ID A0A175YES1_DAUCS Unreviewed; 1858 AA.
AC A0A175YES1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=DCAR_029596 {ECO:0000313|EMBL:KZM81983.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM81983.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM81983.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM81983.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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:KZM81983.1}.
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DR EMBL; LNRQ01000009; KZM81983.1; -; Genomic_DNA.
DR STRING; 79200.A0A175YES1; -.
DR EnsemblPlants; KZM81983; KZM81983; DCAR_029596.
DR Gramene; KZM81983; KZM81983; DCAR_029596.
DR OMA; CILALMP; -.
DR Proteomes; UP000077755; Chromosome 9.
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:SF48; CALLOSE SYNTHASE 3; 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:UP000077755};
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 482..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1425..1448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1468..1490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1502..1523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1589..1613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1667..1685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1697..1718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1730..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1761..1782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1802..1823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..438
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1858 AA; 214177 MW; 785E47DCFB60A775 CRC64;
MAYNRRGSDQ QQQQPPPPRR GLLRTQTAGN LGETMMDSEV VPSSLVEIAP ILRVANEVEP
SNPRVAYLCR FYAFEKAHKL DPTSSGRGVR QFKTALLQRL EREDKATIVG RKKSDAREMQ
NFYQHYYAKY IEALQNATDK ADRTRLTKAY QTAAVLFDVL KAVNLTESVD MADEIIEAHN
KVAEKAEIYV PYNILPLDSE SKNQAIMRYT EIQAAVQALR NTRGLPWSKG KKKKEDEDIL
DWLQAMFGFQ KDNVSNQREH LILLLANVHI RQLPKPEQQP VLDDRALTEV MKKLFKNYKG
WCKYLGRKSS LWLPNIQQDV QQRKLLYIGL YLLIWGEAAN LRFMPECLCY IYHHMAFELY
GMLAGNVSQM TGEHVKPAYG GDDEAFLRKV VTPIYNTIAE EARGSREEKS KHSRWRNYDD
LNEYFWSVDC FKLSWPMRAD ADFFCQPIGH LSIQKNNAMI IMAWSESGQP TSIFEDDGFK
KVLSLFITAA ILKFAQAVLD IIMSWKALHS MSAHVKLRYI LKAVFAAVWM IVLPVTYAYS
WSNTTGLAQT IRSWFGNGQS SPSLFVMAVL LYLFPNMLST LLFVFPFIRL RLEKSNNMIV
SLIMWWSQIK PLVGPTKAIM KVHVRNYQWH EFFPQAKNNI GVVISLWAPI ILVYFMDTQI
WYAIFSTILG GMYGAFRRLG EIRSLVMLRS RFQSLPGAFN NCLIPVENKE RPKKGLKSTL
SHKFPEFQIP SNKDKEAARF AQLWNQIITT FRDEDLISNS EKSLLLMPYW SNRDLDLIQW
PPFLLASKLP IALDMAKYSR GRHNDLIKRL ETDNYMRYAV IECYASCKNI INFLVLGERE
KLVLEEIFSK VDHHIHNADV ISGLNISSLP SLCDQLIRLI EYLKENNKDD KDNVVIVLQN
MLEVVTRDII TEDLIHSLVE SSHGGSYPVD EDEGMKPLSA QSQFFGKLNF PVTEETEAWM
EKIRRLHLLL TVKESAMDVP SNLEARRRMS FFSNSLFMDM PTAPKVRNML SFCALTPYYV
EDVLFSIKSL EKPNEDGVSI LFYLQKIYPD EWTNFLERVE RKNEEELKES LEMEDQLRLW
ASYRGQTLTK TVRGMMYYRQ ALELQAFLDM AKDDELMKGY KAAESNTEED LRNERSLLAQ
CQAVADMKFT YVVSCQQYGI HKRSRDPRAQ DILRLMTTYP SLRVAYVDEV EETNKGQTKN
KLKKVYYSVL VKAVPKSLDS AEPVQNLDEV IYRIKLPGPA ILGEGKPENQ NHALIFTRGE
GLQTIDMNQD NYMEEAFKMR NLLEEFLPRK NFQNDWNKDS EKRGFKNPTI LGFREHIFTG
SVSSLAWFMS NQETSFVTIG QRLLASPLKD LALYDSFNST LRGGNITHHE YIQVGKGRDV
GLNQISQFEA KIANGNGEQT MSRDIYRLGH RFDFFRMLSC YFTTIGFYFS NLITVLIVYV
FLYGRLYLVL SGLEEAMSKE PAIRDNKPLQ VALASQSFVQ IGYLMALPMV MEIGLEHGFS
KAFTDFVLMQ LQLAPIFFTF SLGTKTHYFG RTLLHGGAEY RGTGRGFVVF HAKFAENYRL
YSRSHFVKGI ELMVLLLVYH IFGRAYEGVL AYLLITISIW FMVGSWLFAP FLFNPSGFEW
QKIVEDWSDW KKWMLNRGGI GVSQEKSWES WWEKEQNHLK FSGARGIIVE ILLSLRFFIY
QYGLVYHLTF AKHSKSFLVY GLSWIVILVI LFVVKAVSVG RRKFSANFQL VFRMINGVIF
IISVAALITL VVLVDMQFRD IVVCILALMP SGWGLLLIAQ ALKPLVVKAG IWASVQTLAR
GYEMFMGLLL FTPVAFLAWF PFVSEFQTRM LFNQAFSRGL QISRILGGPE DKSSRNKE
//
