RLEKEEEETK PQLAKNDPRE
IQAYYQNFYE KYIKEGETSR KPEEMARLYQ IASVLYDVLK TVVPSPKVDY ETRRYAEEVE
RKRDRYEHYN ILPLYAVGTK PAIVELPEVK AAFSAVRNVR NLPRRRIHLP SNTPNEMRKA
RTKLNDILEW LASEFGFQRG NVANQREHII LLLANADIRK RNDEEYDELK PSTVTELMDK
TFKSYYSWCK YLHSTSNLKF PDDCDKQQLQ LIYISLYLLI WGEASNVRFM PECICYIFHN
MANDVYGILF SNVEAVSGET YETEEVIDEE SFLRTVITPI YQVIRNEAKR NKGGTASHSQ
WRNYDDLNEY FWSKKCFKIG WPLDLKADFF LNSDEITPQD ERLNQVTYGK SKPKTNFVEV
RTFWNLFRDF DRMWIFLVMA FQAMVIVGWH GSGSLGDIFD KDVFKTVLTI FITSAYLTLL
QAALDIILNF NAWKNFKFSQ ILRYLLKFAV AFMWAVLLPI AYSKSVQRPT GVVKFFSTWT
GDWKDQSFYT YAVSFYVLPN ILAALLFLVP PFRRAMECSD MRPIKVIMWW AQPKLYVGRG
MHEDMFSLFK YTTFWIMLLI SKLAFNYYVE ILPLITPTKM IMNLHIGHYQ WHEFFPHATN
NIGVVIAIWA PIVLVYLMDT QIWYAIFSTL FGGIHGAFSH LGEIRTLGML RSRFESIPIA
FSRTLMPSED AKRKHADDYV DQKNITNFSQ VWNEFIYSMR SEDKISDRDR DLLLVPSSSG
DVSVIQWPPF LLASKIPIAV DMAKDFKGKE DAELFRKIKS DSYMYYAVIE SYETLKKIIY
ALLEDEADRR VMNQVFLEVD MSMQQQRFIY EFRMSGLPLL SDKLEKFLSI LLSDYEDQGT
YKSQLINVFQ DVIEIITQDL LVNGHEILER ARVHSPDIKN EKKEQRFEKI NIHLVRDRCW
REKVIRLHLL LSVKESAINV PQNLEARRRI TFFANSLFMN MPSAPRIRDM LSFSVLTPYY
KEDVLYSEED LNKENEDGIS ILFYLQKIYP DEWTNYLDRL KDPKLPEKDK SEFLREWVSY
RGQTLARTVR GMMYYRQALE LQCYQEVAGE QAEFSVFRAM ASNDENQKAF LERARALADL
KFTYVVSCQV YGNQKKSGDI HNRSCYTNIL QLMLKYPSLR VAYVDEREET ADAKSPKVFY
SVLLKGGDKF DEEIYRIKLP GPPAEIGEGK PENQNHAIIF TRGEALQTID MNQDNYFEEA
FKLRNVLEEF NKERVGRRKP TILGLREHIF TGSVSSLAWF MSNQESSFVT IGQRILANPL
RVRFHYGHPD IFDRIFHITR GGVSKASKVI NLSEDIFGGF NSTLRGGYVT HHEYIQVGKG
RDVGLNPISI FEAKVANGNG EQTLSRDVYR LGHRFDFYRM LSFYFTTIGF YFSSMLTVLT
VYAFLYGRMY MVMSGLEKEI LRLASPNQLE ALEQALATQS IFQLGFLMVL PMVMEIGLEH
GFRSAIVDFF IMQLQLASVF FTFQLGTKSH YYGRTILHGG SKYRPTGRGF VVFHAKFAEN
YRLYSRSHFV KGLELLLLLV VYQIYGHSYR SSNLYLYITV SMWFMVGSWL FAPFIFNPSG
FEWQKTVDDW TDWKRWLGDR GGIGIPVEKS WESWWNVEQE HLKHTSIRGR ILEITLALRF
FIYQYGIVYQ LNISQRSKSF LVYGLSWVVL LTSLLVLKMV SMGRRRFGTD FQLMFRILKA
LLFLGFLSVM TILFVVFKLT LTDLSASVLA FLPTGWAILL IGQVLRSPIK ALGVWDSVKE
LGRAYENIMG LVIFAPIAVL SWFPIVSEFQ ARLLFNQAFS RGLQISMILA GRKDKATSSH
K
