UAP1_MOUSE
ID UAP1_MOUSE Reviewed; 522 AA.
AC Q91YN5; Q8BG76; Q8BXD6; Q8VD59;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=UDP-N-acetylhexosamine pyrophosphorylase;
DE Includes:
DE RecName: Full=UDP-N-acetylgalactosamine pyrophosphorylase;
DE EC=2.7.7.83;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
GN Name=Uap1;
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 AGX1 AND 3), AND VARIANT
RP HIS-366.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and 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] (ISOFORMS AGX2 AND 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (AGX2) from
RT Mus musculus.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Converts UTP and GlcNAc-1-P into UDP-GlcNAc, and UTP and
CC GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher
CC activity towards GalNAc-1-P, while isoform AGX2 has 8 times more
CC activity towards GlcNAc-1-P (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-galactosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:34363, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:61970, ChEBI:CHEBI:67138; EC=2.7.7.83;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC -!- SUBUNIT: Monomer and homodimer. Isoform AGX1 is a homodimer. Isoform
CC AGX2 is a monomer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=AGX2;
CC IsoId=Q91YN5-1; Sequence=Displayed;
CC Name=AGX1;
CC IsoId=Q91YN5-2; Sequence=VSP_014525;
CC Name=3;
CC IsoId=Q91YN5-3; Sequence=VSP_014524;
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; AK047566; BAC33089.1; -; mRNA.
DR EMBL; AK049519; BAC33791.1; -; mRNA.
DR EMBL; AK081690; BAC38294.1; -; mRNA.
DR EMBL; BC016406; AAH16406.1; -; mRNA.
DR EMBL; BC017547; AAH17547.1; -; mRNA.
DR CCDS; CCDS15467.1; -. [Q91YN5-3]
DR CCDS; CCDS83631.1; -. [Q91YN5-2]
DR CCDS; CCDS83632.1; -. [Q91YN5-1]
DR RefSeq; NP_001291974.1; NM_001305045.1.
DR RefSeq; NP_001291975.1; NM_001305046.1.
DR RefSeq; NP_598567.2; NM_133806.5.
DR RefSeq; XP_006496670.1; XM_006496607.3.
DR RefSeq; XP_006496671.2; XM_006496608.3.
DR PDB; 1VM8; X-ray; 2.50 A; A/B=1-522.
DR PDBsum; 1VM8; -.
DR AlphaFoldDB; Q91YN5; -.
DR SMR; Q91YN5; -.
DR BioGRID; 223459; 2.
DR STRING; 10090.ENSMUSP00000106983; -.
DR iPTMnet; Q91YN5; -.
DR PhosphoSitePlus; Q91YN5; -.
DR EPD; Q91YN5; -.
DR jPOST; Q91YN5; -.
DR MaxQB; Q91YN5; -.
DR PaxDb; Q91YN5; -.
DR PeptideAtlas; Q91YN5; -.
DR PRIDE; Q91YN5; -.
DR ProteomicsDB; 298168; -. [Q91YN5-1]
DR ProteomicsDB; 298169; -. [Q91YN5-2]
DR ProteomicsDB; 298170; -. [Q91YN5-3]
DR DNASU; 107652; -.
DR GeneID; 107652; -.
DR KEGG; mmu:107652; -.
DR UCSC; uc007dlw.2; mouse. [Q91YN5-3]
DR UCSC; uc007dly.2; mouse. [Q91YN5-2]
DR CTD; 6675; -.
DR MGI; MGI:1334459; Uap1.
DR eggNOG; KOG2388; Eukaryota.
DR InParanoid; Q91YN5; -.
DR PhylomeDB; Q91YN5; -.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00533.
DR BioGRID-ORCS; 107652; 0 hits in 59 CRISPR screens.
DR ChiTaRS; Uap1; mouse.
DR EvolutionaryTrace; Q91YN5; -.
DR PRO; PR:Q91YN5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91YN5; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0052630; F:UDP-N-acetylgalactosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; ISO:MGI.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; ISO:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..522
FT /note="UDP-N-acetylhexosamine pyrophosphorylase"
FT /id="PRO_0000185768"
FT MOTIF 108..111
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 303..304
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT BINDING 108..111
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 122
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 196
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 222
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 377
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 454..470
FT /note="Missing (in isoform AGX1)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014525"
FT VAR_SEQ 454
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014524"
FT VARIANT 366
FT /note="Y -> H (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:16141072"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 135..154
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 325..334
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 382..388
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 418..435
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1VM8"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1VM8"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:1VM8"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:1VM8"
SQ SEQUENCE 522 AA; 58609 MW; 121B4ACCCDDD43B5 CRC64;
MNVNDLKQRL SQAGQEHLLQ FWNELSEAQQ VELYMELQAM NFEELNSFFR KAIGEFDRSS
HQEKVDARME PVPRQVLGSA TRDQEQLQAW ESEGLSQISQ NKVAVLLLAG GQGTRLGVSY
PKGMYDVGLP SHKTLFQIQA ERILKLQQLA EKHHGNKCTI PWYIMTSGRT MESTKEFFTK
HKFFGLKKEN VVFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME
QRGICSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ
VVEYSEISLA TAQRRSSDGR LLFNAGNIAN HFFTVPFLKD VVNVYEPQLQ HHVAQKKIPY
VDSQGYFIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT
ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS EAITADVNHN LKDANDVPIQ
CEISPLISYA GEGLEGYVAD KEFHAPLIID ENGVHELVKN GI
