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CALS9_ARATH
ID   CALS9_ARATH             Reviewed;        1890 AA.
AC   Q9SFU6; F4JDA3; Q8LF10;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Callose synthase 9;
DE            EC=2.4.1.34;
DE   AltName: Full=1,3-beta-glucan synthase;
DE   AltName: Full=Protein GLUCAN SYNTHASE-LIKE 10;
GN   Name=CALS9; Synonyms=GSL10; OrderedLocusNames=At3g07160; ORFNames=T1B9.18;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1532-1890.
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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   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).
RN   [6]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=18315544; DOI=10.1111/j.1365-313x.2008.03462.x;
RA   Toeller A., Brownfield L., Neu C., Twell D., Schulze-Lefert P.;
RT   "Dual function of Arabidopsis glucan synthase-like genes GSL8 and GSL10 in
RT   male gametophyte development and plant growth.";
RL   Plant J. 54:911-923(2008).
CC   -!- FUNCTION: Involved in sporophytic and gametophytic development.
CC       Required for normal plant development. During pollen formation,
CC       required for the entry of microspores into mitosis and microspore
CC       symmetric division. May be required for correct temporal and spatial
CC       control of callose deposition during pollen mitosis. 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:18315544}.
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 with a
CC       peak at bicellular pollen stage. {ECO:0000269|PubMed:18315544}.
CC   -!- DISRUPTION PHENOTYPE: Plants develop deformed or collapsed and inviable
CC       pollen grains. {ECO:0000269|PubMed:18315544}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF20230.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAM61660.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC012395; AAF20230.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE74506.1; -; Genomic_DNA.
DR   EMBL; AY085106; AAM61660.1; ALT_INIT; mRNA.
DR   RefSeq; NP_187372.5; NM_111596.6.
DR   AlphaFoldDB; Q9SFU6; -.
DR   BioGRID; 5238; 4.
DR   STRING; 3702.AT3G07160.1; -.
DR   CAZy; GT48; Glycosyltransferase Family 48.
DR   iPTMnet; Q9SFU6; -.
DR   SwissPalm; Q9SFU6; -.
DR   PaxDb; Q9SFU6; -.
DR   PRIDE; Q9SFU6; -.
DR   EnsemblPlants; AT3G07160.1; AT3G07160.1; AT3G07160.
DR   GeneID; 819903; -.
DR   Gramene; AT3G07160.1; AT3G07160.1; AT3G07160.
DR   KEGG; ath:AT3G07160; -.
DR   Araport; AT3G07160; -.
DR   TAIR; locus:2098565; AT3G07160.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_000742_1_1_1; -.
DR   InParanoid; Q9SFU6; -.
DR   OMA; NEMARMY; -.
DR   PRO; PR:Q9SFU6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SFU6; baseline and differential.
DR   Genevisible; Q9SFU6; AT.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; 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:0052543; P:callose deposition in cell wall; IMP:TAIR.
DR   GO; GO:0048589; P:developmental growth; IMP:TAIR.
DR   GO; GO:0055047; P:generative cell mitosis; IMP:TAIR.
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: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; IPR023175; Vta1/CALS_N_sf.
DR   Pfam; PF14288; FKS1_dom1; 1.
DR   Pfam; PF02364; Glucan_synthase; 1.
DR   SMART; SM01205; FKS1_dom1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1890
FT                   /note="Callose synthase 9"
FT                   /id="PRO_0000334581"
FT   TOPO_DOM        1..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..560
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        561..581
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        582..591
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        592..612
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        613..658
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        659..679
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        680..722
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        723..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        744..1457
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1458..1478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1479..1512
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1513..1533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1534..1539
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1540..1560
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1561..1609
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1610..1630
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1631..1651
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1652..1703
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1704..1724
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1725..1732
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1733..1753
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1754..1768
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1769..1789
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1790..1795
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1796..1816
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1817..1838
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1839..1859
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1860..1890
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1577
FT                   /note="R -> M (in Ref. 3; AAM61660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1890 AA;  217087 MW;  FA18F086C071360B CRC64;
     MSRAESSWER LVNAALRRDR TGGVAGGNQS SIVGYVPSSL SNNRDIDAIL RAADEIQDED
     PNIARILCEH GYSLAQNLDP NSEGRGVLQF KTGLMSVIKQ KLAKREVGTI DRSQDILRLQ
     EFYRLYREKN NVDTLKEEEK QLRESGAFTD ELERKTVKRK RVFATLKVLG SVLEQLAKEI
     PEELKHVIDS DAAMSEDTIA YNIIPLDAPV TTNATTTFPE VQAAVAALKY FPGLPKLPPD
     FPIPATRTAD MLDFLHYIFG FQKDSVSNQR EHIVLLLANE QSRLNIPEET EPKLDDAAVR
     KVFLKSLENY IKWCDYLCIQ PAWSNLEAIN GDKKLLFLSL YFLIWGEAAN IRFLPECLCY
     IFHHMVREMD EILRQQVARP AESCMPVDSR GSDDGVSFLD HVIAPLYGVV SAEAFNNDNG
     RAPHSAWRNY DDFNEYFWSL HSFELGWPWR TSSSFFQKPI PRKKLKTGRA KHRGKTSFVE
     HRTFLHLYHS FHRLWIFLAM MFQALAIIAF NKDDLTSRKT LLQILSLGPT FVVMKFSESV
     LEVIMMYGAY STTRRLAVSR IFLRFIWFGL ASVFISFLYV KSLKAPNSDS PIVQLYLIVI
     AIYGGVQFFF SILMRIPTCH NIANKCDRWP VIRFFKWMRQ ERHYVGRGMY ERTSDFIKYL
     LFWLVVLSAK FSFAYFLQIK PLVGPTRMIV KQNNIPYSWH DFVSRKNYNA LTVASLWAPV
     VAIYLLDIHI FYTIFSAFLG FLLGARDRLG EIRSLEAIHK LFEEFPGAFM RALHVPLTNR
     TSDTSHQTVD KKNKVDAAHF APFWNQIIKS LREEDYITDF EMELLLMPKN SGRLELVQWP
     LFLLSSKILL AKEIAAESNS QEEILERIER DDYMKYAVEE VYHTLKLVLT ETLEAEGRLW
     VERIYEDIQT SLKERNIHHD FQLNKLSLVI TRVTALLGIL KENETPEHAK GAIKALQDLY
     DVMRLDILTF NMRGHYETWN LLTQAWNEGR LFTKLKWPKD PELKALVKRL YSLFTIKDSA
     AHVPRNLEAR RRLQFFTNSL FMDVPPPKSV RKMLSFSVFT PYYSEVVLYS MAELTKRNED
     GISILFYLQK IYPDEWKNFL ARIGRDENAL EGDLDNERDI LELRFWASYR GQTLARTVRG
     MMYYRKALML QSYLERKAGN DATDAEGFEL SPEARAQADL KFTYVVTCQI YGRQKEDQKP
     EAVDIALLMQ RNEALRIAYI DVVDSPKEGK SHTEYYSKLV KADISGKDKE IYSIKLPGDP
     KLGEGKPENQ NHAIVFTRGN AIQTIDMNQD NYFEEALKMR NLLEEFDRDH GIRPPTILGV
     REHVFTGSVS SLASFMSNQE TSFVTLGQRV LAKPLKIRMH YGHPDVFDRV FHITRGGISK
     ASRVINISED IFAGFNTTLR QGNVTHHEYI QVGKGRDVGL NQIALFEGKV AGGNGEQVLS
     RDVYRLGQLL DFFRMMSFFF TTVGFYLCTM LTVLTVYIFL YGRAYLALSG VGATIRERAI
     LLDDTALSAA LNAQFLFQIG VFTAVPMVLG FILEQGFLQA IVSFITMQFQ LCTVFFTFSL
     GTRTHYFGRT ILHGGARYQA TGRGFVVKHI KFSENYRLYS RSHFVKAMEV ILLLVVYLAY
     GNDEAGAVSY ILLTVSSWFL AVSWLFAPYL FNPAGFEWQK VVEDFKEWTN WLFYRGGIGV
     KGAESWEAWW EEELSHIRTL SGRIMETILS LRFFIFQYGI VYKLKLQGSD TSFAVYGWSW
     VAFAMIIVLF KVFTFSQKIS VNFQLLLRFI QGLSLLMALA GIIVAVVLTP LSVTDIFACV
     LAFIPTGWGI LSIACAWKPV LKRMGMWKSI RSLARLYDAL MGMLIFLPVA LCSWFPFVST
     FQTRMMFNQA FSRGLEISLI LAGDNPNSGL
 
 
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