CALSA_ARATH
ID CALSA_ARATH Reviewed; 1904 AA.
AC Q9SJM0; C8C9X2; Q0WN58;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 5.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Callose synthase 10;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein CHORUS;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 8;
GN Name=CALS10; Synonyms=GSL8; OrderedLocusNames=At2g36850; ORFNames=T1J8.3;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20430748; DOI=10.1242/dev.049197;
RA Guseman J.M., Lee J.S., Bogenschutz N.L., Peterson K.M., Virata R.E.,
RA Xie B., Kanaoka M.M., Hong Z., Torii K.U.;
RT "Dysregulation of cell-to-cell connectivity and stomatal patterning by
RT loss-of-function mutation in Arabidopsis CHORUS (GLUCAN SYNTHASE-LIKE 8).";
RL Development 137:1731-1741(2010).
RN [2]
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 [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 1830-1904.
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 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 [6]
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).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18315544; DOI=10.1111/j.1365-313x.2008.03462.x;
RA Toeller A., Brownfield L., Neu C., Twell D., Schulze-Lefert P.;
RT "Dual function of Arabidopsis glucan synthase-like genes GSL8 and GSL10 in
RT male gametophyte development and plant growth.";
RL Plant J. 54:911-923(2008).
CC -!- FUNCTION: Involved in sporophytic and gametophytic development.
CC Required for normal plant development and for the proper accumulation
CC of callose at cell plates, cll walls and plasmodesmata. During pollen
CC formation, required for the entry of microspores into mitosis. During
CC plant growth and development, callose is found as a transitory
CC component of the cell plate in dividing cells, is a major component of
CC pollen mother cell walls and pollen tubes, and is found as a structural
CC component of plasmodesmatal canals. Required for proper cell division
CC and tissue patterning throughout plant organs, including stomatal
CC patterning. {ECO:0000269|PubMed:18315544, ECO:0000269|PubMed:20430748}.
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 -!- DEVELOPMENTAL STAGE: Expressed throughout pollen development with a at
CC mature pollen stage. {ECO:0000269|PubMed:18315544}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethality with severe dwarfism. Plants
CC develop collapsed and inviable pollen grains.
CC {ECO:0000269|PubMed:18315544, ECO:0000269|PubMed:20430748}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GQ373182; ACV04899.1; -; mRNA.
DR EMBL; AC006922; AAD31571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09306.1; -; Genomic_DNA.
DR EMBL; AK229594; BAF01442.1; -; mRNA.
DR PIR; E84785; E84785.
DR RefSeq; NP_850271.5; NM_179940.6.
DR AlphaFoldDB; Q9SJM0; -.
DR BioGRID; 3602; 2.
DR STRING; 3702.AT2G36850.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR iPTMnet; Q9SJM0; -.
DR SwissPalm; Q9SJM0; -.
DR PaxDb; Q9SJM0; -.
DR PRIDE; Q9SJM0; -.
DR ProteomicsDB; 240543; -.
DR EnsemblPlants; AT2G36850.1; AT2G36850.1; AT2G36850.
DR GeneID; 818258; -.
DR Gramene; AT2G36850.1; AT2G36850.1; AT2G36850.
DR KEGG; ath:AT2G36850; -.
DR Araport; AT2G36850; -.
DR TAIR; locus:2058001; AT2G36850.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_1_1_1; -.
DR InParanoid; Q9SJM0; -.
DR OMA; TIWNSIW; -.
DR OrthoDB; 48442at2759; -.
DR BioCyc; ARA:AT2G36850-MON; -.
DR PRO; PR:Q9SJM0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJM0; baseline and differential.
DR Genevisible; Q9SJM0; AT.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0048589; P:developmental growth; IMP:TAIR.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; Leucine-rich repeat; Membrane; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1904
FT /note="Callose synthase 10"
FT /id="PRO_0000334582"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1474..1494
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1529..1549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1554..1574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1621..1641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1644..1664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1747..1767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1783..1803
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1811..1831
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1853..1873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 100..132
FT /note="HAT 1"
FT REPEAT 678..701
FT /note="LRR 1"
FT REPEAT 751..774
FT /note="LRR 2"
FT REPEAT 925..948
FT /note="LRR 3"
FT REPEAT 1074..1107
FT /note="HAT 2"
FT REPEAT 1159..1181
FT /note="LRR 4"
FT REPEAT 1659..1691
FT /note="HAT 3"
FT CONFLICT 1830..1831
FT /note="TW -> YG (in Ref. 4; BAF01442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1904 AA; 218378 MW; 7FC337410084EFCF CRC64;
MARVYSNWDR LVRATLRREQ LRNTGQGHER VSSGLAGAVP PSLGRATNID AILQAADEIQ
SEDPSVARIL CEQAYSMAQN LDPNSDGRGV LQFKTGLMSV IKQKLAKRDG ASIDRDRDIE
RLWEFYKLYK RRHRVDDIQK EEQKWRESGT TFSSNVGEIL KMRKVFATLR ALIEVLEVLS
RDADPNGVGR SIRDELGRIK KADATLSAEL TPYNIVPLEA QSMTNAIGVF PEVRGAVQAI
RYTEHFPRLP VDFEISGQRD ADMFDLLEYI FGFQRDNVRN QREHLVLTLS NAQSQLSIPG
QNDPKIDENA VNEVFLKVLD NYIKWCKYLR IRVVYNKLEA IDRDRKLFLV SLYFLIWGEA
ANVRFLPECI CYIFHNMAKE LDAKLDHGEA VRADSCLTGT DTGSVSFLER IICPIYETIS
AETVRNNGGK AAHSEWRNYD DFNEYFWTPA CFELSWPMKT ESRFLSKPKG RKRTAKSSFV
EHRTYLHLFR SFIRLWIFMF IMFQSLTIIA FRNEHLNIET FKILLSAGPT YAIMNFIECL
LDVVLMYGAY SMARGMAISR LVIRFLWWGL GSAFVVYYYV KVLDERNKPN QNEFFFHLYI
LVLGCYAAVR LIFGLLVKLP ACHALSEMSD QSFFQFFKWI YQERYFVGRG LFENLSDYCR
YVAFWLVVLA SKFTFAYFLQ IKPLVKPTNT IIHLPPFQYS WHDIVSKSND HALTIVSLWA
PVLAIYLMDI HIWYTLLSAI IGGVMGAKAR LGEIRTIEMV HKRFESFPEA FAQNLVSPVV
KRVPLGQHAS QDGQDMNKAY AAMFSPFWNE IIKSLREEDY LSNREMDLLS IPSNTGSLRL
VQWPLFLLCS KILVAIDLAM ECKETQEVLW RQICDDEYMA YAVQECYYSV EKILNSMVND
EGRRWVERIF LEISNSIEQG SLAITLNLKK LQLVVSRFTA LTGLLIRNET PDLAKGAAKA
MFDFYEVVTH DLLSHDLREQ LDTWNILARA RNEGRLFSRI AWPRDPEIIE QVKRLHLLLT
VKDAAANVPK NLEARRRLEF FTNSLFMDMP QARPVAEMVP FSVFTPYYSE TVLYSSSELR
SENEDGISIL FYLQKIFPDE WENFLERIGR SESTGDADLQ ASSTDALELR FWVSYRGQTL
ARTVRGMMYY RRALMLQSFL ERRGLGVDDA SLTNMPRGFE SSIEARAQAD LKFTYVVSCQ
IYGQQKQQKK PEATDIGLLL QRYEALRVAF IHSEDVGNGD GGSGGKKEFY SKLVKADIHG
KDEEIYSIKL PGDPKLGEGK PENQNHAIVF TRGEAIQTID MNQDNYLEEA IKMRNLLEEF
HGKHGIRRPT ILGVREHVFT GSVSSLAWFM SNQETSFVTL GQRVLAYPLK VRMHYGHPDV
FDRIFHITRG GISKASRVIN ISEDIYAGFN STLRQGNITH HEYIQVGKGR DVGLNQIALF
EGKVAGGNGE QVLSRDVYRI GQLFDFFRMM SFYFTTVGFY VCTMMTVLTV YVFLYGRVYL
AFSGADRAIS RVAKLSGNTA LDAALNAQFL VQIGIFTAVP MVMGFILELG LLKAIFSFIT
MQFQLCSVFF TFSLGTRTHY FGRTILHGGA KYRATGRGFV VQHIKFADNY RLYSRSHFVK
AFEVALLLII YIAYGYTDGG ASSFVLLTIS SWFLVISWLF APYIFNPSGF EWQKTVEDFE
DWVSWLMYKG GVGVKGELSW ESWWEEEQAH IQTLRGRILE TILSLRFFMF QYGIVYKLDL
TRKNTSLALY GYSWVVLVVI VFLFKLFWYS PRKSSNILLA LRFLQGVASI TFIALIVVAI
AMTDLSIPDM FACVLGFIPT GWALLSLAIT WKQVLRVLGL WETVREFGRI YDAAMGMLIF
SPIALLSWFP FISTFQSRLL FNQAFSRGLE ISIILAGNRA NVET
