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CALS7_ARATH
ID   CALS7_ARATH             Reviewed;        1958 AA.
AC   Q9SHJ3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Callose synthase 7;
DE            EC=2.4.1.34;
DE   AltName: Full=1,3-beta-glucan synthase;
DE   AltName: Full=Protein GLUCAN SYNTHASE-LIKE 7;
GN   Name=CALS7; Synonyms=GSL7; OrderedLocusNames=At1g06490; ORFNames=F12K11.17;
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=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   [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   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24822.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007592; AAF24822.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27993.1; -; Genomic_DNA.
DR   PIR; F86200; F86200.
DR   RefSeq; NP_172136.2; NM_100528.3.
DR   AlphaFoldDB; Q9SHJ3; -.
DR   SMR; Q9SHJ3; -.
DR   STRING; 3702.AT1G06490.1; -.
DR   CAZy; GT48; Glycosyltransferase Family 48.
DR   PaxDb; Q9SHJ3; -.
DR   PRIDE; Q9SHJ3; -.
DR   EnsemblPlants; AT1G06490.1; AT1G06490.1; AT1G06490.
DR   GeneID; 837160; -.
DR   Gramene; AT1G06490.1; AT1G06490.1; AT1G06490.
DR   KEGG; ath:AT1G06490; -.
DR   Araport; AT1G06490; -.
DR   TAIR; locus:2009185; AT1G06490.
DR   eggNOG; KOG0916; Eukaryota.
DR   HOGENOM; CLU_000742_0_0_1; -.
DR   InParanoid; Q9SHJ3; -.
DR   OrthoDB; 48442at2759; -.
DR   BioCyc; ARA:AT1G06490-MON; -.
DR   BioCyc; MetaCyc:AT1G06490-MON; -.
DR   PRO; PR:Q9SHJ3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SHJ3; baseline and differential.
DR   Genevisible; Q9SHJ3; 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; IMP:TAIR.
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:0080165; P:callose deposition in phloem sieve plate; IMP:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0010233; P:phloem transport; IMP:TAIR.
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   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1958
FT                   /note="Callose synthase 7"
FT                   /id="PRO_0000334579"
FT   TOPO_DOM        1..504
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        526..535
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        557..569
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        570..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        591..620
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        621..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        642..673
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        674..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        695..730
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        731..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        752..1496
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1497..1517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1518..1547
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1548..1568
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1569..1576
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1577..1597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1598..1640
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1641..1661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1662..1667
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1668..1688
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1689..1742
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1743..1763
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1764..1771
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1772..1792
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1793..1812
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1813..1833
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1834..1835
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1836..1856
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1857..1878
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1879..1899
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1900..1958
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1958 AA;  228032 MW;  40AC43FFC980F692 CRC64;
     MASTSSGGRG EDGRPPQMQP VRSMSRKMTR AGTMMIEHPN EDERPIDSEL VPSSLASIAP
     ILRVANDIDQ DNARVAYLCR FHAFEKAHRM DPTSSGRGVR QFKTYLLHKL EEEEEITEHM
     LAKSDPREIQ LYYQTFYENN IQDGEGKKTP EEMAKLYQIA TVLYDVLKTV VPQARIDDKT
     LRYAKEVERK KEQYEHYNIL PLYALGAKTA VMELPEIKAA ILAVCNVDNL PRPRFHSASA
     NLDEVDRERG RSFNDILEWL ALVFGFQRGN VANQREHLIL LLANIDVRKR DLENYVEIKP
     STVRKLMEKY FKNYNSWCKY LRCDSYLRFP AGCDKQQLSL LYIGLYLLIW GEASNVRFMP
     ECLCYIFHNM ANEVHGILFG NVYPVTGDTY EAGAPDEEAF LRNVITPIYQ VLRKEVRRNK
     NGKASHSKWR NYDDLNEYFW DKRCFRLKWP MNFKADFFIH TDEISQVPNQ RHDQVSHGKR
     KPKTNFVEAR TFWNLYRSFD RMWMFLVLSL QTMIIVAWHP SGSILAIFTE DVFRNVLTIF
     ITSAFLNLLQ ATLDLVLSFG AWKSLKFSQI MRYITKFLMA AMWAIMLPIT YSKSVQNPTG
     LIKFFSSWVG SWLHRSLYDY AIALYVLPNI LAAVFFLLPP LRRIMERSNM RIVTLIMWWA
     QPKLYIGRGM HEEMFALFKY TFFWVMLLLS KLAFSYYVEI LPLVNPTKLI WDMHVVNYEW
     HEFFPNATHN IGVIIAIWGP IVLVYFMDTQ IWYAIFSTLF GGIYGAFSHL GEIRTLGMLR
     SRFKVVPSAF CSKLTPLPLG HAKRKHLDET VDEKDIARFS QMWNKFIHTM RDEDLISDRE
     RDLLLVPSSS GDVTVVQWPP FLLASKIPIA LDMAKDFKGK EDVDLFKKIK SEYYMHYAVV
     EAYETVRDII YGLLQDESDK RIVREICYEV DISIQQHRFL SEFRMTGMPL LSDKLEKFLK
     ILLSDYEEDD YKSQIINVLQ DIIEIITQDV MVNGHEILER AHLQSGDIES DKKEQRFEKI
     DLSLTQNISW REKVVRLLLL LTVKESAINI PQSLEARRRM TFFANSLFMN MPDAPRVRDM
     LSFSVLTPYY KEDVLYSEEE LNKENEDGIT ILFYLQRIYP EEWSNYCERV NDLKRNLSEK
     DKAEQLRQWV SYRGQTLSRT VRGMMYYRVA LELQCFQEYT EENATNGGYL PSESNEDDRK
     AFSDRARALA DLKFTYVVSC QVYGNQKKSS ESRDRSCYNN ILQLMLKYPS LRVAYIDERE
     ETVNGKSQKV FYSVLLKGCD KLDEEIYRIK LPGPPTEIGE GKPENQNHAI IFTRGEALQT
     IDMNQDNYFE ECFKMRNVLQ EFDEGRRGKR NPTILGLREH IFTGSVSSLA WFMSNQETSF
     VTIGQRVLAN PLRVRFHYGH PDIFDRIFHI TRGGISKASK IINLSEDIFA GYNSTLRGGY
     VTHHEYIQAG KGRDVGMNQI SFFEAKVANG NGEQTLSRDV YRLGRRFDFY RMLSFYFTTV
     GFYFSSMITV LTVYVFLYGR LYLVLSGLEK NILQSASVHE SNALEQALAA QSVFQLGFLM
     VLPMVMEIGL EKGFRTALGD FIIMQLQLAS VFFTFQLGTK AHYFGRTILH GGSKYRATGR
     GFVVFHAKFA ENYRLYSRSH FVKGLELVIL LVVYQVYGTS YRSSSTYMYI TFSMWFLVTS
     WLFAPFIFNP SGFEWQKTVD DWTDWKRWMG NRGGIGIVLD KSWESWWDIE QEHLKHTNLR
     GRVLEILLAL RFLLYQYGIV YHLNIARRHT TFLVYGLSWA ILLSVLLVLK MVSMGRRKFG
     TDFQVMFRIL KALLFLGFLS VMTVLFVVCG LTISDLFASI LAFLPTGWAI LLIGQALRSV
     FKGLGFWDSV KELGRAYEYI MGLVIFTPIA VLSWFPFVSE FQTRLLFNQA FSRGLQISMI
     LAGKKDKETP STKYLGHTEE SFGLEHDTNT FNHYYLWT
 
 
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