GenomeNet

Database: UniProt
Entry: CALSA_ARATH
LinkDB: CALSA_ARATH
Original site: 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   24-JAN-2024, entry version 129.
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=10.1105/tpc.13.4.755;
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9SJM0; -.
DR   CAZy; GT48; Glycosyltransferase Family 48.
DR   iPTMnet; Q9SJM0; -.
DR   SwissPalm; Q9SJM0; -.
DR   PaxDb; 3702-AT2G36850-1; -.
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; AT2G36850; GSL8.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_000742_1_1_1; -.
DR   InParanoid; Q9SJM0; -.
DR   OMA; ICENEVM; -.
DR   OrthoDB; 211713at2759; -.
DR   BioCyc; ARA:AT2G36850-MONOMER; -.
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: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: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   PANTHER; PTHR12741:SF67; CALLOSE SYNTHASE 10; 1.
DR   PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
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
//
DBGET integrated database retrieval system