CALS3_ARATH
ID CALS3_ARATH Reviewed; 1955 AA.
AC Q9LXT9; F4K2E8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Callose synthase 3;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 12;
GN Name=CALS3; Synonyms=GSL12; OrderedLocusNames=At5g13000;
GN ORFNames=T24H18.170;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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: Involved in callose synthesis at the forming cell plate
CC during cytokinesis. During plant growth and development, callose is
CC found as a transitory component of the cell plate in dividing cells, is
CC a major component of pollen mother cell walls and pollen tubes, and is
CC found as a structural component of plasmodesmatal canals (By
CC similarity). {ECO:0000250}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LXT9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88264.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353013; CAB88264.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91839.1; -; Genomic_DNA.
DR PIR; T49914; T49914.
DR RefSeq; NP_196804.6; NM_121303.8. [Q9LXT9-1]
DR AlphaFoldDB; Q9LXT9; -.
DR SMR; Q9LXT9; -.
DR STRING; 3702.AT5G13000.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9LXT9; -.
DR PaxDb; Q9LXT9; -.
DR PRIDE; Q9LXT9; -.
DR ProteomicsDB; 239092; -. [Q9LXT9-1]
DR EnsemblPlants; AT5G13000.1; AT5G13000.1; AT5G13000. [Q9LXT9-1]
DR GeneID; 831140; -.
DR Gramene; AT5G13000.1; AT5G13000.1; AT5G13000. [Q9LXT9-1]
DR KEGG; ath:AT5G13000; -.
DR Araport; AT5G13000; -.
DR TAIR; locus:2182335; AT5G13000.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; Q9LXT9; -.
DR OrthoDB; 48442at2759; -.
DR BioCyc; ARA:AT5G13000-MON; -.
DR PRO; PR:Q9LXT9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LXT9; baseline and differential.
DR Genevisible; Q9LXT9; 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; 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: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; IPR026953; CALS.
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 PANTHER; PTHR12741:SF48; PTHR12741:SF48; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1955
FT /note="Callose synthase 3"
FT /id="PRO_0000334575"
FT TOPO_DOM 1..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..558
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..604
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..1517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1518..1538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1539..1566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1567..1587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1588..1597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1598..1618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1619..1661
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1662..1682
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1683..1688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1689..1709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1710..1761
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1762..1782
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1783..1792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1793..1813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1814..1833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1834..1854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1855..1856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1857..1877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1878..1899
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1900..1920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1921..1955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1955 AA; 226184 MW; BE0E685D1F0EE13E CRC64;
MSATRGGPDQ GPSQPQQRRI IRTQTAGNLG ESFDSEVVPS SLVEIAPILR VANEVESSNP
RVAYLCRFYA FEKAHRLDPT SSGRGVRQFK TALLQRLERE HDPTLMGRVK KSDAREMQSF
YQHYYKKYIQ ALHNAADKAD RAQLTKAYQT ANVLFEVLKA VNLTQSIEVD REILEAQDKV
AEKTQLYVPY NILPLDPDSA NQAIMRYPEI QAAVLALRNT RGLPWPEGHK KKKDEDMLDW
LQEMFGFQKD NVANQREHLI LLLANVHIRQ FPKPDQQPKL DDQALTEVMK KLFKNYKKWC
KYLGRKSSLW LPTIQQEMQQ RKLLYMALYL LIWGEAANLR FMPECLCYIY HHMAFELYGM
LAGNVSPMTG ENVKPAYGGE EDAFLRKVVT PIYEVIQMEA QRSKKGKSKH SQWRNYDDLN
EYFWSVDCFR LGWPMRADAD FFCLPVAVPN TEKDGDNSKP IVARDRWVGK VNFVEIRSFW
HVFRSFDRMW SFYILCLQAM IIMAWDGGQP SSVFGADVFK KVLSVFITAA IMKLGQAVLD
VILNFKAHQS MTLHVKLRYI LKVFSAAAWV IILPVTYAYS WKDPPAFART IKSWFGSAMH
SPSLFIIAVV SYLSPNMLAG VMFLFPLLRR FLERSNYRIV MLMMWWSQPR LYVGRGMHES
AFSLFKYTMF WVLLIATKLA FSYYIEIRPL VAPTQAIMKA RVTNFQWHEF FPRAKNNIGV
VIALWAPIIL VYFMDSQIWY AIFSTLFGGI YGAFRRLGEI RTLGMLRSRF ESLPGAFNDR
LIPDGKNQQK KKGIRATLSH NFTEDKVPVN KEKEAARFAQ LWNTIISSFR EEDLISDREM
DLLLVPYWAD RDLDLIQWPP FLLASKIPIA LDMAKDSNGK DRELKKRIES DTYMKCAVRE
CYASFKNIIK FVVQGNREKE VIEIIFAEVD KHIDTGDLIQ EYKMSALPSL YDHFVKLIKY
LLDNKEEDRD HVVILFQDML EVVTRDIMME DYNISSLVDS SHGGTWHGGM IPLEQQYQLF
ASSGAIRFPI EPVTEAWKEK IKRIYLLLTT KESAMDVPSN LEARRRISFF SNSLFMDMPM
APKVRNMLSF SVLTPYYTEE VLFSLRDLET PNEDGVSILF YLQKIFPDEW NNFLERVKCL
SEEELKESDE LEEELRLWAS YRGQTLTRTV RGMMYYRKAL ELQAFLDMAM HEDLMEGYKA
VELNSENNSR GERSLWAQCQ AVADMKFTYV VSCQQYGIHK RSGDPRAQDI LRLMTRYPSL
RVAYIDEVEE PVKDKSKKGN QKVYYSVLVK VPKSTDHSTL AQNLDQVIYR IRLPGPAILG
EGKPENQNHA IIFSRGEGLQ TIDMNQDNYM EEALKMRNLL QEFLTKHDGV RHPSILGLRE
HIFTGSVSSL AWFMSNQETS FVTIGQRLLA NPLRVRFHYG HPDVFDRLFH LTRGGVSKAS
KVINLSEDIF AGFNSTLREG NVTHHEYIQV GKGRDVGLNQ ISMFEAKIAN GNGEQTLSRD
IYRLGHRFDF FRMMSCYFTT VGFYFSTLIT VLTVYIFLYG RLYLVLSGLE QGLSTQKGIR
DNTPLQIALA SQSFVQIGFL MALPMLMEIG LERGFRTALS EFVLMQLQLA PVFFTFSLGT
KTHYYGRTLL HGGAKYRSTG RGFVVFHAKF ADNYRLYSRS HFVKGLEMML LLVVYQIFGS
AYRGVLAYLL ITISMWFMVG TWLFAPFLFN PSGFEWQKIV DDWTDWNKWI NNIGGIGVPA
EKSWESWWEE EQEHLRYSGK RGIVVEILLA LRFFIYQYGL VYHLTITEKT KNFLVYGVSW
LVIFLILFVM KTVSVGRRRF SASFQLMFRL IKGLIFMTFI AIIVILITLA HMTIQDIIVC
ILAFMPTGWG MLLIAQACKP VVHRAGFWGS VRTLARGYEI VMGLLLFTPV AFLAWFPFVS
EFQTRMLFNQ AFSRGLQISR ILGGHRKDRS SRNKE
