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CSLF3_ORYSI
ID   CSLF3_ORYSI             Reviewed;         868 AA.
AC   A2YMH5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Probable mixed-linked glucan synthase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=1,3;1,4-beta-D-glucan synthase 3;
DE   AltName: Full=Cellulose synthase-like protein F3;
DE   AltName: Full=OsCslF3;
GN   Name=CSLF3; ORFNames=OsI_025518;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [2]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11842136; DOI=10.1104/pp.010875;
RA   Hazen S.P., Scott-Craig J.S., Walton J.D.;
RT   "Cellulose synthase-like genes of rice.";
RL   Plant Physiol. 128:336-340(2002).
CC   -!- FUNCTION: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on
CC       beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in
CC       grasses and cereals (Poaceae). The mixed-linked glucans (which are not
CC       present in walls of dicotyledons or most other monocotyledonous plants)
CC       are particularly important constituents of the walls of the starchy
CC       endosperm and aleurone cells of cereal grains such as oats, wheat, rice
CC       and barley. They can account for up to 70% by weight of the wall (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase-like F subfamily. {ECO:0000305}.
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DR   EMBL; CM000132; EAZ04286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2YMH5; -.
DR   SMR; A2YMH5; -.
DR   STRING; 39946.A2YMH5; -.
DR   EnsemblPlants; BGIOSGA024117-TA; BGIOSGA024117-PA; BGIOSGA024117.
DR   Gramene; BGIOSGA024117-TA; BGIOSGA024117-PA; BGIOSGA024117.
DR   HOGENOM; CLU_001418_3_1_1; -.
DR   OMA; YIGTWTA; -.
DR   Proteomes; UP000007015; Chromosome 7.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR   GO; GO:0071669; P:plant-type cell wall organization or biogenesis; IEA:UniProt.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005150; Cellulose_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF03552; Cellulose_synt; 2.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..868
FT                   /note="Probable mixed-linked glucan synthase 3"
FT                   /id="PRO_0000319403"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        649..669
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        717..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        771..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        809..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        837..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          36..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        573
FT                   /evidence="ECO:0000255"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   868 AA;  97816 MW;  6AFF8010648717CF CRC64;
     MASPASVAGG GEDSNGCSSL IDPLLVSRTS SIGGAERKAA GGGGGGAKGK HWAAADKGER
     RAAKECGGED GRRPLLFRSY RVKGSLLHPY RALIFARLIA VLLFFGWRIR HNNSDIMWFW
     TMSVAGDVWF GFSWLLNQLP KFNPVKTIPD LTALRQYCDL ADGSYRLPGI DVFVTTADPI
     DEPVLYTMNC VLSILAADYP VDRSACYLSD DSGALILYEA LVETAKFATL WVPFCRKHCI
     EPRSPESYFE LEAPSYTGSA QEEFKNDSRI VHLEYDEFKV RLEALPETIR KRSDVYNSMK
     TDQGAPNATW MANGTQWPGT WIEPIENHRK GHHAGIVKVV LDHPIRGHNL SLKDSTGNNL
     NFNATDVRIP MLVYVSRGKN PNYDHNKKAG ALNAQLRASA LLSNAQFIIN FDCDHYINNS
     QALRAAICFM LDQREGDNTA FVQFPQRFDN VDPKDRYGNH NRVFFDGTML ALNGLQGPSY
     LGTGCMFRRL ALYGIDPPHW RQDNITPESS KFGNSILLLE SVLEALNQDR FATPSPVNDI
     FVNELEMVVS ASFDKETDWG KGVGYIYDIA TEDIVTGFRI HGQGWRSMYC TMEHDAFCGT
     APINLTERLH QIVRWSGGSL EMFFSHNNPL IGGRRLQPLQ RVSYLNMTIY PVTSLFILLY
     AISPVMWLIP DEVYIQRPFT RYVVYLLMII LMIHMIGWLE IKWAGITWLD YWRNEQFFMI
     GSTSAYPTAV LHMVVNLLTK KGIHFRVTSK QTTADTNDKF ADLYEMRWVP MLIPTMVVLV
     ANIGAIGVAI GKMAVYMGVW TIAQKRHAIM GLLFNMWVMF LLYPFALAIM GRWAKRPIIL
     VVLLPIIFVI VALVYVATHI LLANIIPF
 
 
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