ALG5_HUMAN
ID ALG5_HUMAN Reviewed; 324 AA.
AC Q9Y673; B4DR37; Q5TBA6;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase;
DE Short=DolP-glucosyltransferase;
DE EC=2.4.1.117;
DE AltName: Full=Asparagine-linked glycosylation protein 5 homolog;
GN Name=ALG5; ORFNames=HSPC149;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10359825; DOI=10.1073/pnas.96.12.6982;
RA Imbach T., Burda P., Kuhnert P., Wevers R.A., Aebi M., Berger E.G.,
RA Hennet T.;
RT "A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene
RT causes carbohydrate-deficient glycoprotein syndrome type-Ic.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6982-6987(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y673-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y673-2; Sequence=VSP_041019;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, placenta, liver, heart,
CC brain, kidney, skeletal muscle, and lung.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF102850; AAD41465.1; -; mRNA.
DR EMBL; AF161498; AAF29113.1; -; mRNA.
DR EMBL; AK299085; BAG61149.1; -; mRNA.
DR EMBL; AL138706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08578.1; -; Genomic_DNA.
DR EMBL; BC012531; AAH12531.1; -; mRNA.
DR CCDS; CCDS45033.1; -. [Q9Y673-2]
DR CCDS; CCDS9361.1; -. [Q9Y673-1]
DR PIR; T51776; T51776.
DR RefSeq; NP_001135836.1; NM_001142364.1. [Q9Y673-2]
DR RefSeq; NP_037470.1; NM_013338.4. [Q9Y673-1]
DR AlphaFoldDB; Q9Y673; -.
DR SMR; Q9Y673; -.
DR BioGRID; 118935; 53.
DR IntAct; Q9Y673; 14.
DR MINT; Q9Y673; -.
DR STRING; 9606.ENSP00000239891; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GlyGen; Q9Y673; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y673; -.
DR PhosphoSitePlus; Q9Y673; -.
DR SwissPalm; Q9Y673; -.
DR BioMuta; ALG5; -.
DR DMDM; 27734217; -.
DR EPD; Q9Y673; -.
DR jPOST; Q9Y673; -.
DR MassIVE; Q9Y673; -.
DR MaxQB; Q9Y673; -.
DR PaxDb; Q9Y673; -.
DR PeptideAtlas; Q9Y673; -.
DR PRIDE; Q9Y673; -.
DR ProteomicsDB; 86611; -. [Q9Y673-1]
DR ProteomicsDB; 86612; -. [Q9Y673-2]
DR Antibodypedia; 2385; 154 antibodies from 18 providers.
DR DNASU; 29880; -.
DR Ensembl; ENST00000239891.4; ENSP00000239891.3; ENSG00000120697.10. [Q9Y673-1]
DR Ensembl; ENST00000443765.6; ENSP00000390533.1; ENSG00000120697.10. [Q9Y673-2]
DR GeneID; 29880; -.
DR KEGG; hsa:29880; -.
DR MANE-Select; ENST00000239891.4; ENSP00000239891.3; NM_013338.5; NP_037470.1.
DR UCSC; uc001uvy.4; human. [Q9Y673-1]
DR CTD; 29880; -.
DR DisGeNET; 29880; -.
DR GeneCards; ALG5; -.
DR HGNC; HGNC:20266; ALG5.
DR HPA; ENSG00000120697; Low tissue specificity.
DR MIM; 604565; gene.
DR neXtProt; NX_Q9Y673; -.
DR OpenTargets; ENSG00000120697; -.
DR PharmGKB; PA134977026; -.
DR VEuPathDB; HostDB:ENSG00000120697; -.
DR eggNOG; KOG2977; Eukaryota.
DR GeneTree; ENSGT00940000153481; -.
DR HOGENOM; CLU_033536_9_1_1; -.
DR InParanoid; Q9Y673; -.
DR OMA; MVNTDAV; -.
DR OrthoDB; 1107630at2759; -.
DR PhylomeDB; Q9Y673; -.
DR TreeFam; TF314844; -.
DR PathwayCommons; Q9Y673; -.
DR Reactome; R-HSA-480985; Synthesis of dolichyl-phosphate-glucose.
DR SABIO-RK; Q9Y673; -.
DR SignaLink; Q9Y673; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 29880; 96 hits in 1087 CRISPR screens.
DR ChiTaRS; ALG5; human.
DR GenomeRNAi; 29880; -.
DR Pharos; Q9Y673; Tbio.
DR PRO; PR:Q9Y673; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y673; protein.
DR Bgee; ENSG00000120697; Expressed in parotid gland and 203 other tissues.
DR ExpressionAtlas; Q9Y673; baseline and differential.
DR Genevisible; Q9Y673; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; TAS:Reactome.
DR GO; GO:0004576; F:oligosaccharyl transferase activity; TAS:ProtInc.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
DR CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..324
FT /note="Dolichyl-phosphate beta-glucosyltransferase"
FT /id="PRO_0000059098"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 95..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041019"
SQ SEQUENCE 324 AA; 36946 MW; 44E1826BAB5B36CB CRC64;
MAPLLLQLAV LGAALAAAAL VLISIVAFTT ATKMPALHRH EEEKFFLNAK GQKETLPSIW
DSPTKQLSVV VPSYNEEKRL PVMMDEALSY LEKRQKRDPA FTYEVIVVDD GSKDQTSKVA
FKYCQKYGSD KVRVITLVKN RGKGGAIRMG IFSSRGEKIL MADADGATKF PDVEKLEKGL
NDLQPWPNQM AIACGSRAHL EKESIAQRSY FRTLLMYGFH FLVWFLCVKG IRDTQCGFKL
FTREAASRTF SSLHVERWAF DVELLYIAQF FKIPIAEIAV NWTEIEGSKL VPFWSWLQMG
KDLLFIRLRY LTGAWRLEQT RKMN
