ALG11_MOUSE
ID ALG11_MOUSE Reviewed; 492 AA.
AC Q3TZM9; Q6P7W8; Q8BL38;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE EC=2.4.1.131;
DE AltName: Full=Asparagine-linked glycosylation protein 11 homolog;
DE AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN Name=Alg11;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Embryo;
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 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Mannosyltransferase involved in the last steps of the
CC synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the
CC cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition
CC of the 4th and 5th mannose residues to the dolichol-linked
CC oligosaccharide chain (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TZM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TZM9-2; Sequence=VSP_026940;
CC Name=3;
CC IsoId=Q3TZM9-3; Sequence=VSP_026941;
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AK046475; BAC32746.1; -; mRNA.
DR EMBL; AK157746; BAE34179.1; -; mRNA.
DR EMBL; BC061469; AAH61469.1; -; mRNA.
DR CCDS; CCDS40292.1; -. [Q3TZM9-2]
DR CCDS; CCDS57613.1; -. [Q3TZM9-1]
DR RefSeq; NP_001230090.1; NM_001243161.1. [Q3TZM9-1]
DR RefSeq; NP_898965.1; NM_183142.4. [Q3TZM9-2]
DR AlphaFoldDB; Q3TZM9; -.
DR SMR; Q3TZM9; -.
DR STRING; 10090.ENSMUSP00000072382; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; Q3TZM9; -.
DR PhosphoSitePlus; Q3TZM9; -.
DR MaxQB; Q3TZM9; -.
DR PaxDb; Q3TZM9; -.
DR PeptideAtlas; Q3TZM9; -.
DR PRIDE; Q3TZM9; -.
DR ProteomicsDB; 296218; -. [Q3TZM9-1]
DR ProteomicsDB; 296219; -. [Q3TZM9-2]
DR ProteomicsDB; 296220; -. [Q3TZM9-3]
DR Antibodypedia; 49847; 215 antibodies from 19 providers.
DR DNASU; 207958; -.
DR Ensembl; ENSMUST00000072572; ENSMUSP00000072382; ENSMUSG00000063362. [Q3TZM9-1]
DR Ensembl; ENSMUST00000110737; ENSMUSP00000106365; ENSMUSG00000063362. [Q3TZM9-2]
DR GeneID; 207958; -.
DR KEGG; mmu:207958; -.
DR UCSC; uc009lcl.2; mouse. [Q3TZM9-2]
DR UCSC; uc009lcm.2; mouse. [Q3TZM9-1]
DR CTD; 440138; -.
DR MGI; MGI:2142632; Alg11.
DR VEuPathDB; HostDB:ENSMUSG00000063362; -.
DR eggNOG; KOG1387; Eukaryota.
DR GeneTree; ENSGT00550000075118; -.
DR HOGENOM; CLU_017896_2_0_1; -.
DR InParanoid; Q3TZM9; -.
DR OMA; RFNIHLH; -.
DR PhylomeDB; Q3TZM9; -.
DR TreeFam; TF313056; -.
DR BioGRID-ORCS; 207958; 26 hits in 73 CRISPR screens.
DR PRO; PR:Q3TZM9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TZM9; protein.
DR Bgee; ENSMUSG00000063362; Expressed in spermatocyte and 223 other tissues.
DR ExpressionAtlas; Q3TZM9; baseline and differential.
DR Genevisible; Q3TZM9; 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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase 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; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; PTHR45919; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /id="PRO_0000295617"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026941"
FT VAR_SEQ 93..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026940"
SQ SEQUENCE 492 AA; 55270 MW; E8347784DC963823 CRC64;
MAADTGSWCV YAVLRFFYSL FFPGLMICGV LCVYLVIGLW VIRWHLQRKK KSVSTSKNGK
EQTVVAFFHP YCNAGGGGER VLWCALRALQ KKYPEAVYVV YTGDINVSGQ QILDGAFRRF
NIKLAHPVQF VFLRKRYLVE DSRYPHFTLL GQSLGSILLG WEALMQRVPD VYIDSMGYAF
TLPLFKYVGG CRVGSYVHYP TISTDMLSVV KNQNPGFNNA AFISRNALLS KAKLIYYYLF
AFVYGLVGSC SDIVMVNSSW TLNHILSLWK VGHCTNIVYP PCDVQTFLDI PLHEKKVTPG
HLLVSIGQFR PEKNHALQIK AFAKLLNEKA AELGHSLKLV LIGGCRNKDD EFRVNQLRSL
SENLGVQENV EFKINISFDE LKNYLSEATI GLHTMWNEHF GIGVVECMAA GTVILAHNSG
GPKLDIVIPH EGQITGFLAE SEEGYADSMA HILSLSAEER LQIRKNARAS ISRFSDQEFE
VAFLCSMEKL LT
