ID ALG9_MOUSE Reviewed; 611 AA. AC Q8VDI9; Q8BT44; Q8C378; Q8C7G0; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Alpha-1,2-mannosyltransferase ALG9 {ECO:0000305}; DE EC=2.4.1.259 {ECO:0000250|UniProtKB:Q9H6U8}; DE EC=2.4.1.261 {ECO:0000250|UniProtKB:Q9H6U8}; DE AltName: Full=Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000305}; DE AltName: Full=Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase {ECO:0000305}; GN Name=Alg9 {ECO:0000312|MGI:MGI:1924753}; 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; TISSUE=Embryo, Head, Liver, and Ovary; 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]. 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). CC -!- FUNCTION: Catalyzes the transfer of mannose from Dol-P-Man to lipid- CC linked oligosaccharides. {ECO:0000250|UniProtKB:Q9H6U8}. 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->3)-alpha-D- CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc- CC diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha- CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man- CC (1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29531, CC Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628, CC Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, CC ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517; CC EC=2.4.1.259; Evidence={ECO:0000250|UniProtKB:Q9H6U8}; 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->2)-alpha-D- CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man- CC (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->2)-alpha-D-Man-(1->3)-[alpha-D-Man- CC (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:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, CC Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519, CC ChEBI:CHEBI:132520; EC=2.4.1.261; CC Evidence={ECO:0000250|UniProtKB:Q9H6U8}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000250|UniProtKB:Q9H6U8}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q9H6U8}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q9H6U8}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC39717.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK020231; BAC25619.1; -; mRNA. DR EMBL; AK050335; BAC34195.1; -; mRNA. DR EMBL; AK054293; BAC35720.1; -; mRNA. DR EMBL; AK086674; BAC39717.1; ALT_FRAME; mRNA. DR EMBL; BC021791; AAH21791.1; -; mRNA. DR CCDS; CCDS23175.1; -. DR RefSeq; NP_598742.1; NM_133981.2. DR AlphaFoldDB; Q8VDI9; -. DR STRING; 10090.ENSMUSP00000034561; -. DR CAZy; GT22; Glycosyltransferase Family 22. DR GlyCosmos; Q8VDI9; 3 sites, No reported glycans. DR GlyGen; Q8VDI9; 3 sites. DR iPTMnet; Q8VDI9; -. DR PhosphoSitePlus; Q8VDI9; -. DR SwissPalm; Q8VDI9; -. DR EPD; Q8VDI9; -. DR MaxQB; Q8VDI9; -. DR PaxDb; 10090-ENSMUSP00000034561; -. DR PeptideAtlas; Q8VDI9; -. DR ProteomicsDB; 296224; -. DR Pumba; Q8VDI9; -. DR DNASU; 102580; -. DR Ensembl; ENSMUST00000034561.11; ENSMUSP00000034561.5; ENSMUSG00000032059.14. DR GeneID; 102580; -. DR KEGG; mmu:102580; -. DR UCSC; uc009pkt.2; mouse. DR AGR; MGI:1924753; -. DR CTD; 79796; -. DR MGI; MGI:1924753; Alg9. DR VEuPathDB; HostDB:ENSMUSG00000032059; -. DR eggNOG; KOG2515; Eukaryota. DR GeneTree; ENSGT00950000183090; -. DR HOGENOM; CLU_018152_1_1_1; -. DR InParanoid; Q8VDI9; -. DR OMA; PRDMHAK; -. DR OrthoDB; 162888at2759; -. DR PhylomeDB; Q8VDI9; -. 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; 102580; 10 hits in 77 CRISPR screens. DR ChiTaRS; Alg9; mouse. DR PRO; PR:Q8VDI9; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q8VDI9; Protein. DR Bgee; ENSMUSG00000032059; Expressed in spermatocyte and 240 other cell types or tissues. DR ExpressionAtlas; Q8VDI9; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR InterPro; IPR005599; GPI_mannosylTrfase. DR PANTHER; PTHR22760:SF2; ALPHA-1,2-MANNOSYLTRANSFERASE ALG9; 1. DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1. DR Pfam; PF03901; Glyco_transf_22; 1. DR Genevisible; Q8VDI9; MM. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..611 FT /note="Alpha-1,2-mannosyltransferase ALG9" FT /id="PRO_0000215788" FT TOPO_DOM 1..135 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 136..156 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 157..171 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 193..213 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 214..234 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 235..249 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 250..270 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 271..310 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 311..331 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 332..342 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 343..363 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 364..370 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 371..391 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 392..405 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 406..426 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 427..611 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 77 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 550 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 593 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 8 FT /note="Q -> R (in Ref. 1; BAC34195)" FT /evidence="ECO:0000305" SQ SEQUENCE 611 AA; 69561 MW; 3C96FFC7854F0133 CRC64; MASRRARQRL KGGGGGGGGG GDAGPAAEKL EQLGSREAGA EPRPESGNKA GQVWAPEGST AFKCLLSARL CAALLSNISD CDETFNYWEP THYLIYGKGF QTWEYSPVYA IRSYAYLLLH AWPAAFHARI LQTNKILVFY FLRCLLAFVS CVCELYFYKA VCKKFGLHVS RMMLAFLVLS TGMFCSSSAF LPSSFCMYTT LIAMTGWYMD KTPIAVLGVA AGAILGWPFS AALGLPIAFD LLARKHRWKS FLLWSLVALA LFLVPVVVID SYYYGKLVVA PLNIVLYNVF TSHGPDLYGT EPWYFYLING FLNFNVAFAL ALLVLPLTFL MEYLLQRFHV QNLGHPYWLT LAPMYIWFII FFIQPHKEER FLFPVYPLIC LCGAVALSAL QKCYHFVFQR YRLEHYTVTS NWLALGTVFL FGLLSFSRSV ALFRGYHGPL DLYPEFYRIA TDPTIHTVPE GRPVNVCVGK EWYRFPSSFL LPDNWQLQFI PSEFRGQLPK PFAEGPLATR TVPTHMNDQN REEPSRYIDI SKCHYLVDLD TMRETPREPN YSSHREEWVS LAHRPFLDAS RSSKLLRAFY VPFLSDQYTV YVNYTILKPR KAKPSRKKSG G //