UGT4_DACCO
ID UGT4_DACCO Reviewed; 504 AA.
AC A0A291PQG3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=UDP-glycosyltransferase UGT4 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=UDP-glucosyltransferase 4 {ECO:0000303|PubMed:29215010};
DE Short=DcUGT4 {ECO:0000303|PubMed:29215010};
DE Flags: Precursor;
GN Name=UGT4 {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:ATL15305.1};
RN [1] {ECO:0000312|EMBL:ATL15305.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
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: Catalyzes the transfer of a glycosyl group from a UDP-sugar
CC to an acceptor molecule. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:29215010};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:29215010}.
CC -!- DEVELOPMENTAL STAGE: Expressed in adult female.
CC {ECO:0000269|PubMed:29215010}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000255|RuleBase:RU003718}.
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DR EMBL; KY860726; ATL15305.1; -; mRNA.
DR AlphaFoldDB; A0A291PQG3; -.
DR SMR; A0A291PQG3; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Microsome; Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..504
FT /note="UDP-glycosyltransferase UGT4"
FT /evidence="ECO:0000255"
FT /id="PRO_5011814698"
FT TOPO_DOM 24..474
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 504 AA; 58644 MW; 645B014719B3F72E CRC64;
MTLLRDLLLL YINSLLFINP SIGENILVFL PTKTYSHFKP LEPLFQELAM RGHNVTVFSG
FSLTKNISNY SSIVFSAEIE FVNIGMGNLR KQSRIYNWIY VHNELQNYFT QLISDNQLQE
LLSNKDTQFD LIFIELYHVD GVFALSHRFN CPIIGLSFQP VLPIYNWLIG NPTTFSYIPH
VYLPFTDIMS FWKRIINAVF SIFTAAFYNF VSTKGYQKHV DLLLRQTESP KLNIEELSES
LSLILAEFHF SSAYTRPNLP NVIDIAGIHI QSPKPLPQDL LDFLDQSEHG VIYVSLGTLI
DPIHTDHLGL NLINVFRKLR QRVIWKWKKE FFHDVPKNVL IGEWFPQIDI LNHPRCKLFI
SHGGYHSMLE SIYSSVPILG IPFFTDQHHN TAIIEKLKIG KKASTEASEE DLLTAVKELL
SNETFKRNSQ HQSSIFRDRP MSPMDTAIYW TEYILRYKGA SHMKSAVIDL YWFQYILLDI
ILFYSLIVLI LLCILRIFFR MLTK