ID H9GIX0_ANOCA Unreviewed; 535 AA.
AC H9GIX0;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Alpha-1,3-glucosyltransferase {ECO:0000256|RuleBase:RU363110};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363110};
GN Name=ALG8 {ECO:0000313|Ensembl:ENSACAP00000012215.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000012215.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000012215.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000012215.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000012215.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
CC Evidence={ECO:0000256|ARBA:ARBA00034048};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU363110}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363110}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363110}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00008715, ECO:0000256|RuleBase:RU363110}.
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 RefSeq; XP_003226022.1; XM_003225974.3.
DR AlphaFoldDB; H9GIX0; -.
DR STRING; 28377.ENSACAP00000012215; -.
DR Ensembl; ENSACAT00000012465.4; ENSACAP00000012215.3; ENSACAG00000012469.4.
DR GeneID; 100567213; -.
DR KEGG; acs:100567213; -.
DR CTD; 79053; -.
DR eggNOG; KOG2576; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_022045_2_0_1; -.
DR InParanoid; H9GIX0; -.
DR OrthoDB; 5488939at2759; -.
DR TreeFam; TF315002; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000012469; Expressed in embryonic post-anal tail and 12 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IEA:Ensembl.
DR GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IEA:Ensembl.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR12413:SF2; DOLICHYL PYROPHOSPHATE GLC1MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE-RELATED; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU363110};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363110};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363110};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363110};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363110};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363110}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 197..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 244..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 370..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 440..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 470..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
FT TRANSMEM 498..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363110"
SQ SEQUENCE 535 AA; 61362 MW; 12ACE992167E52B4 CRC64;
MRGAACLAKK QTIMAAQRSD KLFLPVAFGV TLLKFLLIPT YHSTDFEVHR NWLAITHSLP
VSQWYYEATS EWTLDYPPFF AWFEYVLSHV AKYFDREMLV VQNLNYSSHE TIFFQRLSVI
FTDVLFIYAV HECCKCVNGK QGGKEPFENP SFVLSVLLLW NFGLLIVDHI HFQYNGFLFG
FMLLSIARLF QKRHLEGAFL FAILLHLKHI NLYVAPAYGM YLLRSYCFTA DNPDGSIRWR
KFNFLRLTAL GLIVCLVTAC SLGPFIVWGQ LPQVLSRLFP FKRGLCHAYW APNFWAIYSA
VDKALSVIGL KYKFLNPAEM PKAAMTGGLV QEFQHTVLPS VTPLATLVCT AIFMLPSVFC
LWFKPQGPRG FLRCLVLCAL TSFMFGWHVH EKAILLVILP LSLLSVEKSR DAGVYLILAT
TGHLSLFPLL FTAPELPIKI LLMLLFTVYS FSSLKTLFRK EGPLLNWLET LYLLGLLPLE
ILCEIVFPFT AWISKFPFLP LMLISVYCAL GIMYAWLKLY ISVFRGPLTF RQKKE
//
