ALG8_MOUSE
ID ALG8_MOUSE Reviewed; 526 AA.
AC Q6P8H8; E9Q3H5; Q3TKP5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase {ECO:0000250|UniProtKB:P40351};
DE EC=2.4.1.265 {ECO:0000250|UniProtKB:P40351};
DE AltName: Full=Asparagine-linked glycosylation protein 8 homolog;
DE AltName: Full=Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase {ECO:0000250|UniProtKB:P40351};
DE AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase {ECO:0000250|UniProtKB:P40351};
GN Name=Alg8 {ECO:0000303|PubMed:28375157, ECO:0000312|MGI:MGI:2141959};
GN Synonyms=Gm1089;
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 MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [5]
RP FUNCTION.
RX PubMed=28375157; DOI=10.1172/jci90129;
RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M.,
RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E.,
RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P.,
RA Torres V.E., Somlo S.;
RT "Isolated polycystic liver disease genes define effectors of polycystin-1
RT function.";
RL J. Clin. Invest. 127:1772-1785(2017).
CC -!- FUNCTION: Adds the second glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol before it is transferred
CC to the nascent peptide (By similarity). Required for PKD1/Polycystin-1
CC maturation and localization to the plasma membrane of the primary cilia
CC (PubMed:28375157). {ECO:0000250|UniProtKB:P40351,
CC ECO:0000269|PubMed:28375157}.
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:0000250|UniProtKB:P40351};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK166755; BAE38996.1; -; mRNA.
DR EMBL; AK166897; BAE39100.1; -; mRNA.
DR EMBL; AC155933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL16291.1; -; Genomic_DNA.
DR EMBL; BC061244; AAH61244.1; -; mRNA.
DR CCDS; CCDS52313.1; -.
DR RefSeq; NP_950200.2; NM_199035.2.
DR AlphaFoldDB; Q6P8H8; -.
DR SMR; Q6P8H8; -.
DR BioGRID; 238146; 1.
DR STRING; 10090.ENSMUSP00000095901; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR PhosphoSitePlus; Q6P8H8; -.
DR EPD; Q6P8H8; -.
DR MaxQB; Q6P8H8; -.
DR PaxDb; Q6P8H8; -.
DR PRIDE; Q6P8H8; -.
DR ProteomicsDB; 296194; -.
DR Antibodypedia; 31296; 114 antibodies from 20 providers.
DR DNASU; 381903; -.
DR Ensembl; ENSMUST00000098300; ENSMUSP00000095901; ENSMUSG00000035704.
DR GeneID; 381903; -.
DR KEGG; mmu:381903; -.
DR UCSC; uc009ijc.2; mouse.
DR CTD; 79053; -.
DR MGI; MGI:2141959; Alg8.
DR VEuPathDB; HostDB:ENSMUSG00000035704; -.
DR eggNOG; KOG2576; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_022045_2_0_1; -.
DR InParanoid; Q6P8H8; -.
DR OMA; WDTFVGA; -.
DR OrthoDB; 595382at2759; -.
DR PhylomeDB; Q6P8H8; -.
DR TreeFam; TF315002; -.
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; 381903; 20 hits in 73 CRISPR screens.
DR ChiTaRS; Alg8; mouse.
DR PRO; PR:Q6P8H8; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6P8H8; protein.
DR Bgee; ENSMUSG00000035704; Expressed in embryonic post-anal tail and 226 other tissues.
DR Genevisible; Q6P8H8; MM.
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:0000033; F:alpha-1,3-mannosyltransferase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR InterPro; IPR039487; ALG8.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Probable dolichyl pyrophosphate Glc1Man9GlcNAc2
FT alpha-1,3-glucosyltransferase"
FT /id="PRO_0000174163"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="A -> G (in Ref. 4; AAH61244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59535 MW; 5AB213946EF09D11 CRC64;
MAASGSATAG GHWFSALALG VTLLKCLLIP TYHSTDFEVH RNWLAITHSL PISQWYYEAT
SEWTLDYPPF FAWFEYALSH IAKYFDQEML NIHNLNYYSS RTLLFQRFSV ILTDALFVYA
VHECCKCIDG KRTGKDLTEK PKFILSVLLL WNFGLLIVDH IHFQYNGFLS GLLLLSIARL
FQKRHIEGAL LFAVLLHLKH IYLYVAPAYG VYLLRSYCFT ASKPDGSVRW SSFSVVRVTS
LGLIVFLVSA LSLGPFLALN QLPQVFSRLF PFKRGLCHAY WAPNFWALYN ALDKVLSVIG
LKLKLLDPSQ IPRASMTSGL VQQFQHTVLP SVSPLATLIC TLIAILPSVF CLWFKPQGPR
GFLRCLVLCA LSSFMFGWHV HEKAILLAIL PMSLLSVEKA GDATVFLILA TTGHYSLFPL
LFTAPELPIK ILLMLLFTVY SISSLKTLFR KEKPLFNWME TVYLLGLGPL EVCCEFLLPF
TSWKLKYPFI PLLLTSVYCA VGITYAWTRL YASVLTGSLV SKTKKH
