ALG1_MOUSE
ID ALG1_MOUSE Reviewed; 482 AA.
AC Q921Q3; Q3UKT8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.142 {ECO:0000250|UniProtKB:Q9BT22};
DE AltName: Full=Asparagine-linked glycosylation protein 1 homolog;
DE AltName: Full=Beta-1,4-mannosyltransferase;
DE AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN Name=Alg1 {ECO:0000312|MGI:MGI:2384774};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; 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=Testis;
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: Catalyzes the addition of the first of nine mannose moieties
CC to form a dolichol-lipid linked oligosaccharide intermediate required
CC for proper N-linked glycosylation. {ECO:0000250|UniProtKB:Q9BT22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC Evidence={ECO:0000250|UniProtKB:Q9BT22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13866;
CC Evidence={ECO:0000250|UniProtKB:Q9BT22};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9BT22}.
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=Q921Q3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921Q3-2; Sequence=VSP_032516;
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 33 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC011281; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK145871; BAE26713.1; -; mRNA.
DR EMBL; BC011281; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS49753.1; -. [Q921Q3-1]
DR RefSeq; NP_663337.2; NM_145362.2. [Q921Q3-1]
DR AlphaFoldDB; Q921Q3; -.
DR SMR; Q921Q3; -.
DR BioGRID; 228964; 3.
DR STRING; 10090.ENSMUSP00000097770; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR iPTMnet; Q921Q3; -.
DR PhosphoSitePlus; Q921Q3; -.
DR EPD; Q921Q3; -.
DR MaxQB; Q921Q3; -.
DR PaxDb; Q921Q3; -.
DR PeptideAtlas; Q921Q3; -.
DR PRIDE; Q921Q3; -.
DR ProteomicsDB; 296221; -. [Q921Q3-1]
DR ProteomicsDB; 296222; -. [Q921Q3-2]
DR DNASU; 208211; -.
DR Ensembl; ENSMUST00000049207; ENSMUSP00000046534; ENSMUSG00000039427. [Q921Q3-2]
DR Ensembl; ENSMUST00000100196; ENSMUSP00000097770; ENSMUSG00000039427. [Q921Q3-1]
DR GeneID; 208211; -.
DR KEGG; mmu:208211; -.
DR UCSC; uc007yby.2; mouse. [Q921Q3-1]
DR UCSC; uc012aba.2; mouse. [Q921Q3-2]
DR CTD; 56052; -.
DR MGI; MGI:2384774; Alg1.
DR VEuPathDB; HostDB:ENSMUSG00000039427; -.
DR eggNOG; KOG2941; Eukaryota.
DR GeneTree; ENSGT00390000008647; -.
DR HOGENOM; CLU_012079_0_0_1; -.
DR InParanoid; Q921Q3; -.
DR OMA; PLKVLWQ; -.
DR OrthoDB; 816895at2759; -.
DR PhylomeDB; Q921Q3; -.
DR TreeFam; TF314121; -.
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; 208211; 29 hits in 77 CRISPR screens.
DR ChiTaRS; Alg1; mouse.
DR PRO; PR:Q921Q3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q921Q3; protein.
DR Bgee; ENSMUSG00000039427; Expressed in right kidney and 240 other tissues.
DR Genevisible; Q921Q3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR InterPro; IPR026051; ALG1-like.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR13036; PTHR13036; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..482
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /id="PRO_0000080250"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..482
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BT22"
FT VAR_SEQ 70..96
FT /note="NSKPRDELLQNDRIRIVKLTDLRGLGA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032516"
FT CONFLICT 339..341
FT /note="QHV -> RHI (in Ref. 2; BC011281)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="G -> R (in Ref. 2; BC011281)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54417 MW; FA98A1062D8A53F6 CRC64;
MAASCVALLV LALLLLVLLL GLWKRGRQTG RARHMVVVVL GDVGRSPRMQ YHALSLAQSG
FSVTLLGFYN SKPRDELLQN DRIRIVKLTD LRGLGAGPRI LQYGVKVVFQ AVYLLWKMMR
MDPAAYIFLQ NPPGLPAIAV CWFVGCICGS KLVIDWHNYG YSIMGLVHGP RHPIVLLAKW
YEKFFGRLSH LNLCVTNAMR EDLAENWCVR AVTLYDKPAS FFKETPLDLQ HELFMKLSHT
YSPFQSCSDP SHPDTERSAF TERDCQSGVV RRLHGRPALL VSSTSWTEDE DFSILLRALE
KFEQQALTGD SLPSLVCVIT GKGPLREHYR HLISQKHLQH VRFCTPWLEA EDYPLLLGSA
DLGVCLHMSS SGLDLPMKVV DMFGCHLPVC AVNFKCLHEL VRHGENGLVF KDAEELAAQL
QMLFSKFPDP AGKLSQFRKK LQESGQQRWD ESWQHTVLPL LAHSQMTPRP HPPCGHPSCR
GF
