ALG12_MOUSE
ID ALG12_MOUSE Reviewed; 486 AA.
AC Q8VDB2; Q3UQK8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
DE EC=2.4.1.260;
DE AltName: Full=Asparagine-linked glycosylation protein 12 homolog;
DE AltName: Full=Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase;
DE AltName: Full=Mannosyltransferase ALG12 homolog;
GN Name=Alg12;
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 [MRNA].
RC STRAIN=FVB/N;
RX PubMed=12200473; DOI=10.1093/oxfordjournals.molbev.a004208;
RA Oriol R., Martinez-Duncker I., Chantret I., Mollicone R., Codogno P.;
RT "Common origin and evolution of glycosyltransferases using Dol-P-
RT monosaccharides as donor substrate.";
RL Mol. Biol. Evol. 19:1451-1463(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [3]
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).
CC -!- FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto
CC the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2))
CC required for protein glycosylation. {ECO:0000250}.
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)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
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->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
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 glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; AJ429133; CAD22101.1; -; mRNA.
DR EMBL; AK142322; BAE25031.1; -; mRNA.
DR EMBL; AC117700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49694.1; -.
DR RefSeq; NP_001135829.1; NM_001142357.1.
DR RefSeq; NP_663452.1; NM_145477.2.
DR RefSeq; XP_006520905.1; XM_006520842.2.
DR AlphaFoldDB; Q8VDB2; -.
DR STRING; 10090.ENSMUSP00000123935; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR iPTMnet; Q8VDB2; -.
DR PhosphoSitePlus; Q8VDB2; -.
DR EPD; Q8VDB2; -.
DR MaxQB; Q8VDB2; -.
DR PaxDb; Q8VDB2; -.
DR PRIDE; Q8VDB2; -.
DR ProteomicsDB; 296395; -.
DR Antibodypedia; 28215; 99 antibodies from 22 providers.
DR DNASU; 223774; -.
DR Ensembl; ENSMUST00000162183; ENSMUSP00000123935; ENSMUSG00000035845.
DR GeneID; 223774; -.
DR KEGG; mmu:223774; -.
DR UCSC; uc007xeo.2; mouse.
DR CTD; 79087; -.
DR MGI; MGI:2385025; Alg12.
DR VEuPathDB; HostDB:ENSMUSG00000035845; -.
DR eggNOG; KOG2516; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_008917_0_0_1; -.
DR InParanoid; Q8VDB2; -.
DR OMA; FTQYDHH; -.
DR OrthoDB; 330169at2759; -.
DR PhylomeDB; Q8VDB2; -.
DR TreeFam; TF314453; -.
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; 223774; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Alg12; mouse.
DR PRO; PR:Q8VDB2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VDB2; protein.
DR Bgee; ENSMUSG00000035845; Expressed in spermatid and 180 other tissues.
DR ExpressionAtlas; Q8VDB2; baseline and differential.
DR Genevisible; Q8VDB2; MM.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:InterPro.
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:0000009; F:alpha-1,6-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039485; ALG12.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF1; PTHR22760:SF1; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-
FT mannosyltransferase"
FT /id="PRO_0000215782"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 245
FT /note="W -> G (in Ref. 1; CAD22101)"
FT /evidence="ECO:0000305"
FT CONFLICT 476..485
FT /note="LVLLERLLRP -> AGTSRAAA (in Ref. 1; CAD22101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54543 MW; 011C1DA60919D0A3 CRC64;
MAGKKSSGKR SWPLLGLLVT VATIHLVICP YTKVEESFNL QATHDLLYHQ LDIDKYDHHE
FPGVVPRTFL GPLVIAAFSS PVVYVLSLLE VSKFYSQLIV RGVLGLGVIS GLWTLQKEVR
QQFGATVAVM FCWISATQFH LMFYCTRTLP NVLALAVVLP ALTAWLQRRW ALFVWLSAFV
IIGFRAELAM LLGIALLLTL YQRRLTVARV LRHAIPAGLL CLGLTVAVDS YFWRYLVWPE
GVVLWYNTVL NKSSNWGTSP LLWYFYSALP RGLGCSLLFI PLGAVDRRTY ALALPSLGFV
ALYSLLPHKE LRFIIYTFPV LNIMAARGCT YILNKKSWPY KVRAMLVTGH ILVNVAYTAT
SLYVSHFNYP GGVAMQQLHE LVPPQTDVLL HIDVAAAQTG VSRFLQVNDD WRYDKSEDVG
AAAMLNYTHI LMEAVPGHPA LYRDTHRVLA SIEGTTGISL NLMKLPPFDV NLQTKLVLLE
RLLRPA
