UniProt: A0A0E0FMP3

Database: UniProt
Entry: A0A0E0FMP3_ORYNI

LinkDB:  A0A0E0FMP3_ORYNI 
Original site:  A0A0E0FMP3_ORYNI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein domain (10)   
   InterPro (5)   
   Pfam (4)   
   SMART (1)   
All databases (16)   

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ID   A0A0E0FMP3_ORYNI        Unreviewed;      1471 AA.
AC   A0A0E0FMP3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-JAN-2026, entry version 33.
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 nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G20840.4};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA01G20840.4}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G20840.4};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA01G20840.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang J., Kudrna D., Lee S., Talag J., Rajasekar S., Welchert J.,
RA   Hsing Y.-I., Wing R.A.;
RT   "OnivRS2 (Oryza nivara Reference Sequence Version 2).";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC         beta-D-glucosyl](n+1) + UDP + H(+); 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:ARBA00047777};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC       {ECO:0000256|ARBA:ARBA00009040}.
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DR   EnsemblPlants; ONIVA01G20840.4; ONIVA01G20840.4; ONIVA01G20840.
DR   Gramene; ONIVA01G20840.4; ONIVA01G20840.4; ONIVA01G20840.
DR   Proteomes; UP000006591; Chromosome 1.
DR   GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR   InterPro; IPR058851; CALS1_helical.
DR   InterPro; IPR026899; FKS1-like_dom1.
DR   InterPro; IPR003440; Glyco_trans_48_dom.
DR   InterPro; IPR039431; Vta1/CALS_N.
DR   InterPro; IPR023175; Vta1/CALS_N_sf.
DR   PANTHER; PTHR12741:SF16; CALLOSE SYNTHASE 7; 1.
DR   PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR   Pfam; PF25968; CALS1; 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:UP000006591};
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        508..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        559..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        584..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1228..1247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1253..1275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1329..1350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1379..1399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1420..1438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          331..430
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1471 AA;  170336 MW;  39352E11EE90B94D CRC64;
     MATGGGGLSG PQPSLRRGLS RAFTMRPEGY SGEDGGEYSE ESELVPNSLA PIVPILRAAN
     EIEEENQRVA YLCRFTAFEK AHTMDPNSGG RGVRQFKTYL LHRLEKDEHE TQRRLAGTDA
     KEIQRFYEHY CKKNLVDGLK TKKPEEMARH YQIASVLYDV LKTVTPEKFH AEFDIYAKEV
     EKEKASFSHY NILPLNISGQ RQPVMEIPEI KAAVDLLRKI DGLPMPRLDP VSAEKETDVP
     TVRDLFDWLW LTFGFQKGNV ENQKEHLILL LANIDMRKGA NAYQSDRHNH VMHSDTVRSL
     MRKIFENYIY WCRYLHLESN IKIPNDASTQ QPEILYIGLY LLIWGEASNS HQYKNTIIPI
     RQDFDPPFRR EGSDDAFLQL VIQPIYSVMK QEAAMNKRGR TSHSKWRNYD DLNEYFWSKR
     CFKQLKWPMD SAADFFAVPL KIKTEEAMVI VAWSPSGLPS AIFDPTVFRN VLTIFITAAF
     LNFLQATLEI ILNWKAWRSL ECSQMIRYIL KFVVAVAWLI ILPTTVLERS NSRIIRFFLW
     WTQPKLYVAR GMYEDTCSLL KYTLFWILLL ICKLTFSFYV EHNLGVVITV WAPIVMIRTL
     GMLRSRFEAI PIAFGKHLVP GHDSQPKRHE HEEDKINKFS DIWNAFIHSL REEDLISNRV
     VDRIHDRIED SIRRQSLRTD EDIEPIKTQI ANLLQDIMEI ITQDIMKNGQ GILKDENRNN
     QLFANINLDS VKDKTWKEKP FCFCISVLTP YFKEEVLFSA EDLYKKNEDG ISILFYLRKI
     YPDEWKNFLE RIEFQPTDEE SLKTKMDEIR PWASYRGQTL TRTVKLEHRR TVESSQQGWA
     SFDMARAIAD IKFTYVVSCQ VYGMQKTSKD PKDKACYLNI LNLMYPSLRV AYIDEVEAPA
     GNGTTEKTYY SVLVKGGEKY DEEIYRIKLP GKPTDIGEGK PENQNHAIVF TRGEALQAID
     MNQDNYLEEA FKMRNVLEEF ESEKYGKRKP TILGLREHIF TGSVSSLAWF MSNQETSFVT
     IGQRVLANPL KVRFHYGHPD IFDRLFHITR GGISKASKTI NLSEDIFSGF NSTMREGNVT
     HHEYMQVGKG RDVGMNQISS FEAKVANGNV MSGLERSILL DPRIEQNIKP LENALASQSF
     FQLGLLLVLP MVMEVGLEKG FRTALGEFVI MQLQLASVFF TFQLGTKTHY YGRTILHGGA
     KYRPTGRGFV VYHAKFADNY RMYSRSHFVK GLELLILLVV YLVYGSSYRS SSMYLFVTFS
     IWFLVASWLF APFIFNPSCF EWQKTVDDWT DWRKWMGNRG GIGMSVDQSW EAWWISEQEH
     LRKTSIRSLL LEIILSLRFL IYQYGIVYHL NIARRSKSIL MVSIGRQKFG TDLQLMFRIL
     KGLLFLGFVS VMAIGQACSP LVKKAMLWDS IMELGRSYEN LMGLVLFLPI GLLSWFPFVS
     EFQTRLLFNQ AFSRGLQISR ILAGQKDIGE E
//

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