ID F7CUP3_MOUSE Unreviewed; 446 AA. AC F7CUP3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 2. DT 26-FEB-2020, entry version 43. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT 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 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 HOGENOM; CLU_2644422_0_0_1; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000036820; Expressed in bone marrow macrophage and 189 other tissues. 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 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 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT REGION 279..280 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT REGION 372..374 FT /note="Substrate binding" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT ACT_SITE 338 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1" FT METAL 187 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT METAL 255 FT /note="Divalent metal cation; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT METAL 276 FT /note="Divalent metal cation; via tele nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 198 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 287 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 316 FT /note="Substrate; via tele nitrogen" FT /evidence="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 //