ID A0A2H5PCA5_CITUN Unreviewed; 1978 AA.
AC A0A2H5PCA5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CUMW_123110 {ECO:0000313|EMBL:GAY49961.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY49961.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY49961.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(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:GAY49961.1}.
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DR EMBL; BDQV01000057; GAY49961.1; -; Genomic_DNA.
DR STRING; 55188.A0A2H5PCA5; -.
DR Proteomes; UP000236630; 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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF47; CALLOSE SYNTHASE 9; 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:UP000236630};
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 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 754..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1546..1568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1603..1621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1627..1648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1692..1710
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1716..1739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1792..1809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1821..1841
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1853..1877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1883..1904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1924..1945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 378..490
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1978 AA; 227546 MW; 4B69882EFC8E079E CRC64;
MIVTCQRFLR RVNYTNQTFQ KALAQLPSSC TTGCHRQLAA STQLLEKMSR VEDLWERLVR
AALRRERTGK DALGQPVSGI AGYVPSSLAN NRDIDAILRA ADEIQEEDPI CEHAYSLAQN
LDPNSEGRGV LQFKTGLMSV IKQKLAKREV GTIDRSQDVA RLQEFYKRYR EKNNVDKLRE
EEMLLRESGV FSGHLGELER KTVKRKRVFA TLKVLGMVLE QLTQEIPEEL KQVIDSDAAM
TDDLVAYNIV PLDAPTVANA IVSFPEVQAA VSALKYFGDL PRLPEDFPIP PSRNIDMLDF
LHFVFGFQKD NVSNQREHIV LLLANEQSRL GIPDENEPKL DEAAVQRVFM KSLDNYIKWC
DYLCIQPVWS SLEAVGKEKK ILFVSLYLLI WGEAANIRFL PECLCYIFHH MAREMDVILG
QQTAQPANSC TSENGVSFLD QVITPLYEVV AAEAANNDNG RAPHSAWRNY DDFNEYFWSL
HCFELSWPWR KSSSFFLKPT PRSKNLLNPG GGKRRGKTSF VEHRSFLHLY HSFHRLWIFL
VMMFQGLAII GFNDENINSK KFLREVLSLG PTYVVMKFFE SVLDVLMMYG AYSTSRRLAV
SRIFLRFIWF SFASVFITFL YVKGVQEDSK PNARSIIFRL YVIVIGIYAG FQFFLSCLMR
IPACHRLTNQ CDRWPLMRFI HWMREERYYV GRGMYERSTD FIKYMLFWLV ILSGKFSFAY
FLQIKPLVKP TRYIVDMDAV EYSWHDFVSR KTLIQFYVGG LLKNISVGNL VMSMLWPFSY
GVYLQYLPLK NVVPICMFFL LMPQIYLLDI YIFYTLMSAA YGFLLGARDR LGEIRSVEAV
HALFEEFPRA FMDTLHVPLP DRTSHPSSGQ AVEKKKFDAA RFSPFWNEII KNLREEDYIT
NLEMELLLMP KNSGSLLLVQ WPLFLLASKI FYAKDIAVEN RDSQDELWER ISRDEYMKYA
VEEFYHTLKF ILTETLEAEG RMVERIYDDI NVSVEKRSIH VDFQLTKLPL VISRVTALMG
VLKEAETPVL QKGAVQAVQD LYDVVRHDVL SINMRENYDT WNLLSKARTE GRLFSKLKWP
KDAELKAQVK RLHSLLTIKD SASNIPRNLE ARRRLEFFTN SLFMDMPPAK PAREIVFTPY
YSEIVLYSMD ELLKKNEDGI SILFYLQKIY PDEWKNFLSR IGRDENSQDT ELFDSPSDIL
ELRFWASYRA QTLARTVRGM MYYRKALMLQ AYLERMTSGD TEAALSSLDA SDTQGFELSR
EARAHADLKF TYVVTSQIYG KQKEDQKPEA ADIALLMQRN EALRVAFIDD VETLKDGKVH
REFYSKLVKG DINGKDKEIY SIKLPGNPKL GEGKPENQNH AVIFTRGNAI QTIDMNQDNY
FEEALKMRNL LEEFHADHGI RPPTILGVRE HVFTGSVSSL AYFMSNQETS FVTLGQRVLA
NPLKCRMHYG HPDVFDRVFH ITRGGISKAS RVINISEDIY AGFNTTLRQG NVTHHEYIQV
GKGRDVGLNQ IAVFEGKVAG GNGEQVLSRD VYRLGQLFDF FRMMSFYFTT VGYYFCTMLT
VLTVYAFLYG KTYLALSGVG EELQVRAQVT ENTALTAALN TQFLFQIGIF TAVPMVLGFI
LEQGFLAAVV NFITMQLQLC SVFFTFSLGT RTHYFGRTIL HGGARYQATG RGFVVRHIKF
SENYRLYSRS HFVKGLEVVL LLIVYIAYGY NEGGTLGYIL LSISSWFMAL SWLFAPYLFN
PSGFEWQKVV EDFRDWTNWL FYRGGIGVKG EESWEAWWDE ELSHIRTFSG RIAETILSLR
FFIFQYGIVY KLNIQGSDTS LTVYGLSWVV FAVLILLFKV FTFSQKISVN FQLLLRFIQG
LSLLVALAGL SVAVAITKLS IPDVFACILA FVPTGWGILC IASAWKPLMK KLGLWKSVRS
IARLYDAGMG MLIFIPIAMF SWFPFISTFQ TRLMFNQAFS RGLEISLILA GNNPNTEM
//
