ID F7CUP3_MOUSE Unreviewed; 446 AA. AC F7CUP3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 2. DT 02-OCT-2024, entry version 64. DE SubName: Full=Amidohydrolase domain containing 2 {ECO:0000313|Ensembl:ENSMUSP00000122523.3}; GN Name=Amdhd2 {ECO:0000313|Ensembl:ENSMUSP00000122523.3, 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:ENSMUSP00000122523.3, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000122523.3, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523.3, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RG Mouse Genome Sequencing Consortium; 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:0007829|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:ENSMUSP00000122523.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523.3}; RX PubMed=21750661; RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N., RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D., RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L., RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J., RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P., RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G., RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.; RT "Modernizing reference genome assemblies."; RL PLoS Biol. 9:e1001091-e1001091(2011). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000122523.3} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000122523.3}; RG Ensembl; RL Submitted (JUN-2024) 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 AlphaFoldDB; F7CUP3; -. DR SMR; F7CUP3; -. DR jPOST; F7CUP3; -. DR PeptideAtlas; F7CUP3; -. DR ProteomicsDB; 318653; -. DR Ensembl; ENSMUST00000138685.3; ENSMUSP00000122523.3; ENSMUSG00000036820.13. DR AGR; MGI:2443978; -. DR MGI; MGI:2443978; Amdhd2. DR VEuPathDB; HostDB:ENSMUSG00000036820; -. DR GeneTree; ENSGT00390000012605; -. DR HOGENOM; CLU_2644422_0_0_1; -. DR UniPathway; UPA00629; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000036820; Expressed in right kidney and 182 other cell types or tissues. DR ExpressionAtlas; F7CUP3; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd00854; NagA; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR003764; GlcNAc_6-P_deAcase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1. DR PIRSF; PIRSF038994; NagA; 2. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 2. PE 1: Evidence at protein level; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F7CUP3, KW ECO:0007829|ProteomicsDB:F7CUP3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT ACT_SITE 338 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1" FT BINDING 187 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 198 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 276 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3" FT BINDING 279..280 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 287 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 316 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2" FT BINDING 372..374 FT /ligand="substrate" 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 //