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CALS1_ARATH
ID   CALS1_ARATH             Reviewed;        1950 AA.
AC   Q9AUE0; Q0WPU7; Q9LR43; Q9SYJ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Callose synthase 1;
DE            EC=2.4.1.34;
DE   AltName: Full=1,3-beta-glucan synthase;
DE   AltName: Full=Protein GLUCAN SYNTHASE-LIKE 6;
GN   Name=CALS1; Synonyms=GSL6; OrderedLocusNames=At1g05570;
GN   ORFNames=F3F20.1, T25N20.22;
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], SUBCELLULAR LOCATION, GENE FAMILY,
RP   NOMENCLATURE, AND INTERACTION WITH UGT1 AND PHRAGMOPLASTIN.
RC   STRAIN=cv. Columbia; TISSUE=Shoot meristem;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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 1202-1950.
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   SUBUNIT, AND INTERACTION WITH UGT1.
RX   PubMed=11283335; DOI=10.2307/3871339;
RA   Hong Z., Zhang Z., Olson J.M., Verma D.P.S.;
RT   "A novel UDP-glucose transferase is part of the callose synthase complex
RT   and interacts with phragmoplastin at the forming cell plate.";
RL   Plant Cell 13:769-779(2001).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11785931; DOI=10.1023/a:1013679111111;
RA   Verma D.P.S., Hong Z.;
RT   "Plant callose synthase complexes.";
RL   Plant Mol. Biol. 47:693-701(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=14555698; DOI=10.1105/tpc.016097;
RA   Jacobs A.K., Lipka V., Burton R.A., Panstruga R., Strizhov N.,
RA   Schulze-Lefert P., Fincher G.B.;
RT   "An Arabidopsis callose synthase, GSL5, is required for wound and papillary
RT   callose formation.";
RL   Plant Cell 15:2503-2513(2003).
RN   [8]
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. Not required for callose formation after wounding
CC       or pathogen attack. 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.
CC       {ECO:0000269|PubMed:14555698}.
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   -!- ACTIVITY REGULATION: May be regulated by ROP1 through the interaction
CC       with UGT1.
CC   -!- SUBUNIT: Interacts with UGT1 and phragmoplastin. May form a functional
CC       complex with UGT1, ROP1 and phragmoplastin.
CC       {ECO:0000269|PubMed:11283334, ECO:0000269|PubMed:11283335}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11283334,
CC       ECO:0000269|PubMed:11785931}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11283334, ECO:0000269|PubMed:11785931}.
CC       Note=Localized in the forming cell plate during cytokinesis.
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=Q9AUE0-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD30609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAF79729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF237733; AAK37413.1; -; mRNA.
DR   EMBL; AC005106; AAF79729.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC007153; AAD30609.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27855.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60178.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60179.1; -; Genomic_DNA.
DR   EMBL; AK228963; BAF00852.1; -; mRNA.
DR   PIR; E86189; E86189.
DR   RefSeq; NP_001322482.1; NM_001331555.1. [Q9AUE0-1]
DR   RefSeq; NP_001322483.1; NM_001331556.1. [Q9AUE0-1]
DR   RefSeq; NP_563743.2; NM_100436.5. [Q9AUE0-1]
DR   AlphaFoldDB; Q9AUE0; -.
DR   SMR; Q9AUE0; -.
DR   BioGRID; 22301; 1.
DR   IntAct; Q9AUE0; 2.
DR   STRING; 3702.AT1G05570.1; -.
DR   CAZy; GT48; Glycosyltransferase Family 48.
DR   iPTMnet; Q9AUE0; -.
DR   PaxDb; Q9AUE0; -.
DR   PRIDE; Q9AUE0; -.
DR   ProteomicsDB; 239091; -. [Q9AUE0-1]
DR   EnsemblPlants; AT1G05570.1; AT1G05570.1; AT1G05570. [Q9AUE0-1]
DR   EnsemblPlants; AT1G05570.3; AT1G05570.3; AT1G05570. [Q9AUE0-1]
DR   EnsemblPlants; AT1G05570.4; AT1G05570.4; AT1G05570. [Q9AUE0-1]
DR   GeneID; 837059; -.
DR   Gramene; AT1G05570.1; AT1G05570.1; AT1G05570. [Q9AUE0-1]
DR   Gramene; AT1G05570.3; AT1G05570.3; AT1G05570. [Q9AUE0-1]
DR   Gramene; AT1G05570.4; AT1G05570.4; AT1G05570. [Q9AUE0-1]
DR   KEGG; ath:AT1G05570; -.
DR   Araport; AT1G05570; -.
DR   TAIR; locus:2031938; AT1G05570.
DR   eggNOG; KOG0916; Eukaryota.
DR   InParanoid; Q9AUE0; -.
DR   OrthoDB; 48442at2759; -.
DR   PhylomeDB; Q9AUE0; -.
DR   BioCyc; ARA:AT1G05570-MON; -.
DR   PRO; PR:Q9AUE0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9AUE0; baseline and differential.
DR   Genevisible; Q9AUE0; AT.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0009504; C:cell plate; IDA:TAIR.
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:0009506; C:plasmodesma; HDA:TAIR.
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; IPR039431; Vta1/CALS_N.
DR   InterPro; IPR023175; Vta1/CALS_N_sf.
DR   PANTHER; PTHR12741:SF59; PTHR12741:SF59; 1.
DR   Pfam; PF14288; FKS1_dom1; 1.
DR   Pfam; PF02364; Glucan_synthase; 2.
DR   Pfam; PF04652; Vta1; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   1: Evidence at protein level;
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..1950
FT                   /note="Callose synthase 1"
FT                   /id="PRO_0000334573"
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..505
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        527..552
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        574..599
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        600..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        621..655
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        656..676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        677..712
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        713..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        734..1511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1512..1532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1533..1560
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1561..1581
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1582..1591
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1592..1612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1613..1655
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1656..1676
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1677..1682
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1683..1703
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1704..1755
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1756..1776
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1777..1787
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1788..1808
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1809..1828
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1829..1849
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1850..1851
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1852..1872
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1873..1894
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1895..1915
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1916..1950
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        577
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        88
FT                   /note="T -> A (in Ref. 1; AAK37413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="Q -> R (in Ref. 1; AAK37413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        560
FT                   /note="A -> S (in Ref. 1; AAK37413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        725
FT                   /note="L -> P (in Ref. 1; AAK37413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1268..1270
FT                   /note="KGT -> EGA (in Ref. 1; AAK37413)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1396
FT                   /note="V -> A (in Ref. 4; BAF00852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1653
FT                   /note="R -> H (in Ref. 4; BAF00852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1950 AA;  225761 MW;  25EA79B202BA7443 CRC64;
     MAQRREPDPP PPQRRILRTQ TVGSLGEAML DSEVVPSSLV EIAPILRVAN EVEASNPRVA
     YLCRFYAFEK AHRLDPTSSG RGVRQFKTAL LQRLERENET TLAGRQKSDA REMQSFYQHY
     YKKYIQALLN AADKADRAQL TKAYQTAAVL FEVLKAVNQT EDVEVADEIL ETHNKVEEKT
     QIYVPYNILP LDPDSQNQAI MRLPEIQAAV AALRNTRGLP WTAGHKKKLD EDILDWLQSM
     FGFQKDNVLN QREHLILLLA NVHIRQFPKP DQQPKLDDRA LTIVMKKLFR NYKKWCKYLG
     RKSSLWLPTI QQEVQQRKLL YMGLYLLIWG EAANLRFMPE CLCYIYHHMA FELYGMLAGS
     VSPMTGEHVK PAYGGEDEAF LQKVVTPIYQ TISKEAKRSR GGKSKHSVWR NYDDLNEYFW
     SIRCFRLGWP MRADADFFCQ TAEELRLERS EIKSNSGDRW MGKVNFVEIR SFWHIFRSFD
     RLWSFYILCL QAMIVIAWNG SGELSAIFQG DVFLKVLSVF ITAAILKLAQ AVLDIALSWK
     ARHSMSLYVK LRYVMKVGAA AVWVVVMAVT YAYSWKNASG FSQTIKNWFG GHSHNSPSLF
     IVAILIYLSP NMLSALLFLF PFIRRYLERS DYKIMMLMMW WSQPRLYIGR GMHESALSLF
     KYTMFWIVLL ISKLAFSYYA EIKPLVGPTK DIMRIHISVY SWHEFFPHAK NNLGVVIALW
     SPVILVYFMD TQIWYAIVST LVGGLNGAFR RLGEIRTLGM LRSRFQSIPG AFNDCLVPQD
     NSDDTKKKRF RATFSRKFDQ LPSSKDKEAA RFAQMWNKII SSFREEDLIS DREMELLLVP
     YWSDPDLDLI RWPPFLLASK IPIALDMAKD SNGKDRELKK RLAVDSYMTC AVRECYASFK
     NLINYLVVGE REGQVINDIF SKIDEHIEKE TLITELNLSA LPDLYGQFVR LIEYLLENRE
     EDKDQIVIVL LNMLELVTRD IMEEEVPSLL ETAHNGSYVK YDVMTPLHQQ RKYFSQLRFP
     VYSQTEAWKE KIKRLHLLLT VKESAMDVPS NLEARRRLTF FSNSLFMDMP PAPKIRNMLS
     FSVLTPYFSE DVLFSIFGLE QQNEDGVSIL FYLQKIFPDE WTNFLERVKC GNEEELRARE
     DLEEELRLWA SYRGQTLTKT VRGMMYYRKA LELQAFLDMA KDEELLKGYK ALELTSEEAS
     KSGGSLWAQC QALADMKFTF VVSCQQYSIH KRSGDQRAKD ILRLMTTYPS IRVAYIDEVE
     QTHKESYKGT EEKIYYSALV KAAPQTKPMD SSESVQTLDQ LIYRIKLPGP AILGEGKPEN
     QNHAIIFTRG EGLQTIDMNQ DNYMEEAFKM RNLLQEFLEK HGGVRCPTIL GLREHIFTGS
     VSSLAWFMSN QENSFVTIGQ RVLASPLKVR FHYGHPDIFD RLFHLTRGGI CKASKVINLS
     EDIFAGFNST LREGNVTHHE YIQVGKGRDV GLNQISMFEA KIANGNGEQT LSRDLYRLGH
     RFDFFRMLSC YFTTIGFYFS TMLTVLTVYV FLYGRLYLVL SGLEEGLSSQ RAFRNNKPLE
     AALASQSFVQ IGFLMALPMM MEIGLERGFH NALIEFVLMQ LQLASVFFTF QLGTKTHYYG
     RTLFHGGAEY RGTGRGFVVF HAKFAENYRF YSRSHFVKGI ELMILLLVYQ IFGQSYRGVV
     TYILITVSIW FMVVTWLFAP FLFNPSGFEW QKIVDDWTDW NKWIYNRGGI GVPPEKSWES
     WWEKELEHLR HSGVRGITLE IFLALRFFIF QYGLVYHLST FKGKNQSFWV YGASWFVILF
     ILLIVKGLGV GRRRFSTNFQ LLFRIIKGLV FLTFVAILIT FLALPLITIK DLFICMLAFM
     PTGWGMLLIA QACKPLIQQL GIWSSVRTLA RGYEIVMGLL LFTPVAFLAW FPFVSEFQTR
     MLFNQAFSRG LQISRILGGQ RKDRSSKNKE
 
 
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