GL6D1_MACFA
ID GL6D1_MACFA Reviewed; 308 AA.
AC Q4R5T7; Q9BH00;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Glycosyltransferase 6 domain-containing protein 1;
DE EC=2.4.1.-;
GN Name=GLT6D1; ORFNames=QflA-10350, QtsA-20904;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RX PubMed=11806829; DOI=10.1186/gb-2001-3-1-research0006;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Prediction of unidentified human genes on the basis of sequence similarity
RT to novel cDNAs from cynomolgus monkey brain.";
RL Genome Biol. 3:RESEARCH0006.1-RESEARCH0006.5(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB055256; BAB21880.1; -; mRNA.
DR EMBL; AB169456; BAE01538.1; -; mRNA.
DR RefSeq; NP_001270822.1; NM_001283893.1.
DR AlphaFoldDB; Q4R5T7; -.
DR SMR; Q4R5T7; -.
DR STRING; 9541.XP_005580515.1; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GeneID; 101865068; -.
DR CTD; 360203; -.
DR eggNOG; ENOG502RU0J; Eukaryota.
DR OrthoDB; 1204439at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Glycosyltransferase 6 domain-containing protein 1"
FT /id="PRO_0000311972"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..308
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 82..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 173..175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 195..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="K -> R (in Ref. 1; BAE01538)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="V -> F (in Ref. 1; BAB21880)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="I -> T (in Ref. 1; BAB21880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 36420 MW; 94384DC1EF1BBE5E CRC64;
MNSKRMLLLV LFAFSLMLVE RYFRNHQVEE LRLSDWFHPR KRPDVITKTD WLAPIVWEGT
FDRQVLEKHY RRRNITVGLA VFATGRFAEE YLRLFLHSAN KHFMTGYRVI FYIMVDAFLQ
LPDIQPSPLR TFKAFEVDAE RWWLEGSLVY MKSLGEHITS HIQDEVDFLF SMAVNQVFQN
EFGVETLGPL VAQLHAWWYF RNTKNFPYER RPTSAASIPF GQGDFYYGSL MVGGTPRNIL
DFIEEYLNGV IHDIKNGLNS TYEKHLNKYF YLNKPTKLLS PEYSWDLAFS PPPQIQYVKV
AHDSHRKL