ID B8A9R1_ORYSI Unreviewed; 1207 AA.
AC B8A9R1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN ORFNames=OsI_03775 {ECO:0000313|EMBL:EEC71499.1};
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 {ECO:0000313|EMBL:EEC71499.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC71499.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
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., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; CM000126; EEC71499.1; -; Genomic_DNA.
DR AlphaFoldDB; B8A9R1; -.
DR STRING; 39946.B8A9R1; -.
DR EnsemblPlants; BGIOSGA000810-TA; BGIOSGA000810-PA; BGIOSGA000810.
DR Gramene; BGIOSGA000810-TA; BGIOSGA000810-PA; BGIOSGA000810.
DR HOGENOM; CLU_000742_2_1_1; -.
DR OMA; HENDVYH; -.
DR Proteomes; UP000007015; Chromosome 1.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF7; CALLOSE SYNTHASE 12; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 327..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 502..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 549..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..291
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1207 AA; 140267 MW; 48804F0D6251C44E CRC64;
MSLLRNRRAA AAAAAAGSGE QTVVQAAYNI IPIQDVVMHG DHPSLQVPEV RAAVEALSHA
SDFPAPPLAR VWDPHRADIF DWLGATFGFQ ADNVRNQREH LVLLLANAQL RAAPRFPKDH
PIDVLHLTVA RGIRRKLLKN YTSWCAYLGQ KRHFRVPSGG GGGRRTGAAT GNDVRMDLLY
TALYLLIWGE AANLRFMPEC LCYIFHYMAL DLHHVVEQSI DIETGRPAMP AVCGEDAFLI
RVVTPIYNVL KNEVEASRNG TKPHSAWRNY DDVNEYFWSR RVFKRLRWPL DPSRSFFVEP
GKTGRIGKTG FVEQRSFWNV YRSFDRVWVM HILFFQAAMI VAWDGKTPWV SLRFRDIQVR
VLSVFITWGG LRFVQAMLDA GTQYSLVSRE TKTVAVRMVL KVLVAAGWTI TFSVLYKRMW
DQRWRDRRWS FAANTRVLNY LEAAAVFVIP QVLAIVLFII PWIRNFLEKT NWKILYVLTW
WFQTRTFVGR GLREGLIDNI KYSIFWVCLL VSKFSFSYFL QIKPMVGPTK VIFKLHDIKR
NWFEFMPHTE RLAVIILWLP VIIIYLMDIQ IWYAVFSSLT GALIGLFSHL GEIRSVEQLR
LRFQFFASAM QFNLMPEEHL DTVHGGIRSK FYDAINRLKL RYGFGRPYRK IEANEVEAKR
FALVWNEIIQ TFREEDIISD KELGLLELPA VVWRIRVVRW PCLLLKNELL LALSQAAELV
ADDRTHWNKI CNNEYRRCAV IEAYDSIRHL LLEIIKERTN EHIIVNQLFL AFDGAMEYGK
FTEEYRLTLL PQIHKYVISL VEQLLLKDKD QIKIVRTLQD LYDLAVHDFP KIKKDFEQLR
REGLALSRPT ESQLLFQDAI KCPDDDDVSF YKQVRRLHTI LTSRDSMDDV PKNPEARRRI
TFFSNSLFMN MPRAPTVQRM MAFSVLTPCY NEDVLYNKDQ LRRENEDGIS ILFYLQKIYE
DDWKNFLERM QREGMASDDG IWAGKFQDLR LWASYRGQTL ARTVRGMMYY YRALKMLAFL
DNASEVEITE GTKQLASFGS IQYENDVYPM NGGLSQRPRR RLERGTSTVS QLFKGQEDGA
AIMKYTYVVA CQIYGNQKKA KDQRAEDILT LMKKNDALRV AYVDEVHPEI GDTQYYSVLV
KFDPVLQREV EIYRIRLPGQ LKLGEGKPEN QNHAIIFTRG SNKVIAVRPS SVTSVQLLMQ
CGRLSVY
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