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   24-JAN-2024, entry version 131.
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; 10090-ENSMUSP00000095901; -.
DR   ProteomicsDB; 296194; -.
DR   Pumba; Q6P8H8; -.
DR   Antibodypedia; 31296; 121 antibodies from 20 providers.
DR   DNASU; 381903; -.
DR   Ensembl; ENSMUST00000098300.6; ENSMUSP00000095901.5; ENSMUSG00000035704.18.
DR   GeneID; 381903; -.
DR   KEGG; mmu:381903; -.
DR   UCSC; uc009ijc.2; mouse.
DR   AGR; MGI:2141959; -.
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; YHSTDFD; -.
DR   OrthoDB; 5488939at2759; -.
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; 22 hits in 80 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 229 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; 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; 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.
DR   Genevisible; Q6P8H8; MM.
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
//