ID A0A2G2ZVZ7_CAPAN Unreviewed; 1190 AA.
AC A0A2G2ZVZ7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=T459_08255 {ECO:0000313|EMBL:PHT86149.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT86149.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT86149.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHT86149.1}.
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DR EMBL; AYRZ02000003; PHT86149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2ZVZ7; -.
DR STRING; 4072.A0A2G2ZVZ7; -.
DR EnsemblPlants; PHT86149; PHT86149; T459_08255.
DR Gramene; PHT86149; PHT86149; T459_08255.
DR OMA; FFPEVQG; -.
DR Proteomes; UP000222542; Chromosome 3.
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; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF67; CALLOSE SYNTHASE 10; 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; 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:UP000222542};
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 494..513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 347..460
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 19..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 137807 MW; 9275A029C354938F CRC64;
MARVYENWER LVRATLRREQ LRQTSPGHGR TPSGIAGSVP DSLQRTTNIN AILQAADEIQ
DEDPNVARIL CEQAYSMAQN LDPNSDGRGV LQFKTGLMSV IKQKLAKKEG ARIDRNRDIE
RLWEFYQQYK RRHKVDDIRR EEQKWRESGA VTANLGELGL RFSEMRKVFA TLRAVVEVME
SLSKDAPPDG VGRLITEELR RIKKSDTTLS AELAPYNIVP LEAPSLTNAI GFFPEVQGAI
SAIKYTEQFP QLPAVFDNSG QRDMDMFDLL EYVFGFQKDN IRNQRENVIL IVANAQSGLG
IPVEADPKID ENVITEVFLK VLDNYIKWCR YLRIRLVWNK LEAINRDRKL FLVSLYFCIW
GEAANVRFLP ECICYIFHHM ARELDAILDR GEASPAPSCI GENQSVSFLE QIICPIYETI
AAEAARNNNG KAAHSKWRNY DDFNEYFWSP ACFELGWPFK KESSFLRKPP KKGRRTGKST
FVEHRTFLHL YRSFHRLWIF LVVMFQALTI IAFSNEKINL DTFKKLLSVG PTFAVMNFIE
SSLDVLLMFG AYSTARGMAI SRIVIRFFWT GVSSAFVIYV YLKLLEERDT NKDFYFRLYI
LVLGVYAGIR IVFALLTKLP ACHTLSEMSD QSFFQFFKWI YQIKPLVGPT KMIRRMPALP
YSWHDFISKN NNHILTIVSL WAPVVAIYLM DIHIWYTLLS AIVGGVMGAR ARLGEIRSIE
MVHKRFESFP EAFVKNLVSP QTKRTPIDRQ LSETSQDNNK VYAALFSPFW NEIIKSLREE
DYVSNREMDL LSMPSNTGSL RLVQWPLFLL CSKILLAIDL ALDCKDTQGD LWTRISRDEY
MAYAVQECYY SIEKILYSLV DGEGRLWVER IYREINNSIM EGSLVITLSL KKLPVVLSRF
TALTGLLIRN ETPELSKGAA KAMYDLYEVV SDDLLSSDLR EQLGTWNILA RARNEGRLFS
RVEWPRDPEI KEQVKRLHLL LTVKDSAANI PKNLEARRRL EFFTNSLFMD MPSAKPVSEM
MPFCVFTPYY SETVLYSSSD LRVENEDGIS TLFYLQKIFP DGASKLHLVQ WEKKTTTENW
GGLGVKDLRR SDLTVENLKK RKFICISRRF LCKETSEDVD LVLHCSSTSR LWWDMFSWFG
IYWMMPRSVK DTLSCWKFGK NRRKCRAWNV VPLALMWIVW CERNRGLLKV
//
