UGT5_DACCO
ID UGT5_DACCO Reviewed; 526 AA.
AC A0A291PQF1;
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 UGT5 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=UDP-glucosyltransferase 5 {ECO:0000303|PubMed:29215010};
DE Short=DcUGT5 {ECO:0000303|PubMed:29215010};
GN Name=UGT5 {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:ATL15306.1};
RN [1] {ECO:0000312|EMBL:ATL15306.1}
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; KY860727; ATL15306.1; -; mRNA.
DR AlphaFoldDB; A0A291PQF1; -.
DR SMR; A0A291PQF1; -.
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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="UDP-glycosyltransferase UGT5"
FT /id="PRO_0000450687"
FT TOPO_DOM 1..474
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 526 AA; 60071 MW; CA8E44327A7D8853 CRC64;
MIFFYFLTLT SFISVAFSYN ILGVFPFQAK SHFGFIDPLL VRLAELGHNV TIYDPYPKSE
KLPNYNEIDV SECFVFNTLY EEIDTFIKTA ASPFSSLWYS FEETLAVFQK ENFDKCAPLR
ELLNSTVKYD LLITETFLTD ITLLFVNKFK IPFITSTPNV PFPWLADRMG NPLNPSYIPN
LFSDYPFDKM TFFNRLWNTL FYVMALGGHN AIILKNEEKI NKYYFGSSVP SLYNIARETS
IMLINAHETL NPVIPLVPGM IPVSGIHIKQ PAALPQNIEK FINESTHGVV YFCMGSLLRG
ETFPAEKRDA FLYAFSKIPQ RVLWKWEGEV LPGKSENIMT SKWMPQRDIL AHPNVKLFIS
HGGLLGTSEA VYEGVPVIGI PIFGDQRTNI KALEANGAGE LLDYNDISGE VVLEKIQRLI
NDPKYKESAR QLSIRYKDRP MSPLDTAVYW TEYVIRHKGA PHLKTAAVDM PWYQYLLLDV
IAFLIFILVS VILIIYYGVK ISLRYLCALI FGNSSSLKPT KKVKDN