CALS2_ARATH
ID CALS2_ARATH Reviewed; 1950 AA.
AC Q9SL03; F4IRV4; Q8GYW2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Callose synthase 2;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 3;
GN Name=CALS2; Synonyms=GSL3; OrderedLocusNames=At2g31960; ORFNames=F22D22.29;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 1204-1950.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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 -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC006223; AAD15408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08612.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08613.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61514.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61516.1; -; Genomic_DNA.
DR EMBL; AK117353; BAC42023.1; ALT_INIT; mRNA.
DR PIR; C84727; C84727.
DR RefSeq; NP_001189653.1; NM_001202724.2.
DR RefSeq; NP_001318331.1; NM_001336361.1.
DR RefSeq; NP_001323731.1; NM_001336363.1.
DR RefSeq; NP_850178.2; NM_179847.3.
DR AlphaFoldDB; Q9SL03; -.
DR SMR; Q9SL03; -.
DR STRING; 3702.AT2G31960.2; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9SL03; -.
DR PaxDb; Q9SL03; -.
DR PRIDE; Q9SL03; -.
DR ProteomicsDB; 239184; -.
DR EnsemblPlants; AT2G31960.1; AT2G31960.1; AT2G31960.
DR EnsemblPlants; AT2G31960.2; AT2G31960.2; AT2G31960.
DR EnsemblPlants; AT2G31960.3; AT2G31960.3; AT2G31960.
DR EnsemblPlants; AT2G31960.5; AT2G31960.5; AT2G31960.
DR GeneID; 817755; -.
DR Gramene; AT2G31960.1; AT2G31960.1; AT2G31960.
DR Gramene; AT2G31960.2; AT2G31960.2; AT2G31960.
DR Gramene; AT2G31960.3; AT2G31960.3; AT2G31960.
DR Gramene; AT2G31960.5; AT2G31960.5; AT2G31960.
DR KEGG; ath:AT2G31960; -.
DR Araport; AT2G31960; -.
DR TAIR; locus:2045452; AT2G31960.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; Q9SL03; -.
DR OrthoDB; 48442at2759; -.
DR BioCyc; ARA:AT2G31960-MON; -.
DR PRO; PR:Q9SL03; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL03; baseline and differential.
DR Genevisible; Q9SL03; 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: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:SF70; PTHR12741:SF70; 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 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..1950
FT /note="Callose synthase 2"
FT /id="PRO_0000334574"
FT TOPO_DOM 1..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..598
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..1511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1512..1532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1533..1560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1561..1581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1582..1591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1613..1655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1656..1676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1677..1682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1683..1703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1704..1755
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1756..1776
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1777..1787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1788..1808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1809..1827
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1828..1848
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1849..1851
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1852..1872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1873..1894
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1895..1915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1916..1950
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1950 AA; 226019 MW; 29E48783AF58EB26 CRC64;
MAQRKGPDPP PPQRRILRTQ TAGNLGEAML DSEVVPSSLV EIAPILRVAN EVEASNPRVA
YLCRFYAFEK AHRLDPTSSG RGVRQFKTAL LQRLERENET TLAGRQKSDA REMQSFYQHY
YKKYIQALQN AADKADRAQL TKAYQTAAVL FEVLKAVNQT EDVEVADEIL EAHTKVEEKS
QIYVPYNILP LDPDSQNQAI MRFPEIQATV SALRNTRGLP WPAGHKKKLD EDMLDWLQTM
FGFQKDNVSN QREHLILLLA NVHIRQFPRP EQQPRLDDRA LTIVMKKLFK NYKKWCKYLG
RKSSLWLPTI QQEVQQRKLL YMGLYLLIWG EAANLRFLPE CLCYIYHHMA FELYGMLAGS
VSPMTGEHVK PAYGGEDEAF LQKVVTPIYK TIAKEAKRSR GGKSKHSEWR NYDDLNEYFW
SIRCFRLGWP MRADADFFCQ TAEELRLDRS ENKPKTGDRW MGKVNFVEIR SFWHIFRSFD
RMWSFYILSL QAMIIIAWNG SGKLSGIFQG DVFLKVLSIF ITAAILKLAQ AVLDIALSWK
SRHSMSFHVK LRFIFKAVAA AIWVVLMPLT YAYSWKTPSG FAETIKNWFG GHQNSSPSFF
IIVILIYLSP NMLSTLLFAF PFIRRYLERS DYKIVMLMMW WSQPRLYIGR GMHESALSLF
KYTMFWVVLL ISKLAFSFYA EIKPLVKPTK DIMRVHISVY RWHEFFPHAK SNMGVVIALW
SPVILVYFMD TQIWYAIVST LVGGLNGAFR RLGEIRTLGM LRSRFQSLPE AFNACLVPNE
KSETPKKKGI MATFTRKFDQ VPSSKDKEAA RFAQMWNKII SSFREEDLIS DREMELLLVP
YWADRDLDLI RWPPFLLASK IPIALDMAKD SNGKDRELTK RLSVDSYMTC AVRECYASFK
NLINFLVVGE REGQVINEIF SRIDEHIEKE TLIKDLNLSA LPDLYGQFVR LIEYLMENRE
EDKDQIVIVL LNMLEVVTRD IMDEEVPSML ESTHNGTYVK YDVMTPLHQQ RKYFSQLRFP
VYSQTEAWKE KIKRLHLLLT VKESAMDVPS NLEARRRLTF FSNSLFMEMP DAPKIRNMLS
FSVLTPYYSE DVLFSIFGLE KQNEDGVSIL FYLQKIFPDE WTNFLERVKC GSEEELRARE
ELEEELRLWA SYRGQTLTKT VRGMMYYRKA LELQAFLDMA KDEELMKGYK ALELTSEDAS
KSGTSLWAQC QALADMKFTF VVSCQQYSVQ KRSGDQRAKD ILRLMTTYPS LRVAYIDEVE
QTHKESYKGA DEKIYYSALV KAAPQTKSMD SSESVQTLDQ VIYRIKLPGP AILGEGKPEN
QNHSIIFTRG EGLQTIDMNQ DNYMEEAFKM RNLLQEFLVK HGGVRTPTIL GLREHIFTGS
VSSLAWFMSN QENSFVTIGQ RVLASPLKVR FHYGHPDVFD RLFHLTRGGV CKASKVINLS
EDIFAGFNST LREGNVTHHE YIQVGKGRDV GLNQISMFEA KIANGNGEQT LSRDLYRLGH
RFDFFRMLSC YFTTIGFYFS TMLTVLTVYV FLYGRLYLVL SGLEEGLSNQ KAFRSNMPLQ
AALASQSFVQ IGFLMALPMM MEIGLERGFH NALIDFVLMQ LQLASVFFTF QLGTKTHYYG
RTLFHGGAEY RGTGRGFVVF HAKFAENYRF YSRSHFVKGI ELMILLLVYQ IFGHAYRGVV
TYILITVSIW FMVVTWLFAP FLFNPSGFEW QKIVDDWTDW NKWIYNRGGI GVPPEKSWES
WWEKEIGHLR HSGKRGIILE IVLALRFFIF QYGLVYQLST FKQENQSLWI YGASWFVILF
ILLIVKGLGV GRQRFSTNFQ LLFRIIKGFV FLTFLGLLIT FLALRFLTPK DIFLCMLAFM
PTGWGMLLIA QACKPLIQRL GFWSSVRTLA RGYEILMGLL LFTPVAFLAW FPFVSEFQTR
MLFNQAFSRG LQISRILGGQ RKDRSSKNKE
