CALS4_ARATH
ID CALS4_ARATH Reviewed; 1871 AA.
AC Q9LTG5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Callose synthase 4;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 9;
GN Name=CALS4; Synonyms=GSL9; OrderedLocusNames=At5g36870; ORFNames=F5H8.14;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA98065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025605; BAA98065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94119.1; -; Genomic_DNA.
DR RefSeq; NP_198503.3; NM_123045.4.
DR AlphaFoldDB; Q9LTG5; -.
DR BioGRID; 18905; 1.
DR STRING; 3702.AT5G36870.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR PaxDb; Q9LTG5; -.
DR PRIDE; Q9LTG5; -.
DR EnsemblPlants; AT5G36870.1; AT5G36870.1; AT5G36870.
DR GeneID; 833654; -.
DR Gramene; AT5G36870.1; AT5G36870.1; AT5G36870.
DR KEGG; ath:AT5G36870; -.
DR Araport; AT5G36870; -.
DR TAIR; locus:2149089; AT5G36870.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; Q9LTG5; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9LTG5; -.
DR BioCyc; ARA:AT5G36870-MON; -.
DR PRO; PR:Q9LTG5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTG5; baseline and differential.
DR Genevisible; Q9LTG5; 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; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF48; PTHR12741:SF48; 2.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1871
FT /note="Callose synthase 4"
FT /id="PRO_0000334576"
FT TOPO_DOM 1..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..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..583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..1441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1442..1462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1463..1485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1486..1506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1507..1516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1517..1537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1538..1580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1581..1601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1602..1622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1623..1675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1676..1696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1697..1708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1709..1729
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1730..1741
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1742..1762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1763..1772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1773..1793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1794..1815
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1816..1836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1837..1871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1871 AA; 216138 MW; 3BDD16A01AD5DA44 CRC64;
MNQPNRGQIL QTVFSHFFPV ASPDSELVPS SLHEDITPIL RVAKDVEDTN PRSLFLQDLD
IKSVDDSINI LSGHSHALDK ANELDPTSSG RDVRQFKNTI LQWLEKNNES TLKARQKSSD
AHEMQSFYQQ YGDEGINDLL NAGAGSSSSQ RTKIYQTAVV LYDVLDAVHR KANIKVAAKI
LESHAEVEAK NKIYVPYNIL PLDPDSKNHA MMRDPKIVAV LKAIRYTSDL TWQIGHKIND
DEDVLDWLKT MFRFQKDNVS NQREHLILLL ANVQMRQTQR QPNLLDDRAL DTVMEKLLGN
YNKWCNHVGL ESSLRFPKDK QQKVVQQRKL LYTGLYLLIW GEAANLRFMP ECLCYIYHHM
AFELFEMLES KGSKKKYKPK NPTYSGKDED FLTKVVTPVY KTIAEEAKKS GEGKHSEWRN
YDDLNEYFWS KQYLDKLGWP MKANADFFCK TSQQLGLNKS EKKPDLGDGC VGKVNFVEIR
TFWHLFRSFD RMWSFYILSL QAMIIIAWNE TSESGGAVFH KVLSVFITAA KLNLFQAFLD
IALSWKARHS MSTHVRQRYI FKAVAAAVWV LLMPLTYAYS HTSIFIVAIL IYLSPNMLPE
MLLLIPSIRR TLEKSDFRPV KLIMWWSQPE LYIGRGMHES AWSIYKYMMF WIVLLTSKLA
FSYYVEQIKP LMGPTKEIMS VPMPGYWLPE FFPHVKNNRG VVITLWSPVI LVYFMDTQIW
YAIVSTLVGG LYGAFRHIGE IQTLGMLRSR FQSLPGAFNA CLIPNENTKE KGIKLAFSRK
CHKIPNTNGK EAKQFSQMWN TIINSFREED LISNRELELL LMSCWAYPDL DFIRWPIFLL
ASKIPIAVDI AKKRNGKHRE LKNILAEDNC MSCAVRECYA SIKKLLNTLV TGNSDLMLIT
TVFTIIDTHI EKDTLLTELN LSVLPDLHGH FVKLTEYVLQ NKDKDKIQIV NVLLKILEMV
TKDILKEEIK RLHLLLTVKE SAMDVPSNLE ARRRLTFFSN SLFMEMPGAP KIQNMLSFSA
LTPYYSEDVL FSTFDLEKEN DGVSILFYLQ KIFPDEWKNF LERVKCGTEE ELDAIDYLKE
EIRLWASYRG QTLTKTVRGM MYYQKALELQ AFFDLANERE LMKGYKSAEA SSSGSSLWAE
CQALADIKFT YVVACQQYSI HKRSGDQRAK DILTLMTTYP SLRVAYIDEV EQTHIYSKGT
SENFYYSALV KAAPQTYSTD SSDSGHMLDQ VIYQIKLPGP PIIGEGKPEN QNNAIIFTRG
EALQTIDMNQ DYYIEEAFKM RNLLQEFLEK NGGVRYPTIL GLREHIFTRS VSCLAWFMSN
QEHSFVTIGQ RVLANPLKVR FHYGHPDVFD RVFHLTRGGV SKASKVINLS EDIFAGFNST
LREGTVSHHE YIQVGKGRDV GLNQISMFEA KIANGSGEQT LSRDLYRLGH QFDFFRMLSC
YFTTVGFYFC SMLTVLTVYV FLYGRLYLVL SGVEKELGNK PMMMEIILAS QSFVQIVFLM
AMPMIMEIGL ERGFYDALFD FVLMQLQLAS VFFTFQLGTK FHYYCKTLLH GGAEYRGTGR
GFVVFHAKFA ENYRFYSRSH FVKATELGIL LLVYHIFGPT YIGLFTISIW FMVGTWLFAP
FLFNPSGFEW HEIVEDWADW KKWIEYDNGG IGVPPEKSWE SWWEKDIEHL QHSGKWGIVV
EIFFALRFFI FQYGLVYQLS AFKNKYSSLW VFGASWLLIL ILLLTVTVLD YARRRLGTEF
QLLFRIIKVS LFLAFMAIFI TLMTCRLILP QDVFLCMLAL IPTGWGLLLI AQSCKPLIQQ
PGIWSWVMTL AWVYDLVMGS LLFIPIAFMA WFPFISEFQT RMLFNQAFSR GLHISRILSG
QRKHRSSKNK D
