ID AMPD2_RAT Reviewed; 824 AA. AC Q02356; B2GUT6; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 2. DT 24-JAN-2024, entry version 152. DE RecName: Full=AMP deaminase 2 {ECO:0000305}; DE EC=3.5.4.6; DE AltName: Full=AMP deaminase isoform L; GN Name=Ampd2 {ECO:0000312|RGD:2110}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 632-719. RC TISSUE=Brain; RX PubMed=2365682; DOI=10.1016/s0021-9258(19)38422-4; RA Morisaki T., Sabina R.L., Holmes E.W.; RT "Adenylate deaminase. A multigene family in humans and rats."; RL J. Biol. Chem. 265:11482-11486(1990). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-135, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism. CC Catalyzes the deamination of AMP to IMP and plays an important role in CC the purine nucleotide cycle (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from AMP: step 1/1. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. {ECO:0000305}. 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; BC166402; AAI66402.1; -; mRNA. DR EMBL; M38126; AAA40728.1; -; Genomic_DNA. DR PIR; A37056; A37056. DR RefSeq; NP_001095151.1; NM_001101681.2. DR AlphaFoldDB; Q02356; -. DR SMR; Q02356; -. DR STRING; 10116.ENSRNOP00000026051; -. DR BindingDB; Q02356; -. DR iPTMnet; Q02356; -. DR PhosphoSitePlus; Q02356; -. DR jPOST; Q02356; -. DR PaxDb; 10116-ENSRNOP00000026051; -. DR Ensembl; ENSRNOT00000026051.6; ENSRNOP00000026051.5; ENSRNOG00000019240.8. DR Ensembl; ENSRNOT00055035519; ENSRNOP00055028808; ENSRNOG00055020780. DR Ensembl; ENSRNOT00060044863; ENSRNOP00060037212; ENSRNOG00060025840. DR Ensembl; ENSRNOT00065040423; ENSRNOP00065032920; ENSRNOG00065023600. DR GeneID; 362015; -. DR KEGG; rno:362015; -. DR UCSC; RGD:2110; rat. DR AGR; RGD:2110; -. DR CTD; 271; -. DR RGD; 2110; Ampd2. DR eggNOG; KOG1096; Eukaryota. DR GeneTree; ENSGT00950000183011; -. DR InParanoid; Q02356; -. DR OMA; FHRKFPY; -. DR OrthoDB; 20951at2759; -. DR PhylomeDB; Q02356; -. DR TreeFam; TF300439; -. DR Reactome; R-RNO-74217; Purine salvage. DR UniPathway; UPA00591; UER00663. DR PRO; PR:Q02356; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000019240; Expressed in pancreas and 19 other cell types or tissues. DR ExpressionAtlas; Q02356; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003876; F:AMP deaminase activity; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046033; P:AMP metabolic process; ISO:RGD. DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD. DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD. DR GO; GO:0052652; P:cyclic purine nucleotide metabolic process; ISS:UniProtKB. DR GO; GO:0097009; P:energy homeostasis; ISO:RGD. DR GO; GO:0046039; P:GTP metabolic process; ISO:RGD. DR GO; GO:0006188; P:IMP biosynthetic process; ISO:RGD. DR GO; GO:0032264; P:IMP salvage; ISO:RGD. DR GO; GO:0009117; P:nucleotide metabolic process; ISO:RGD. DR GO; GO:0072015; P:podocyte development; ISO:RGD. DR CDD; cd01319; AMPD; 1. DR Gene3D; 4.10.800.20; -; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR006329; AMPD. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01429; AMP_deaminase; 1. DR PANTHER; PTHR11359; AMP DEAMINASE; 1. DR PANTHER; PTHR11359:SF3; AMP DEAMINASE 2; 1. DR Pfam; PF19326; AMP_deaminase; 1. DR PIRSF; PIRSF001251; AMP_deaminase_met; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. DR Genevisible; Q02356; RN. PE 1: Evidence at protein level; KW Hydrolase; Metal-binding; Methylation; Nucleotide metabolism; KW Phosphoprotein; Reference proteome; Zinc. FT CHAIN 1..824 FT /note="AMP deaminase 2" FT /id="PRO_0000194409" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 655 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104" FT BINDING 364 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 435..440 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 633 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 636 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 710 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 711..714 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 44 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9DBT5" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 90 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9DBT5" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 133 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q01433" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q01433" SQ SEQUENCE 824 AA; 94787 MW; 3076B550E17AF95C CRC64; MASYPGPGKS KAKYPFKKRA SLQASAAAPE ARSGLGASPL QSARSLPGTA PCLKHFPLDL RTSMDGKCKE IAEELFSRSL AESELRSAPY EFPEESPIEQ LEERRQRLER QISQDVKLEP DILLRAKQDF LKTDSDSDLQ LYKEQGEGQG DRGLWERDVV LEREFQRVII SGEEKCGVPF TDLLDAAKSV VRALFIREKY MALSLQSFCP TTRRYLQQLA EKPLETRTYE QSPDTPVSAD APVHPPALEQ HPYEHCEPST MPGDLGLGLR MVRGVVHVYT RRDPDEHCPE VELPYPDLQE FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV PHRDFYNIRK VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ TLREVFESMN LTAYDLSVDT LDVHADRNTF HRFDKFNAKY NPIGESVLRE IFIKTDNKIS GKYFAHIIKE VMSDLEESKY QNAELRLSIY GRSRDEWDKL ARWAVNHRVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML ENIFLPLFEA TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA ENISHGLLLR KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS RGLMVSLSTD DPLQFHFTKE PLMEEYSIAT QVWKLSSCDM CELARNSVLM SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN VPDIRVGYRY ETLCQELALI TQAVQSEMLE TIPEEVGIVM SPGP //