ID   AMPD3_RAT               Reviewed;         765 AA.
AC   O09178;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=AMP deaminase 3;
DE            EC=3.5.4.6 {ECO:0000269|PubMed:9291127};
DE   AltName: Full=AMP deaminase isoform E;
GN   Name=Ampd3;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=9291127; DOI=10.1042/bj3260521;
RA   Mahnke-Zizelman D.K., D'Cunha J., Wojnar J.M., Brogley M.A., Sabina R.L.;
RT   "Regulation of rat AMP deaminase 3 (isoform C) by development and skeletal
RT   muscle fibre type.";
RL   Biochem. J. 326:521-529(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP   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       {ECO:0000305|PubMed:9291127}.
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         Evidence={ECO:0000269|PubMed:9291127};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC         Evidence={ECO:0000305|PubMed:9291127};
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. {ECO:0000305|PubMed:9291127}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=O09178-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in adult tissues such as aorta, heart,
CC       kidney, lung, muscle and thyroid. Weakly expressed in thyroid and not
CC       detected in liver. {ECO:0000269|PubMed:9291127}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Adenosine and AMP deaminases family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53348.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; U90888; AAC53348.1; ALT_INIT; mRNA.
DR   RefSeq; NP_113732.1; NM_031544.1.
DR   AlphaFoldDB; O09178; -.
DR   SMR; O09178; -.
DR   BioGRID; 247167; 1.
DR   STRING; 10116.ENSRNOP00000024933; -.
DR   BindingDB; O09178; -.
DR   iPTMnet; O09178; -.
DR   PhosphoSitePlus; O09178; -.
DR   jPOST; O09178; -.
DR   PaxDb; O09178; -.
DR   PRIDE; O09178; -.
DR   DNASU; 25095; -.
DR   GeneID; 25095; -.
DR   KEGG; rno:25095; -.
DR   UCSC; RGD:2111; rat. [O09178-1]
DR   CTD; 272; -.
DR   RGD; 2111; Ampd3.
DR   eggNOG; KOG1096; Eukaryota.
DR   InParanoid; O09178; -.
DR   OrthoDB; 49756at2759; -.
DR   PhylomeDB; O09178; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   Reactome; R-RNO-74217; Purine salvage.
DR   UniPathway; UPA00591; UER00663.
DR   PRO; PR:O09178; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003876; F:AMP deaminase activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046032; P:ADP catabolic process; ISO:RGD.
DR   GO; GO:0046031; P:ADP metabolic process; ISO:RGD.
DR   GO; GO:0006196; P:AMP catabolic process; ISO:RGD.
DR   GO; GO:0046033; P:AMP metabolic process; ISO:RGD.
DR   GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR   GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR   GO; GO:0034101; P:erythrocyte 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   CDD; cd01319; AMPD; 1.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR006329; AMPD.
DR   InterPro; IPR029771; AMPD3.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR11359; PTHR11359; 1.
DR   PANTHER; PTHR11359:SF2; PTHR11359:SF2; 1.
DR   Pfam; PF19326; AMP_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..765
FT                   /note="AMP deaminase 3"
FT                   /id="PRO_0000194412"
FT   ACT_SITE        606
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         386..391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         584
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         587
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         661
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         662..665
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01432"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   765 AA;  88483 MW;  F826FA5966221B09 CRC64;
     MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPKDCPIG QKEAKERELQ
     KELAEQKSVE TAKRKKSFKM IRSQSMSLQM PTQDWKGPPS VSPAMSPTTP LVLGAASKPG
     LAPYDMPEYQ RATISGDYCA GITMEDYEQA AKSLAKALMI REKYARLAYH RFPRTTAQYL
     AHQGESVPLE EGLPDFHPPP LPQEDPYCLD DAPPNLGYLV RMQGGVLFVY DNQTMLERQE
     PHSLPYPDLE TYIVDMSHIL ALITDGPTKT YCHRRLNFLE SKFSLHEMLN EMSEFKELKS
     NPHRDFYNVR KVDTHIHAAA CMNQKHLLRF IKYTYQTEPD RTVAEKLGRK ITLRQVFDSL
     HMDPYDLTVD SLDVHAGRQT FHGFDKFNSK YNPVGASELR DLYLKTENYL GGEYFARMVK
     EVARELEDSK YQYSEPRLSI YGRSPKEWSS LARWFIQHKV YSPNMRWIIQ VPRIYDIFRS
     KKLLPSFGKM LENIFLPLFQ ATINPQDHRE LHLFLKYVTG FDSVDDESKH SDHMFSDKSP
     SPDLWTSEQN PPYSYYLYYM YANIMVLNNL RRERGLSTFL FRPHCGEAGS ITHLVSAFLT
     ADNISHGLLL KKSPVLQYLY YLAQIPIAMS PLSNNSLFLE YSKNPLREFL HKGLHVSLST
     DDPMQFHYTK EALMEEYAIA AQVWKLSTCD LCEIARNSVL QSGLSHQEKQ KFLGQNYYKE
     GPEGNDIRKT NVAQIRMAFR YETLCNELSF LSDAMKSEEI TALAD