ALG3_MOUSE
ID ALG3_MOUSE Reviewed; 438 AA.
AC Q8K2A8; E9QKP9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE EC=2.4.1.258;
DE AltName: Full=Asparagine-linked glycosylation protein 3 homolog;
DE AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
DE AltName: Full=Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase;
DE AltName: Full=Not56-like protein;
GN Name=Alg3; Synonyms=Not, Not56l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC linkage to Man5GlcNAc2-PP-Dol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-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:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC ChEBI:CHEBI:132516; EC=2.4.1.258;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 58 family.
CC {ECO:0000305}.
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DR EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031893; AAH31893.1; -; mRNA.
DR CCDS; CCDS37289.1; -.
DR RefSeq; NP_666051.2; NM_145939.2.
DR AlphaFoldDB; Q8K2A8; -.
DR BioGRID; 228994; 3.
DR STRING; 10090.ENSMUSP00000045272; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR PhosphoSitePlus; Q8K2A8; -.
DR EPD; Q8K2A8; -.
DR MaxQB; Q8K2A8; -.
DR PaxDb; Q8K2A8; -.
DR PeptideAtlas; Q8K2A8; -.
DR PRIDE; Q8K2A8; -.
DR ProteomicsDB; 296095; -.
DR Antibodypedia; 52417; 15 antibodies from 11 providers.
DR Ensembl; ENSMUST00000045918; ENSMUSP00000045272; ENSMUSG00000033809.
DR GeneID; 208624; -.
DR KEGG; mmu:208624; -.
DR UCSC; uc007yqe.2; mouse.
DR CTD; 10195; -.
DR MGI; MGI:1098592; Alg3.
DR VEuPathDB; HostDB:ENSMUSG00000033809; -.
DR eggNOG; KOG2762; Eukaryota.
DR GeneTree; ENSGT00390000013904; -.
DR HOGENOM; CLU_035382_3_0_1; -.
DR InParanoid; Q8K2A8; -.
DR OMA; PERYGIH; -.
DR OrthoDB; 774318at2759; -.
DR PhylomeDB; Q8K2A8; -.
DR TreeFam; TF105870; -.
DR Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 208624; 16 hits in 79 CRISPR screens.
DR ChiTaRS; Psen2; mouse.
DR PRO; PR:Q8K2A8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K2A8; protein.
DR Bgee; ENSMUSG00000033809; Expressed in otic placode and 244 other tissues.
DR ExpressionAtlas; Q8K2A8; baseline and differential.
DR Genevisible; Q8K2A8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; ISO:MGI.
DR GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR InterPro; IPR007873; Glycosyltransferase_ALG3.
DR PANTHER; PTHR12646; PTHR12646; 1.
DR Pfam; PF05208; ALG3; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..438
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000080567"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92685"
FT CONFLICT 354
FT /note="R -> H (in Ref. 2; AAH31893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 50186 MW; 2332C12F413C897F CRC64;
MAAGLRKRGQ PASVGQPAGI WKQWLQRAWQ ERYLLLREPR YTLLVASCLC IAEVGITFWV
IHRVAYTEID WKAYMAQVEG FINGTYDYTQ LQGDTGPLVY PAGFLYIFTG LFYATDRGTD
IPMAQNIFAV LYLVTLVLVF LIYHQTSKVP PFVFFFMCCA SYRVHSIFVL RLFNDPVAMA
LLFLSINLFL AQCWSWGCCC FSLAVSVKMN VLLFAPGLLF LLLTQFGFRG ALPKLAICAA
LQVVLGLPFL LENPIGYLSR SFDLGRQFLF QWTVNWRFLP ETIFLHRAFH LALLAAHLSL
LLLFALCRWH RTGESILALL KDPSKRKVPP QALTPNQIVS ILFTSNFIGI CFSRSLHYQF
YVWYFHTLPY LLWAMPARWL THLLRLLVLG LIELSWNTYP STSFSSAALH LCHAVVLLQL
WLSPESFPKS IQPSRKTH
