CALS5_ARATH
ID CALS5_ARATH Reviewed; 1923 AA.
AC Q3B724; Q8S8D4; Q8S8G9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Callose synthase 5;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-glucan synthase;
DE AltName: Full=Protein GLUCAN SYNTHASE-LIKE 2;
DE AltName: Full=Protein LESS ADHERENT POLLEN 1;
GN Name=CALS5; Synonyms=GSL2, LAP1; OrderedLocusNames=At2g13680;
GN ORFNames=F13J11.3, T10F5.22;
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], FUNCTION, DEVELOPMENTAL STAGE, IDENTIFICATION,
RP MUTAGENESIS OF GLY-651, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16212660; DOI=10.1186/1471-2229-5-22;
RA Nishikawa S., Zinkl G.M., Swanson R.J., Maruyama D., Preuss D.;
RT "Callose (beta-1,3 glucan) is essential for Arabidopsis pollen wall
RT patterning, but not tube growth.";
RL BMC Plant Biol. 5:22-22(2005).
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 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 [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-651.
RX PubMed=15842618; DOI=10.1111/j.1365-313x.2005.02379.x;
RA Dong X., Hong Z., Sivaramakrishnan M., Mahfouz M., Verma D.P.S.;
RT "Callose synthase (CalS5) is required for exine formation during
RT microgametogenesis and for pollen viability in Arabidopsis.";
RL Plant J. 42:315-328(2005).
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).
CC -!- FUNCTION: Required for the formation of the callose wall separating the
CC tetraspores (interstitial wall) and surrounding the pollen mother cells
CC (peripheral wall). Required for exine formation on pollen wall. May be
CC involved in callose synthesis during pollen tube growth. During plant
CC growth and development, callose is found as a transitory component of
CC the cell plate in dividing cells, is a major component of pollen mother
CC cell walls and pollen tubes, and is found as a structural component of
CC plasmodesmatal canals. {ECO:0000269|PubMed:15842618,
CC ECO:0000269|PubMed:16212660}.
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, both in
CC pollen mother cells and in developing and mature pollen grains.
CC Expressed in growing pollen tube. {ECO:0000269|PubMed:15842618,
CC ECO:0000269|PubMed:16212660}.
CC -!- DISRUPTION PHENOTYPE: Plants develop deformed and inviable pollen
CC grains which do not have exin. {ECO:0000269|PubMed:16212660}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15250.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15369.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY337762; AAR00322.1; -; mRNA.
DR EMBL; AC006436; AAM15250.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007063; AAM15369.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06254.1; -; Genomic_DNA.
DR EMBL; BK001470; DAA01511.1; -; mRNA.
DR RefSeq; NP_849953.2; NM_179622.4.
DR AlphaFoldDB; Q3B724; -.
DR SMR; Q3B724; -.
DR STRING; 3702.AT2G13680.1; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR TCDB; 9.B.119.1.2; the glycan synthase, fks1 (fks1) family.
DR PaxDb; Q3B724; -.
DR PRIDE; Q3B724; -.
DR ProteomicsDB; 240314; -.
DR EnsemblPlants; AT2G13680.1; AT2G13680.1; AT2G13680.
DR GeneID; 815852; -.
DR Gramene; AT2G13680.1; AT2G13680.1; AT2G13680.
DR KEGG; ath:AT2G13680; -.
DR Araport; AT2G13680; -.
DR TAIR; locus:2040456; AT2G13680.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_0_0_1; -.
DR InParanoid; Q3B724; -.
DR OMA; HKELDDC; -.
DR OrthoDB; 48442at2759; -.
DR PhylomeDB; Q3B724; -.
DR BioCyc; ARA:AT2G13680-MON; -.
DR PRO; PR:Q3B724; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3B724; baseline and differential.
DR Genevisible; Q3B724; 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; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009556; P:microsporogenesis; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010208; P:pollen wall assembly; IMP:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:TAIR.
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 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1923
FT /note="Callose synthase 5"
FT /id="PRO_0000334577"
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..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..601
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 659..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 680..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..1486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1487..1507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1508..1535
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1536..1556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1557..1566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1567..1587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1588..1630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1631..1651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1652..1657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1658..1678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1679..1732
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1733..1755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1756..1766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1767..1787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1788..1803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1804..1824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1826..1846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1847..1873
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1874..1894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1895..1923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 651
FT /note="G->I: In cals5-4; loss of exine."
FT /evidence="ECO:0000269|PubMed:15842618,
FT ECO:0000269|PubMed:16212660"
SQ SEQUENCE 1923 AA; 220661 MW; BDB264C8530D418C CRC64;
MAQSSTSHDS GPQGLMRRPS RSAATTVSIE VFDHEVVPAS LGTIAPILRV AAEIEHERPR
VAYLCRFYAF EKAHRLDPSS GGRGVRQFKT LLFQRLERDN ASSLASRVKK TDGREVESFY
QQYYEHYVRA LDQGDQADRA QLGKAYQTAG VLFEVLMAVN KSEKVEAVAP EIIAAARDVQ
EKNEIYAPYN ILPLDSAGAS QSVMQLEEVK AAVAALGNTR GLNWPSGFEQ HRKKTGNLDL
LDWLRAMFGF QRDNVRNQRE HLVCLFADNH IRLTPKPEPL NKLDDRAVDT VMSKLFKNYK
NWCKFLGRKH SLRLPQAAQD IQQRKILYMG LYLLIWGEAA NIRFMPECLC YIFHNMAYEL
HGLLAGNVSI VTGENIKPSY GGDDEAFLRK VITPIYRVVQ TEANKNANGK AAHSDWSNYD
DLNEYFWTPD CFSLGWPMRD DGDLFKSTRD TTQGKKGSFR KAGRTGKSNF TETRTFWHIY
HSFDRLWTFY LLALQAMIIL AFERVELREI LRKDVLYALS SIFITAAFLR FLQSVLDVIL
NFPGFHRWKF TDVLRNILKI VVSLAWCVVL PLCYAQSVSF APGKLKQWLS FLPQVKGVPP
LYIMAVALYL LPNVLAAIMF IFPMLRRWIE NSDWHIFRLL LWWSQPRIYV GRGMHESQIA
LIKYTIFWLL LFCCKFAFSY FLQVKLLVKP TNAIMSIRHV KYKWHEFFPN AEHNYGAVVS
LWLPVILVYF MDTQIWYAIF STICGGVIGA FDRLGEIRTL GMLRSRFQSL PGAFNTYLVP
SDKTRRRGFS LSKRFAEVTA ARRTEAAKFS QLWNEIISSF REEDLISDRE MDLLLVPYTS
DPSLKLIQWP PFLLASKIPI ALDMAAQFRT RDSDLWKRIC ADEYMKCAVI ECYESFKHVL
HTLVIGENEK RIIGIIIKEV ESNISKNSFL SNFRMAPLPA LCSKFVELVG ILKNADPAKR
DTVVLLLQDM LEVVTRDMMQ NENRELVELG HTNKESGRQL FAGTDAKPAI LFPPVATAQW
HEQISRLHLL LTVKESAMDV PTNLEAQRRI AFFTNSLFMD MPRAPRVRNM LSFSVLTPYY
SEETVYSKND LEMENEDGVS VVYYLQKIFP DEWTNFLERL DCKDETSVLE SEENILQLRH
WVSLRGQTLF RTVRGMMYYR RALKLQAFLD MANETEILAG YKAISEPTEE DKKSQRSLYT
QLEAVADLKF TYVATCQNYG NQKRSGDRRA TDILNLMVNN PSLRVAYIDE VEEREGGKVQ
KVFYSVLIKA VDNLDQEIYR IKLPGPAKIG EGKPENQNHA LIFTRGEALQ AIDMNQDHYL
EEALKMRNLL EEFNEDHGVR APTILGFREH IFTGSVSSLA WFMSNQETSF VTIGQRVLAS
PLKVRFHYGH PDVFDRIFHI TRGGISKASR GINLSEDIFA GFNSTLRRGN VTHHEYIQVG
KGRDVGLNQI SLFEAKVACG NGEQTLSRDL YRLGHRFDFF RMMSCYFTTV GFYISSMIVV
LTVYAFLYGR LYLSLSGVEE AIVKFAAAKG DSSLKAAMAS QSVVQLGLLM TLPMVMEIGL
ERGFRTALSD LIIMQLQLAP VFFTFSLGTK VHYYGRTILH GGSKYRATGR GFVVKHEKFA
ENYRMYSRSH FVKGMELMVL LICYRIYGKA AEDSVGYALV MGSTWFLVGS WLFAPFFFNP
SGFEWQKIVD DWDDWNKWIS SRGGIGVPAN KSWESWWEEE QEHLLHSGFF GKFWEIFLSL
RYFIYQYGIV YQLNLTKESR MGKQHSIIVY GLSWLVIVAV MIVLKIVSMG RKKFSADFQL
MFRLLKLFLF IGSVVIVGML FHFLKLTVGD IMQSLLAFLP TGWALLQISQ VARPLMKTVG
MWGSVKALAR GYEYIMGVVI FMPVTVLAWF PFVSEFQTRL LFNQAFSRGL QIQRILAGGK
KQK
