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Reviewed, UniProtKB/Swiss-Prot Q9AUE0 (CALS1_ARATH)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Callose synthase 1
    EC=2.4.1.34
Alternative name(s):
    1,3-beta-glucan synthase
    Protein GLUCAN SYNTHASE-LIKE 6
Gene names
Name: CALS1
Synonyms: GSL6
Ordered Locus Names: At1g05570
ORF Names: F3F20.1, T25N20.22
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length1950 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in callose synthesis at the forming cell plate during cytokinesis. Not required for callose formation after wounding or pathogen attack. During plant growth and development, callose is found as a transitory component of the cell plate in dividing cells, is a major component of pollen mother cell walls and pollen tubes, and is found as a structural component of plasmodesmatal canals. Ref.6

Catalytic activity

UDP-glucose + ((1->3)-beta-D-glucosyl)(n) = UDP + ((1->3)-beta-D-glucosyl)(n+1).

Enzyme regulation

May be regulated by ROP1 through the interaction with UGT1.

Subunit structure

Interacts with UGT1 and phragmoplastin. May form a functional complex with UGT1, ROP1 and phragmoplastin. Ref.1 Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Localized in the forming cell plate during cytokinesis. Ref.1 Ref.5

Sequence similarities

Belongs to the glycosyltransferase 48 family.

Sequence caution

The sequence AAD30609.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF79729.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19501950Callose synthase 1
PRO_0000334573

Regions

Topological domain1 – 481481Cytoplasmic Potential
Transmembrane482 – 50221 Potential
Topological domain503 – 5053Extracellular Potential
Transmembrane506 – 52621 Potential
Topological domain527 – 55226Cytoplasmic Potential
Transmembrane553 – 57321 Potential
Topological domain574 – 59926Extracellular Potential
Transmembrane600 – 62021 Potential
Topological domain621 – 65535Cytoplasmic Potential
Transmembrane656 – 67621 Potential
Topological domain677 – 71236Extracellular Potential
Transmembrane713 – 73321 Potential
Topological domain734 – 1511778Cytoplasmic Potential
Transmembrane1512 – 153221 Potential
Topological domain1533 – 156028Extracellular Potential
Transmembrane1561 – 158121 Potential
Topological domain1582 – 159110Cytoplasmic Potential
Transmembrane1592 – 161221 Potential
Topological domain1613 – 165543Extracellular Potential
Transmembrane1656 – 167621 Potential
Topological domain1677 – 16826Cytoplasmic Potential
Transmembrane1683 – 170321 Potential
Topological domain1704 – 175552Extracellular Potential
Transmembrane1756 – 177621 Potential
Topological domain1777 – 178711Cytoplasmic Potential
Transmembrane1788 – 180821 Potential
Topological domain1809 – 182820Extracellular Potential
Transmembrane1829 – 184921 Potential
Topological domain1850 – 18512Cytoplasmic Potential
Transmembrane1852 – 187221 Potential
Topological domain1873 – 189422Extracellular Potential
Transmembrane1895 – 191521 Potential
Topological domain1916 – 195035Cytoplasmic Potential
Compositional bias7 – 126Poly-Pro

Amino acid modifications

Glycosylation5771N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict881T → A in AAK37413. Ref.1
Sequence conflict1261Q → R in AAK37413. Ref.1
Sequence conflict5601A → S in AAK37413. Ref.1
Sequence conflict7251L → P in AAK37413. Ref.1
Sequence conflict1268 – 12703KGT → EGA in AAK37413. Ref.1
Sequence conflict13961V → A in BAF00852. Ref.3
Sequence conflict16531R → H in BAF00852. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9AUE0-1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 25EA79B202BA7443

FASTA1,950225,761
        10         20         30         40         50         60 
MAQRREPDPP PPQRRILRTQ TVGSLGEAML DSEVVPSSLV EIAPILRVAN EVEASNPRVA 

        70         80         90        100        110        120 
YLCRFYAFEK AHRLDPTSSG RGVRQFKTAL LQRLERENET TLAGRQKSDA REMQSFYQHY 

       130        140        150        160        170        180 
YKKYIQALLN AADKADRAQL TKAYQTAAVL FEVLKAVNQT EDVEVADEIL ETHNKVEEKT 

       190        200        210        220        230        240 
QIYVPYNILP LDPDSQNQAI MRLPEIQAAV AALRNTRGLP WTAGHKKKLD EDILDWLQSM 

       250        260        270        280        290        300 
FGFQKDNVLN QREHLILLLA NVHIRQFPKP DQQPKLDDRA LTIVMKKLFR NYKKWCKYLG 

       310        320        330        340        350        360 
RKSSLWLPTI QQEVQQRKLL YMGLYLLIWG EAANLRFMPE CLCYIYHHMA FELYGMLAGS 

       370        380        390        400        410        420 
VSPMTGEHVK PAYGGEDEAF LQKVVTPIYQ TISKEAKRSR GGKSKHSVWR NYDDLNEYFW 

       430        440        450        460        470        480 
SIRCFRLGWP MRADADFFCQ TAEELRLERS EIKSNSGDRW MGKVNFVEIR SFWHIFRSFD 

       490        500        510        520        530        540 
RLWSFYILCL QAMIVIAWNG SGELSAIFQG DVFLKVLSVF ITAAILKLAQ AVLDIALSWK 

       550        560        570        580        590        600 
ARHSMSLYVK LRYVMKVGAA AVWVVVMAVT YAYSWKNASG FSQTIKNWFG GHSHNSPSLF 

       610        620        630        640        650        660 
IVAILIYLSP NMLSALLFLF PFIRRYLERS DYKIMMLMMW WSQPRLYIGR GMHESALSLF 

       670        680        690        700        710        720 
KYTMFWIVLL ISKLAFSYYA EIKPLVGPTK DIMRIHISVY SWHEFFPHAK NNLGVVIALW 

       730        740        750        760        770        780 
SPVILVYFMD TQIWYAIVST LVGGLNGAFR RLGEIRTLGM LRSRFQSIPG AFNDCLVPQD 

       790        800        810        820        830        840 
NSDDTKKKRF RATFSRKFDQ LPSSKDKEAA RFAQMWNKII SSFREEDLIS DREMELLLVP 

       850        860        870        880        890        900 
YWSDPDLDLI RWPPFLLASK IPIALDMAKD SNGKDRELKK RLAVDSYMTC AVRECYASFK 

       910        920        930        940        950        960 
NLINYLVVGE REGQVINDIF SKIDEHIEKE TLITELNLSA LPDLYGQFVR LIEYLLENRE 

       970        980        990       1000       1010       1020 
EDKDQIVIVL LNMLELVTRD IMEEEVPSLL ETAHNGSYVK YDVMTPLHQQ RKYFSQLRFP 

      1030       1040       1050       1060       1070       1080 
VYSQTEAWKE KIKRLHLLLT VKESAMDVPS NLEARRRLTF FSNSLFMDMP PAPKIRNMLS 

      1090       1100       1110       1120       1130       1140 
FSVLTPYFSE DVLFSIFGLE QQNEDGVSIL FYLQKIFPDE WTNFLERVKC GNEEELRARE 

      1150       1160       1170       1180       1190       1200 
DLEEELRLWA SYRGQTLTKT VRGMMYYRKA LELQAFLDMA KDEELLKGYK ALELTSEEAS 

      1210       1220       1230       1240       1250       1260 
KSGGSLWAQC QALADMKFTF VVSCQQYSIH KRSGDQRAKD ILRLMTTYPS IRVAYIDEVE 

      1270       1280       1290       1300       1310       1320 
QTHKESYKGT EEKIYYSALV KAAPQTKPMD SSESVQTLDQ LIYRIKLPGP AILGEGKPEN 

      1330       1340       1350       1360       1370       1380 
QNHAIIFTRG EGLQTIDMNQ DNYMEEAFKM RNLLQEFLEK HGGVRCPTIL GLREHIFTGS 

      1390       1400       1410       1420       1430       1440 
VSSLAWFMSN QENSFVTIGQ RVLASPLKVR FHYGHPDIFD RLFHLTRGGI CKASKVINLS 

      1450       1460       1470       1480       1490       1500 
EDIFAGFNST LREGNVTHHE YIQVGKGRDV GLNQISMFEA KIANGNGEQT LSRDLYRLGH 

      1510       1520       1530       1540       1550       1560 
RFDFFRMLSC YFTTIGFYFS TMLTVLTVYV FLYGRLYLVL SGLEEGLSSQ RAFRNNKPLE 

      1570       1580       1590       1600       1610       1620 
AALASQSFVQ IGFLMALPMM MEIGLERGFH NALIEFVLMQ LQLASVFFTF QLGTKTHYYG 

      1630       1640       1650       1660       1670       1680 
RTLFHGGAEY RGTGRGFVVF HAKFAENYRF YSRSHFVKGI ELMILLLVYQ IFGQSYRGVV 

      1690       1700       1710       1720       1730       1740 
TYILITVSIW FMVVTWLFAP FLFNPSGFEW QKIVDDWTDW NKWIYNRGGI GVPPEKSWES 

      1750       1760       1770       1780       1790       1800 
WWEKELEHLR HSGVRGITLE IFLALRFFIF QYGLVYHLST FKGKNQSFWV YGASWFVILF 

      1810       1820       1830       1840       1850       1860 
ILLIVKGLGV GRRRFSTNFQ LLFRIIKGLV FLTFVAILIT FLALPLITIK DLFICMLAFM 

      1870       1880       1890       1900       1910       1920 
PTGWGMLLIA QACKPLIQQL GIWSSVRTLA RGYEIVMGLL LFTPVAFLAW FPFVSEFQTR 

      1930       1940       1950 
MLFNQAFSRG LQISRILGGQ RKDRSSKNKE 

« Hide

References

« Hide 'large scale' references
[1]"A cell plate-specific callose synthase and its interaction with phragmoplastin."
Hong Z., Delauney A.J., Verma D.P.S.
Plant Cell 13:755-768(2001) [PubMed: 11283334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE, INTERACTION WITH UGT1 AND PHRAGMOPLASTIN.
Strain: cv. Columbia.
Tissue: Shoot meristem.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1202-1950.
Strain: cv. Columbia.
[4]"A novel UDP-glucose transferase is part of the callose synthase complex and interacts with phragmoplastin at the forming cell plate."
Hong Z., Zhang Z., Olson J.M., Verma D.P.S.
Plant Cell 13:769-779(2001) [PubMed: 11283335] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH UGT1.
[5]"Plant callose synthase complexes."
Verma D.P.S., Hong Z.
Plant Mol. Biol. 47:693-701(2001) [PubMed: 11785931] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"An Arabidopsis callose synthase, GSL5, is required for wound and papillary callose formation."
Jacobs A.K., Lipka V., Burton R.A., Panstruga R., Strizhov N., Schulze-Lefert P., Fincher G.B.
Plant Cell 15:2503-2513(2003) [PubMed: 14555698] [Abstract]
Cited for: FUNCTION.
[7]"Two callose synthases, GSL1 and GSL5, play an essential and redundant role in plant and pollen development and in fertility."
Enns L.C., Kanaoka M.M., Torii K.U., Comai L., Okada K., Cleland R.E.
Plant Mol. Biol. 58:333-349(2005) [PubMed: 16021399] [Abstract]
Cited for: NOMENCLATURE.

Cross-references

Sequence databases

AF237733 mRNA. Translation: AAK37413.1.
AC005106 Genomic DNA. Translation: AAF79729.1. Sequence problems.
AC007153 Genomic DNA. Translation: AAD30609.1. Sequence problems.
AK228963 mRNA. Translation: BAF00852.1.
IPIIPI00544652.
PIRE86189.
RefSeqNP_563743.2.
UniGeneAt.15333

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9AUE0. 2 interactions.

Protein family/group databases

CAZyGT48. Glycosyltransferase Family 48.

Proteomic databases

PRIDEQ9AUE0.

Genome annotation databases

GeneID837059.
GenomeReviewsGene locus AT1G05570 in contig CT485782_GR.
KEGGath:AT1G05570.

Organism-specific databases

TAIRAt1g05570.

Family and domain databases

InterProIPR003440. Glyco_trans_48.
[Graphical view]
PfamPF02364. Glucan_synthase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALS1_ARATH
AccessionPrimary (citable) accession number: Q9AUE0
Secondary accession number(s): Q0WPU7, Q9LR43, Q9SYJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 16, 2009
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents