ID M7AZW7_CHEMY Unreviewed; 484 AA.
AC M7AZW7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Hexosyltransferase {ECO:0000256|RuleBase:RU363063};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363063};
GN ORFNames=UY3_14189 {ECO:0000313|EMBL:EMP28695.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28695.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU363063}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000256|ARBA:ARBA00008661, ECO:0000256|RuleBase:RU363063}.
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DR EMBL; KB561123; EMP28695.1; -; Genomic_DNA.
DR AlphaFoldDB; M7AZW7; -.
DR eggNOG; KOG3864; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR Gene3D; 3.90.550.50; -; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11214:SF87; UDP-GLCNAC:BETAGAL BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE 8; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SMART; SM00367; LRR_CC; 2.
DR SUPFAM; SSF52047; RNI-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363063,
KW ECO:0000313|EMBL:EMP28695.1};
KW Golgi apparatus {ECO:0000256|RuleBase:RU363063};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMP28695.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 18..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 54726 MW; 55D024E19A43DEA9 CRC64;
MSRFRRCRAA AFGSTGLTVG AGPREADPRV GSQRPSPRPP GVSVMSLQQC RAFPRLLCAR
RPYSSATCPD PLKGGILQYL CNRFYDIEYL VGWSTKLRYR NLRRKNAYYG YTKETYGDNV
AAAYFVLSNR GRVRFQGQET WFCADRRGKY SSDFLQLRDV PVVAIDLSGS VLNYNGLDNL
VKLTALRSLD LSRCPHVDDW TLSRLHVFKD SLEELSLAGC PQVTERGLAC LHQLEHLRRL
DLSHLPSVPT PGLIRILVEE MLPQCEHQPD LRRLIAAESQ AYGDVLVWDF EDTFFNLTLK
DFLFLGWARA HCPDARFVLK GDDDVFINTP RVLAYLGALD TRRARALYTG QVMANASPFR
QASSKYYIPE SPASKYSIPE SFYAGPYPAY AGGGGYIFSG RLAPALFLLA QHVAFYPIDD
VYTGLCFQAL GVRAEAHPEF QTFDIAEKDR ADPCAHRQLL LVHQRSPQQT MQLWQQLRNP
QLKC
//