UGT2_DACCO
ID UGT2_DACCO Reviewed; 515 AA.
AC A0A291PQH4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=UDP-glucosyltransferase 2 {ECO:0000303|PubMed:29215010};
DE Short=DcUGT2 {ECO:0000303|PubMed:29215010};
DE EC=2.4.1.- {ECO:0000269|PubMed:29215010};
DE Flags: Precursor;
GN Name=UTG2 {ECO:0000303|PubMed:29215010};
OS Dactylopius coccus (Cochineal).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Coccoidea;
OC Dactylopiidae; Dactylopius.
OX NCBI_TaxID=765876 {ECO:0000312|EMBL:ATL15304.1};
RN [1] {ECO:0000312|EMBL:ATL15304.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP GLYCOSYLATION.
RX PubMed=29215010; DOI=10.1038/s41467-017-02031-z;
RA Kannangara R., Siukstaite L., Borch-Jensen J., Madsen B., Kongstad K.T.,
RA Staerk D., Bennedsen M., Okkels F.T., Rasmussen S.A., Larsen T.O.,
RA Frandsen R.J.N., Moeller B.L.;
RT "Characterization of a membrane-bound C-glucosyltransferase responsible for
RT carminic acid biosynthesis in Dactylopius coccus Costa.";
RL Nat. Commun. 8:1987-1987(2017).
CC -!- FUNCTION: Membrane-bound UDP-glucosyltransferase (UGT) which catalyzes
CC the C-glucosylation of kermesate and flavokermesate to produce
CC carminate and flavokermesate 7-C-beta-D-glucoside (dcll) respectively
CC (PubMed:29215010). Carminate is used as a deterrent against insect
CC predators (PubMed:29215010). {ECO:0000269|PubMed:29215010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=kermesate + UDP-alpha-D-glucose = carminate + 2 H(+) + UDP;
CC Xref=Rhea:RHEA:63752, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:149530, ChEBI:CHEBI:149531;
CC Evidence={ECO:0000269|PubMed:29215010};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63753;
CC Evidence={ECO:0000269|PubMed:29215010};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=flavokermesate + UDP-alpha-D-glucose = flavokermesate 7-C-
CC beta-D-glucoside + 2 H(+) + UDP; Xref=Rhea:RHEA:63756,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:149532, ChEBI:CHEBI:149533;
CC Evidence={ECO:0000269|PubMed:29215010};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63757;
CC Evidence={ECO:0000269|PubMed:29215010};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29215010}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Localization to the endoplasmic reticulum membrane
CC is critical for its activity. {ECO:0000269|PubMed:29215010}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult female.
CC {ECO:0000269|PubMed:29215010}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:29215010}.
CC -!- MISCELLANEOUS: Carminate, also known as cochineal dye, is used as a
CC fabric and cosmetics dye and as a natural food coloring.
CC {ECO:0000269|PubMed:29215010}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KY860725; ATL15304.1; -; mRNA.
DR AlphaFoldDB; A0A291PQH4; -.
DR SMR; A0A291PQH4; -.
DR BioCyc; MetaCyc:MON-21278; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016053; P:organic acid biosynthetic process; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..515
FT /note="UDP-glucosyltransferase 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5012109561"
FT TOPO_DOM 21..471
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29215010"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29215010"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 515 AA; 59115 MW; 5AD104249577AC1A CRC64;
MEFRLLILAL FSVLMSTSNG AEILALFPIH GISNYNVAEA LLKTLANRGH NVTVVTSFPQ
KKPVPNLYEI DVSGAKGLAT NSIHFERLQT IIQDVKSNFK NMVRLSRTYC EIMFSDPRVL
NIRDKKFDLV INAVFGSDCD AGFAWKSQAP LISILNARHT PWALHRMGNP SNPAYMPVIH
SRFPVKMNFF QRMINTGWHL YFLYMYFYYG NGEDANKMAR KFFGNDMPDI NEMVFNTSLL
FVNTHFSVDM PYPLVPNCIE IGGIHVKEPQ PLPLEIQKFM DEAEHGVIFF TLGSMVRTST
FPNQTIQAFK EAFAELPQRV LWKFENENED MPSNVLIRKW FPQNDIFGHK NIKAFISHGG
NSGALEAVHF GVPIIGIPLF YDQYRNILSF VKEGVAVLLD VNDLTKDNIL SSVRTVVNDK
SYSERMKALS QLFRDRPMSP LDTAVYWTEY VIRHRGAHHL KTAGAFLHWY QYLLLDVITF
LLVTFCAFCF IVKYICKALI HHYWSSSKSE KLKKN
