GNA1_MOUSE
ID GNA1_MOUSE Reviewed; 184 AA.
AC Q9JK38;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Glucosamine 6-phosphate N-acetyltransferase;
DE EC=2.3.1.4 {ECO:0000250|UniProtKB:Q96EK6};
DE AltName: Full=Phosphoglucosamine acetylase;
DE AltName: Full=Phosphoglucosamine transacetylase;
DE AltName: Full=Protein EMeg32;
GN Name=Gnpnat1; Synonyms=Gna1;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=10777580; DOI=10.1074/jbc.275.17.12821;
RA Boehmelt G., Fialka I., Brothers G., McGinley M.D., Patterson S.D.,
RA Rong M., Hui C.C., Chung S., Huber L.A., Mak T.W., Iscove N.N.;
RT "Cloning and characterization of the murine glucosamine-6-phosphate
RT acetyltransferase EMeg32: differential expression and intracellular
RT membrane association.";
RL J. Biol. Chem. 275:12821-12832(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Colon, Embryonic liver, Kidney, Pancreas, and Small intestine;
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 MRNA].
RC 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-
CC acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q96EK6};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC alpha-D-glucosamine 6-phosphate (route I): step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96EK6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10777580}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10777580}. Endosome membrane
CC {ECO:0000269|PubMed:10777580}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10777580}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Shows a strong differential expression
CC pattern in adult hematopoietic precursor cells.
CC {ECO:0000269|PubMed:10777580}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed at early stages of embryonic
CC development but is confined to bones, skin and the hematopoietic system
CC at later developmental stages. {ECO:0000269|PubMed:10777580}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ001006; CAA04463.1; -; mRNA.
DR EMBL; AK018499; BAB31241.1; -; mRNA.
DR EMBL; AK002466; BAB22120.1; -; mRNA.
DR EMBL; AK007647; BAB25161.1; -; mRNA.
DR EMBL; AK007722; BAB25212.1; -; mRNA.
DR EMBL; AK007764; BAB25240.1; -; mRNA.
DR EMBL; AK008566; BAB25749.1; -; mRNA.
DR EMBL; AK011098; BAB27395.1; -; mRNA.
DR EMBL; BC031116; AAH31116.1; -; mRNA.
DR CCDS; CCDS26976.1; -.
DR RefSeq; NP_062298.1; NM_019425.2.
DR RefSeq; XP_006519338.1; XM_006519275.2.
DR RefSeq; XP_006519339.1; XM_006519276.3.
DR AlphaFoldDB; Q9JK38; -.
DR SMR; Q9JK38; -.
DR BioGRID; 207615; 9.
DR IntAct; Q9JK38; 10.
DR STRING; 10090.ENSMUSP00000042860; -.
DR iPTMnet; Q9JK38; -.
DR PhosphoSitePlus; Q9JK38; -.
DR SwissPalm; Q9JK38; -.
DR EPD; Q9JK38; -.
DR jPOST; Q9JK38; -.
DR MaxQB; Q9JK38; -.
DR PaxDb; Q9JK38; -.
DR PeptideAtlas; Q9JK38; -.
DR PRIDE; Q9JK38; -.
DR ProteomicsDB; 271411; -.
DR Antibodypedia; 10869; 117 antibodies from 22 providers.
DR DNASU; 54342; -.
DR Ensembl; ENSMUST00000046191; ENSMUSP00000042860; ENSMUSG00000037722.
DR Ensembl; ENSMUST00000227468; ENSMUSP00000154084; ENSMUSG00000037722.
DR GeneID; 54342; -.
DR KEGG; mmu:54342; -.
DR UCSC; uc007tgp.1; mouse.
DR CTD; 64841; -.
DR MGI; MGI:1858963; Gnpnat1.
DR VEuPathDB; HostDB:ENSMUSG00000037722; -.
DR eggNOG; KOG3396; Eukaryota.
DR GeneTree; ENSGT00390000008666; -.
DR HOGENOM; CLU_072095_1_0_1; -.
DR InParanoid; Q9JK38; -.
DR OMA; NQRYDWI; -.
DR OrthoDB; 1479446at2759; -.
DR PhylomeDB; Q9JK38; -.
DR TreeFam; TF313790; -.
DR BioCyc; MetaCyc:MON-13176; -.
DR BRENDA; 2.3.1.4; 3474.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; Q9JK38; -.
DR UniPathway; UPA00113; UER00529.
DR BioGRID-ORCS; 54342; 14 hits in 78 CRISPR screens.
DR ChiTaRS; Gnpnat1; mouse.
DR PRO; PR:Q9JK38; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JK38; protein.
DR Bgee; ENSMUSG00000037722; Expressed in morula and 234 other tissues.
DR ExpressionAtlas; Q9JK38; baseline and differential.
DR Genevisible; Q9JK38; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006041; P:glucosamine metabolic process; ISO:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039143; GNPNAT1.
DR PANTHER; PTHR13355; PTHR13355; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endosome; Golgi apparatus; Membrane; Reference proteome;
KW Transferase.
FT CHAIN 1..184
FT /note="Glucosamine 6-phosphate N-acetyltransferase"
FT /id="PRO_0000074554"
FT DOMAIN 39..184
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 108..111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 130..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 165..167
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96EK6"
SQ SEQUENCE 184 AA; 20791 MW; C455BF12027BD8A9 CRC64;
MKPDETPMFD PSLLKEVDWS QNTAIFSPAI SPTHPGEGLV LRPLCTADLN KGFFKVLGQL
TETGVVSPEQ FMKSFEHMKK SGDYYVTVVE DVTLGQIVAT ATLIIEHKFI HSCAKRGRVE
DVVVSDECRG KQLGKLLLST LTLLSKKLNC YKITLECLPQ NVGFYKKFDY TVSEENYMCR
RFLK
