CALS1_ARATH
ID CALS1_ARATH Reviewed; 1950 AA.
AC Q9AUE0; Q0WPU7; Q9LR43; Q9SYJ7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Callose synthase 1;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 6;
GN Name=CALS1; Synonyms=GSL6; OrderedLocusNames=At1g05570;
GN ORFNames=F3F20.1, T25N20.22;
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 [MRNA], SUBCELLULAR LOCATION, GENE FAMILY,
RP NOMENCLATURE, AND INTERACTION WITH UGT1 AND PHRAGMOPLASTIN.
RC STRAIN=cv. Columbia; TISSUE=Shoot meristem;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1202-1950.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBUNIT, AND INTERACTION WITH UGT1.
RX PubMed=11283335; DOI=10.2307/3871339;
RA Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
RT "A novel UDP-glucose transferase is part of the callose synthase complex
RT and interacts with phragmoplastin at the forming cell plate.";
RL Plant Cell 13:769-779(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11785931; DOI=10.1023/a:1013679111111;
RA Verma D.P.S., Hong Z.;
RT "Plant callose synthase complexes.";
RL Plant Mol. Biol. 47:693-701(2001).
RN [7]
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 [8]
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. Not required for callose formation after wounding
CC or pathogen attack. 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.
CC {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 -!- ACTIVITY REGULATION: May be regulated by ROP1 through the interaction
CC with UGT1.
CC -!- SUBUNIT: Interacts with UGT1 and phragmoplastin. May form a functional
CC complex with UGT1, ROP1 and phragmoplastin.
CC {ECO:0000269|PubMed:11283334, ECO:0000269|PubMed:11283335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11283334,
CC ECO:0000269|PubMed:11785931}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11283334, ECO:0000269|PubMed:11785931}.
CC Note=Localized in the forming cell plate during cytokinesis.
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=Q9AUE0-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF237733; AAK37413.1; -; mRNA.
DR EMBL; AC005106; AAF79729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007153; AAD30609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27855.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60178.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60179.1; -; Genomic_DNA.
DR EMBL; AK228963; BAF00852.1; -; mRNA.
DR PIR; E86189; E86189.
DR RefSeq; NP_001322482.1; NM_001331555.1. [Q9AUE0-1]
DR RefSeq; NP_001322483.1; NM_001331556.1. [Q9AUE0-1]
DR RefSeq; NP_563743.2; NM_100436.5. [Q9AUE0-1]
DR AlphaFoldDB; Q9AUE0; -.
DR SMR; Q9AUE0; -.
DR BioGRID; 22301; 1.
DR IntAct; Q9AUE0; 2.
DR STRING; 3702.AT1G05570.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9AUE0; -.
DR PaxDb; Q9AUE0; -.
DR PRIDE; Q9AUE0; -.
DR ProteomicsDB; 239091; -. [Q9AUE0-1]
DR EnsemblPlants; AT1G05570.1; AT1G05570.1; AT1G05570. [Q9AUE0-1]
DR EnsemblPlants; AT1G05570.3; AT1G05570.3; AT1G05570. [Q9AUE0-1]
DR EnsemblPlants; AT1G05570.4; AT1G05570.4; AT1G05570. [Q9AUE0-1]
DR GeneID; 837059; -.
DR Gramene; AT1G05570.1; AT1G05570.1; AT1G05570. [Q9AUE0-1]
DR Gramene; AT1G05570.3; AT1G05570.3; AT1G05570. [Q9AUE0-1]
DR Gramene; AT1G05570.4; AT1G05570.4; AT1G05570. [Q9AUE0-1]
DR KEGG; ath:AT1G05570; -.
DR Araport; AT1G05570; -.
DR TAIR; locus:2031938; AT1G05570.
DR eggNOG; KOG0916; Eukaryota.
DR InParanoid; Q9AUE0; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9AUE0; -.
DR BioCyc; ARA:AT1G05570-MON; -.
DR PRO; PR:Q9AUE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9AUE0; baseline and differential.
DR Genevisible; Q9AUE0; AT.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
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: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: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:SF59; PTHR12741:SF59; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1950
FT /note="Callose synthase 1"
FT /id="PRO_0000334573"
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..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..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..1828
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1829..1849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1850..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"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 88
FT /note="T -> A (in Ref. 1; AAK37413)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="Q -> R (in Ref. 1; AAK37413)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="A -> S (in Ref. 1; AAK37413)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="L -> P (in Ref. 1; AAK37413)"
FT /evidence="ECO:0000305"
FT CONFLICT 1268..1270
FT /note="KGT -> EGA (in Ref. 1; AAK37413)"
FT /evidence="ECO:0000305"
FT CONFLICT 1396
FT /note="V -> A (in Ref. 4; BAF00852)"
FT /evidence="ECO:0000305"
FT CONFLICT 1653
FT /note="R -> H (in Ref. 4; BAF00852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1950 AA; 225761 MW; 25EA79B202BA7443 CRC64;
MAQRREPDPP PPQRRILRTQ TVGSLGEAML DSEVVPSSLV EIAPILRVAN EVEASNPRVA
YLCRFYAFEK AHRLDPTSSG RGVRQFKTAL LQRLERENET TLAGRQKSDA REMQSFYQHY
YKKYIQALLN AADKADRAQL TKAYQTAAVL FEVLKAVNQT EDVEVADEIL ETHNKVEEKT
QIYVPYNILP LDPDSQNQAI MRLPEIQAAV AALRNTRGLP WTAGHKKKLD EDILDWLQSM
FGFQKDNVLN QREHLILLLA NVHIRQFPKP DQQPKLDDRA LTIVMKKLFR NYKKWCKYLG
RKSSLWLPTI QQEVQQRKLL YMGLYLLIWG EAANLRFMPE CLCYIYHHMA FELYGMLAGS
VSPMTGEHVK PAYGGEDEAF LQKVVTPIYQ TISKEAKRSR GGKSKHSVWR NYDDLNEYFW
SIRCFRLGWP MRADADFFCQ TAEELRLERS EIKSNSGDRW MGKVNFVEIR SFWHIFRSFD
RLWSFYILCL QAMIVIAWNG SGELSAIFQG DVFLKVLSVF ITAAILKLAQ AVLDIALSWK
ARHSMSLYVK LRYVMKVGAA AVWVVVMAVT YAYSWKNASG FSQTIKNWFG GHSHNSPSLF
IVAILIYLSP NMLSALLFLF PFIRRYLERS DYKIMMLMMW WSQPRLYIGR GMHESALSLF
KYTMFWIVLL ISKLAFSYYA EIKPLVGPTK DIMRIHISVY SWHEFFPHAK NNLGVVIALW
SPVILVYFMD TQIWYAIVST LVGGLNGAFR RLGEIRTLGM LRSRFQSIPG AFNDCLVPQD
NSDDTKKKRF RATFSRKFDQ LPSSKDKEAA RFAQMWNKII SSFREEDLIS DREMELLLVP
YWSDPDLDLI RWPPFLLASK IPIALDMAKD SNGKDRELKK RLAVDSYMTC AVRECYASFK
NLINYLVVGE REGQVINDIF SKIDEHIEKE TLITELNLSA LPDLYGQFVR LIEYLLENRE
EDKDQIVIVL LNMLELVTRD IMEEEVPSLL ETAHNGSYVK YDVMTPLHQQ RKYFSQLRFP
VYSQTEAWKE KIKRLHLLLT VKESAMDVPS NLEARRRLTF FSNSLFMDMP PAPKIRNMLS
FSVLTPYFSE DVLFSIFGLE QQNEDGVSIL FYLQKIFPDE WTNFLERVKC GNEEELRARE
DLEEELRLWA SYRGQTLTKT VRGMMYYRKA LELQAFLDMA KDEELLKGYK ALELTSEEAS
KSGGSLWAQC QALADMKFTF VVSCQQYSIH KRSGDQRAKD ILRLMTTYPS IRVAYIDEVE
QTHKESYKGT EEKIYYSALV KAAPQTKPMD SSESVQTLDQ LIYRIKLPGP AILGEGKPEN
QNHAIIFTRG EGLQTIDMNQ DNYMEEAFKM RNLLQEFLEK HGGVRCPTIL GLREHIFTGS
VSSLAWFMSN QENSFVTIGQ RVLASPLKVR FHYGHPDIFD RLFHLTRGGI CKASKVINLS
EDIFAGFNST LREGNVTHHE YIQVGKGRDV GLNQISMFEA KIANGNGEQT LSRDLYRLGH
RFDFFRMLSC YFTTIGFYFS TMLTVLTVYV FLYGRLYLVL SGLEEGLSSQ RAFRNNKPLE
AALASQSFVQ IGFLMALPMM MEIGLERGFH NALIEFVLMQ LQLASVFFTF QLGTKTHYYG
RTLFHGGAEY RGTGRGFVVF HAKFAENYRF YSRSHFVKGI ELMILLLVYQ IFGQSYRGVV
TYILITVSIW FMVVTWLFAP FLFNPSGFEW QKIVDDWTDW NKWIYNRGGI GVPPEKSWES
WWEKELEHLR HSGVRGITLE IFLALRFFIF QYGLVYHLST FKGKNQSFWV YGASWFVILF
ILLIVKGLGV GRRRFSTNFQ LLFRIIKGLV FLTFVAILIT FLALPLITIK DLFICMLAFM
PTGWGMLLIA QACKPLIQQL GIWSSVRTLA RGYEIVMGLL LFTPVAFLAW FPFVSEFQTR
MLFNQAFSRG LQISRILGGQ RKDRSSKNKE
