CALS8_ARATH
ID CALS8_ARATH Reviewed; 1976 AA.
AC Q9LUD7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Putative callose synthase 8;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 4;
GN Name=CALS8; Synonyms=GSL4; OrderedLocusNames=At3g14570; ORFNames=MIE1.7;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 -!- 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=Q9LUD7-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02389.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB023038; BAB02389.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75539.1; -; Genomic_DNA.
DR RefSeq; NP_188075.2; NM_112317.3. [Q9LUD7-1]
DR AlphaFoldDB; Q9LUD7; -.
DR STRING; 3702.AT3G14570.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR TCDB; 9.B.119.1.3; the glycan synthase, fks1 (fks1) family.
DR PaxDb; Q9LUD7; -.
DR PRIDE; Q9LUD7; -.
DR EnsemblPlants; AT3G14570.1; AT3G14570.1; AT3G14570. [Q9LUD7-1]
DR GeneID; 820683; -.
DR Gramene; AT3G14570.1; AT3G14570.1; AT3G14570. [Q9LUD7-1]
DR KEGG; ath:AT3G14570; -.
DR Araport; AT3G14570; -.
DR TAIR; locus:2089571; AT3G14570.
DR eggNOG; KOG0916; Eukaryota.
DR InParanoid; Q9LUD7; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q9LUD7; -.
DR BioCyc; ARA:AT3G14570-MON; -.
DR PRO; PR:Q9LUD7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUD7; baseline and differential.
DR Genevisible; Q9LUD7; 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; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
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..1976
FT /note="Putative callose synthase 8"
FT /id="PRO_0000334580"
FT TOPO_DOM 1..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..648
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..1544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1545..1565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1566..1595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1596..1616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1617..1620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1621..1641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1642..1688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1689..1709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1710..1715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1716..1736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1737..1790
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1791..1811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1812..1819
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1820..1840
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1841..1856
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1857..1877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1878..1884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1885..1905
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1906..1928
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1929..1949
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1950..1976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 1676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1976 AA; 228484 MW; 2DEDE6CE91425957 CRC64;
MSHEIVPVDP IDVPSTSYSR PILGPREDSP ERATEFTRSL TFREHVSSEP FDSERLPATL
ASEIQRFLRI ANLVESEEPR IAYLCRFHAF EIAHHMDRNS TGRGVRQFKT SLLQRLELDE
EFTVRRRKEK SDVRELKRVY HAYKEYIIRH GAAFNLDNSQ REKLINARRI ASVLYEVLKT
VTSGAGPQAI ADRESIRAKS EFYVPYNILP LDKGGVHQAI MHLPEIKAAV AIVRNTRGLP
PPEEFQRHQP FLDLFEFLQY AFGFQNGNVA NQREHLILLL SNTIIRQPQK QSSAPKSGDE
AVDALMKKFF KNYTNWCKFL GRKNNIRLPY VKQEALQYKT LYIGLYLLIW GEASNLRFMP
ECLCYIFHHM AYELHGVLTG AVSMITGEKV APAYGGGHES FLADVVTPIY MVVQKEAEKN
KNGTADHSMW RNYDDLNEFF WSLECFEIGW PMRPEHDFFC VESSETSKPG RWRGMLRFRK
QTKKTDEEIE DDEELGVLSE EQPKPTSRWL GKTNFVETRS FWQIFRSFDR MWSFFVLSLQ
ALIIMACHDV GSPLQVFNAN IFEDVMSIFI TSAILKLIKG ILDIIFKWKA RNTMPINEKK
KRLVKLGFAA MWTIILPVLY SHSRRKYICY FTNYKTWLGE WCFSPYMVAV TIYLTGSAIE
LVLFFVPAIS KYIETSNHGI FKTLSWWGQP RLYVGRGMQE TQVSQFKYTF FWILVLLTKF
AFSYAFEIKP LIEPTRLIMK VGVRNYEWHE IFPEVKSNAA AIVAVWAPIM VVYFMDTQIW
YSVYCTIFGG LYGVLHHLGE IRTLGMLRGR FHTLPSAFNA SLIPHSTKDE KRRKQRGFFP
FNLGRGSDGQ KNSMAKFVLV WNQVINSFRT EDLISNKELD LMTMPLSSEV LSGIIRWPIF
LLANKFSTAL SIAKDFVGKD EVLYRRIRKD EYMYYAVKEC YESLKYILQI LVVGDLEKKI
ISGIINEIEE SIRQSSLLEE FKMAELPALH DKCIELVQLL VEGSAEQLQV EKSEELHGKL
VKALQDIFEL VTNDMMVHGD RILDLLQSRE GSGEDTGIFM RVIEPQLFES YGEWRCIHFP
LPDSASLSEQ IQRFLLLLTV KDSAMDIPEN LDARRRLSFF ATSLFMDMPD APKVRNMMSF
SVLTPHYQED INYSTNELHS TKSSVSIIFY MQKIFPDEWK NFLERMGCDN LDALKKEGKE
EELRNWASFR GQTLSRTVRG MMYCREALKL QAFLDMADDE DILEGYKDVE RSNRPLAAQL
DALADMKFTY VVSCQMFGAQ KSSGDPHAQD ILDLMIKYPS LRVAYVEERE EIVLDVPKKV
YYSILVKAVN GFDQEIYRVK LPGPPNIGEG KPENQNHAIV FTRGEALQTI DMNQDHYLEE
AFKMRNLLQE FLRNRGRRPP TILGLREHIF TGSVSSLAWF MSYQETSFVT IGQRLLANPL
RVRFHYGHPD VFDRIFHITR GGISKSSRTI NLSEDVFAGY NTTLRRGCIT YNEYLQVGKG
RDVGLNQISK FEAKVANGNS EQTISRDIYR LGQRFDFFRM LSCYFTTIGF YFSSLISVIG
IYIYLYGQLY LVLSGLQKTL ILEAKVKNIK SLETALASQS FIQLGLLTGL PMVMEIGLEK
GFLIAFQDFI LMQLQLAAFF FTFSLGTKTH YFGRTILHGG AKYRPTGRKV VVFHANFSEN
YRLYSRSHFI KGFELMILLV VYELFKHTSQ SNMAYSFITF SVWFMSFTWL CAPFLFNPSG
FTWEIIVGDW RDWNRWIKEQ GGIGIQQDKS WQSWWNDEQA HLRGSGVGAR CLEIILSLRF
FVYQYGLVYH LDITQSNTNI IVYALSWVVI LATFFTVKAV DLGRQLFSTR KHLVFRFFKV
FVFVSILTII ITLANICHLS VKDLLVSCLA FLPTGWGLIL IAQAVRPKIE GTSLWEFTQV
LARAYDYGMG VVLFAPMAIL AWLPIISAFQ TRFLFNEAFN RRLQIQPILA GKKKNR
