ALG9_MOUSE
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 03-AUG-2022, entry version 136.
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};
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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 GlyGen; Q8VDI9; 3 sites.
DR iPTMnet; Q8VDI9; -.
DR PhosphoSitePlus; Q8VDI9; -.
DR EPD; Q8VDI9; -.
DR MaxQB; Q8VDI9; -.
DR PaxDb; Q8VDI9; -.
DR PeptideAtlas; Q8VDI9; -.
DR PRIDE; Q8VDI9; -.
DR ProteomicsDB; 296224; -.
DR DNASU; 102580; -.
DR Ensembl; ENSMUST00000034561; ENSMUSP00000034561; ENSMUSG00000032059.
DR GeneID; 102580; -.
DR KEGG; mmu:102580; -.
DR UCSC; uc009pkt.2; mouse.
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; GKDWHRY; -.
DR OrthoDB; 1396421at2759; -.
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 72 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 237 other tissues.
DR ExpressionAtlas; Q8VDI9; baseline and differential.
DR Genevisible; Q8VDI9; 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: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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039484; ALG9-like.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF2; PTHR22760:SF2; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
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
