ID F7CUP3_MOUSE Unreviewed; 446 AA. AC F7CUP3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 2. DT 03-JUL-2019, entry version 41. DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|Ensembl:ENSMUSP00000122523}; GN Name=Amdhd2 {ECO:0000313|Ensembl:ENSMUSP00000122523, GN ECO:0000313|MGI:MGI:2443978}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000122523, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000122523, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000122523} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523}; RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PIRSR:PIRSR038994-3}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000256|PIRSR:PIRSR038994-3}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT010502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MaxQB; F7CUP3; -. DR PeptideAtlas; F7CUP3; -. DR PRIDE; F7CUP3; -. DR Ensembl; ENSMUST00000138685; ENSMUSP00000122523; ENSMUSG00000036820. DR MGI; MGI:2443978; Amdhd2. DR eggNOG; KOG3892; Eukaryota. DR eggNOG; COG1820; LUCA. DR GeneTree; ENSGT00390000012605; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000036820; Expressed in 190 organ(s), highest expression level in bone marrow macrophage. DR ExpressionAtlas; F7CUP3; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:InterPro. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro. DR CDD; cd00854; NagA; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR003764; GlcNAc_6-P_deAcase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF038994; NagA; 2. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 2. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}; KW Proteomics identification {ECO:0000213|EPD:F7CUP3, KW ECO:0000213|MaxQB:F7CUP3, ECO:0000213|PeptideAtlas:F7CUP3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 309 424 Amidohydro-rel. {ECO:0000259|Pfam: FT PF01979}. FT REGION 279 280 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR038994-2}. FT REGION 372 374 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR038994-2}. FT ACT_SITE 338 338 Proton donor/acceptor. FT {ECO:0000256|PIRSR:PIRSR038994-1}. FT METAL 187 187 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR038994-3}. FT METAL 255 255 Divalent metal cation; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-3}. FT METAL 276 276 Divalent metal cation; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-3}. FT BINDING 198 198 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-2}. FT BINDING 287 287 Substrate. {ECO:0000256|PIRSR: FT PIRSR038994-2}. FT BINDING 316 316 Substrate; via tele nitrogen. FT {ECO:0000256|PIRSR:PIRSR038994-2}. SQ SEQUENCE 446 AA; 47179 MW; B1B866E612FAA566 CRC64; MRSGQCAAGA PVLQFTNCRI LRGGTLLRED LWVRGGRILD PEKLFFEERR VADEQRDCGG RILAPGFIDV QINGGFGVDF SKATEDVGSG VALVARRLLS HGVTSFCPTL VTSPPEVYHK AHSSSYKCAR SSWALPGRPC SCEPCPHAPS PPLCFPHAAG STGKVLPQIP VKSGGPHGAG VLGVHLEGPF ISREKRGAHP EAYLRSFEAN AFHDVLATYG PLDNVCIVTL APELDRSHEV IQALTAQGIR VSLGHSVADL RAAEVAVQSG ATFITHLFNA MLPFHHRDPG IVGLLTSDQL PPGHCIFYGM IADGIHTNPA ALRIAHRAHP QGLVLVTDAV PALGLGNGRH TLGQQEVEVD GLIAYIAGTK TLGGSIAPMD VCVRHFLQAT GCSVESALEA ASLHPAQMLG LEKTKGSLDF GADAAPPPVQ ITFLDGLSFL PGLSYE //