ALG14_MOUSE
ID ALG14_MOUSE Reviewed; 217 AA.
AC Q9D081; Q8CEP2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=UDP-N-acetylglucosamine transferase subunit ALG14 homolog;
GN Name=Alg14;
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=Head;
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=C57BL/6J, and 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=Kidney, and Pancreas;
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: Involved in protein N-glycosylation. Essential for the second
CC step of the dolichol-linked oligosaccharide pathway. Anchors the
CC catalytic subunit ALG13 to the ER (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with ALG13 to form a functional enzyme.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P38242}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P38242}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the ALG14 family. {ECO:0000305}.
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DR EMBL; AK011733; BAB27807.1; -; mRNA.
DR EMBL; AK017354; BAC25513.1; -; mRNA.
DR EMBL; BC002278; AAH02278.1; -; mRNA.
DR CCDS; CCDS17801.1; -.
DR RefSeq; NP_077140.1; NM_024178.2.
DR AlphaFoldDB; Q9D081; -.
DR SMR; Q9D081; -.
DR STRING; 10090.ENSMUSP00000038387; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q9D081; -.
DR PhosphoSitePlus; Q9D081; -.
DR MaxQB; Q9D081; -.
DR PaxDb; Q9D081; -.
DR PeptideAtlas; Q9D081; -.
DR PRIDE; Q9D081; -.
DR ProteomicsDB; 296193; -.
DR Antibodypedia; 53384; 87 antibodies from 19 providers.
DR DNASU; 66789; -.
DR Ensembl; ENSMUST00000039442; ENSMUSP00000038387; ENSMUSG00000039887.
DR GeneID; 66789; -.
DR KEGG; mmu:66789; -.
DR UCSC; uc008rdx.1; mouse.
DR CTD; 199857; -.
DR MGI; MGI:1914039; Alg14.
DR VEuPathDB; HostDB:ENSMUSG00000039887; -.
DR eggNOG; KOG3339; Eukaryota.
DR GeneTree; ENSGT00390000002579; -.
DR HOGENOM; CLU_064541_2_0_1; -.
DR InParanoid; Q9D081; -.
DR OMA; GPGTCCI; -.
DR OrthoDB; 1449763at2759; -.
DR PhylomeDB; Q9D081; -.
DR TreeFam; TF105628; -.
DR Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR BioGRID-ORCS; 66789; 23 hits in 73 CRISPR screens.
DR PRO; PR:Q9D081; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D081; protein.
DR Bgee; ENSMUSG00000039887; Expressed in sciatic nerve and 240 other tissues.
DR ExpressionAtlas; Q9D081; baseline and differential.
DR Genevisible; Q9D081; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IBA:GO_Central.
DR InterPro; IPR013969; Oligosacch_biosynth_Alg14.
DR PANTHER; PTHR12154; PTHR12154; 1.
DR Pfam; PF08660; Alg14; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..217
FT /note="UDP-N-acetylglucosamine transferase subunit ALG14
FT homolog"
FT /id="PRO_0000265117"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P38242"
FT TRANSMEM 4..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38242"
SQ SEQUENCE 217 AA; 24429 MW; 471268EC8AF6BF15 CRC64;
MLSILILAAT AAGLVILLFQ RLWTVLGPHH VTPRESLRLL IVAGSGGHTT EILRLVGSLS
NAYSPRHYVI AESDEMSAKK IHSLEELSRA QNDSTTEYPK YHLHRIPRSR EVRQSWLSSV
FTTFYSMWFS FPLVLRIKPD LVLCNGPGTC VPICVSALLL GILGVKKVII VYVESICRVE
TLSLSGKILR HLSDYFIVQW PTLKEKYPKS VYLGRIV
