UniProt: A0A0E0NP52

Database: UniProt
Entry: A0A0E0NP52_ORYRU

LinkDB:  A0A0E0NP52_ORYRU 
Original site:  A0A0E0NP52_ORYRU

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (3)   
   SMART (1)   
All databases (14)   

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ID   A0A0E0NP52_ORYRU        Unreviewed;      1661 AA.
AC   A0A0E0NP52;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI03G01980.1, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI03G01980.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   EnsemblPlants; ORUFI03G01980.1; ORUFI03G01980.1; ORUFI03G01980.
DR   Gramene; ORUFI03G01980.1; ORUFI03G01980.1; ORUFI03G01980.
DR   HOGENOM; CLU_000742_0_0_1; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
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   Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 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   PANTHER; PTHR12741:SF65; 1,3-BETA-GLUCAN SYNTHASE; 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; 3.
DR   Pfam; PF04652; Vta1; 1.
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:UP000008022};
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        420..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        456..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        535..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1404..1427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1541..1559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1601..1622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          257..373
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1661 AA;  192490 MW;  F24228A38D2E05F8 CRC64;
     MTSLSRTLSR GGPMQPPGQR RILRTQTAVN LGEQIFDSEV VPSSLVEIAP ILRVANEVEA
     SNPRVAYLCR FYAFEKAHRL DPTSSGRGVR QFKTALLQRL ERENEPTLRG RARKSDAREI
     QAFYQHYYKK YIQALQNVSD QVDRAQLTKA YQTANVLFEV LKAVTQQHSV EVDHEILEAA
     DKVKEKTKIY LPFNILPLDP DSGNQAVMKF PEIQAAAVAL RNTRGLPWPK TYEHKVNEDL
     LDWLQSMLPT IQQEVQQRKL LYMGLYLLIW GEAANLRFMP ECICYIYHHM AFEMYGMLVG
     NVSALTGEYV KPAYGGEKEA FLKKVVTPIY LTIAKEAERS KREKGNHSEW RNYDDLNEYF
     WSAECFRLGW PMRADADFFC QHLNSPDQRN ETTRTEKQKG KVNFVELRSF WHIFRSFDRM
     WSFFILALQV MVILAWNGGS LGNIFDPVVF KKILSIFITS AILNLGQATL DIIFNWKARR
     TMEFAVKLRY VLKFTLAALW VVLLPVTYAY TWENPTGIIR AIKGWFGNGQ NHPSLFVLAV
     VIYLSPSLLA AILFLLPFLR RILESSDYKF VRFVMWWSQL TTDQDNVENI VVSYYLRRRP
     DMTKQNPRLF VGRGMHESAF SLFIYYVEIK PLVEPTKDIM KLPIHTFQWH EFFPKANGNI
     GVVIALWAPI ILVYFMDTQI WYTIFSTLLG GIYGAFQRLG EIRTLGMLRS RFGSIPLAFN
     ACLIPAEESD AKRKKGLKSY LHSRFERKHT DKEKIAARFA QMWNEIITSF REEDLINNKE
     KELLLVPYVA DQALEIMQWP PFLLASKIPI AVDMAKDSNG KDRDLKKRLE NDYYFKCAIE
     ECYASFKNII KDLVQGEPEK RVINTIFAEV EKYIADDKEK NDKNDRDAVI KIFQDMLEVV
     TRDIMEDQLS SILESSHGGS YQRPEGTTTW DQEYQLFQPA GAIKFPLQFT DAWIEKIKRL
     ELLLTVKESA MDVPSNLEAR RRLTFFTNSL FMDMPDAPKV RNMLSFSALT PYYNEPVLFS
     IKELQEENED GVSTLFYLQK IYPDEWKNFQ QRVEWDEELK ENEDKNEELR LWASYRGQTL
     ARTVRGMMYY RKALVLEAFL DMAKHEDLME GYKAVESTDE QWKLQRSLFA QCEAVADMKF
     TYVVSCQQYG NDKRAALPNA QDILQLMRTY PSLRVAYIDQ VEDRVEEKKM EPAYYSTLVK
     VALTKDSEST DPVQNLDQVI YRIKLPGPAM LGEGKPENQN HAIIFTRGEG LQTIDMNQDN
     YMEEALKMRN LLQEFLTEHG VRRPSILGVR EHIFTGRVRF HYGHPDVFDR IFHLTRGGVS
     KASRSINLSE DIFAGYNSTL RGGNITHHEY VQVGKGRDVG LNQISKFEAK VANGNGEQTL
     SRDIYRLGHR FDFFRMLSCY FTTVGFYFST LLTVVTVYVF LYGRLYLALS GLEEGLLTQR
     RYIHNHPLQV ALASQSLVQL GFLMALPMMM EIGLEKGFGQ ALMLTWLFAP FLFNPSGFEW
     TKIVDDWSDW NKWISNRGGI GVSPDKSWES WWEIELEHLK YSGTIGLFVE IILSLRFFIY
     QYGLVYHLNI TGDKSILIAQ ACKPLARRAG LWGSVRALAR AYEIIMGVLL FTPITILAWF
     PFVSEFQTRM LFNQAFSRGL QISRILGGQK KERERSSRNK D
//

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