ID   AMPD1_RAT               Reviewed;         747 AA.
AC   P10759; P78501; Q6LDJ4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 152.
DE   RecName: Full=AMP deaminase 1 {ECO:0000305|PubMed:9133604};
DE            EC=3.5.4.6 {ECO:0000269|PubMed:11102975, ECO:0000269|PubMed:9133604};
DE   AltName: Full=AMP deaminase isoform M;
DE   AltName: Full=Myoadenylate deaminase;
GN   Name=Ampd1 {ECO:0000312|RGD:2109};
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], AND PROTEIN SEQUENCE OF 536-548.
RC   TISSUE=Muscle;
RX   PubMed=3624265; DOI=10.1016/s0021-9258(18)45213-1;
RA   Sabina R.L., Marquetant R., Desai N.M., Kaletha K., Holmes E.W.;
RT   "Cloning and sequence of rat myoadenylate deaminase cDNA. Evidence for
RT   tissue-specific and developmental regulation.";
RL   J. Biol. Chem. 262:12397-12400(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
RX   PubMed=2398891; DOI=10.1128/mcb.10.10.5271-5278.1990;
RA   Mineo I., Clarke P.R., Sabina R.L., Holmes E.W.;
RT   "A novel pathway for alternative splicing: identification of an RNA
RT   intermediate that generates an alternative 5' splice donor site not present
RT   in the primary transcript of AMPD1.";
RL   Mol. Cell. Biol. 10:5271-5278(1990).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   TISSUE=Heart;
RX   PubMed=9133604; DOI=10.1016/s0378-1119(96)00818-9;
RA   Wang X., Morisaki H., Sermsuvitayawong K., Mineo I., Toyama K.,
RA   Ogasawara N., Mukai T., Morisaki T.;
RT   "Cloning and expression of cDNA encoding heart-type isoform of AMP
RT   deaminase.";
RL   Gene 188:285-290(1997).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND MUTAGENESIS OF ARG-388 AND
RP   ARG-425.
RX   PubMed=11102975;
RX   DOI=10.1002/1098-1004(200012)16:6<467::aid-humu3>3.0.co;2-v;
RA   Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T.;
RT   "First missense mutations (R388W and R425H) of AMPD1 accompanied with
RT   myopathy found in a Japanese patient.";
RL   Hum. Mutat. 16:467-472(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81; SER-85; TYR-216 AND
RP   SER-441, AND 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       {ECO:0000305|PubMed:11102975, ECO:0000305|PubMed:9133604}.
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:11102975, ECO:0000269|PubMed:9133604};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778;
CC         Evidence={ECO:0000305|PubMed:11102975, ECO:0000305|PubMed:9133604};
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:11102975,
CC       ECO:0000305|PubMed:9133604}.
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; J02811; AAB54086.1; -; mRNA.
DR   EMBL; M58688; AAA40726.1; -; mRNA.
DR   PIR; A27366; A27366.
DR   RefSeq; NP_620231.1; NM_138876.1.
DR   AlphaFoldDB; P10759; -.
DR   SMR; P10759; -.
DR   STRING; 10116.ENSRNOP00000025248; -.
DR   BindingDB; P10759; -.
DR   iPTMnet; P10759; -.
DR   PhosphoSitePlus; P10759; -.
DR   PaxDb; 10116-ENSRNOP00000025248; -.
DR   Ensembl; ENSRNOT00000112496.1; ENSRNOP00000080039.1; ENSRNOG00000018656.7.
DR   Ensembl; ENSRNOT00060053124; ENSRNOP00060044173; ENSRNOG00060030572.
DR   Ensembl; ENSRNOT00065053698; ENSRNOP00065044144; ENSRNOG00065031130.
DR   GeneID; 25028; -.
DR   KEGG; rno:25028; -.
DR   AGR; RGD:2109; -.
DR   CTD; 270; -.
DR   RGD; 2109; Ampd1.
DR   eggNOG; KOG1096; Eukaryota.
DR   GeneTree; ENSGT00950000183011; -.
DR   HOGENOM; CLU_003782_4_0_1; -.
DR   InParanoid; P10759; -.
DR   OrthoDB; 20951at2759; -.
DR   PhylomeDB; P10759; -.
DR   TreeFam; TF300439; -.
DR   BRENDA; 3.5.4.6; 5301.
DR   Reactome; R-RNO-74217; Purine salvage.
DR   UniPathway; UPA00591; UER00663.
DR   PRO; PR:P10759; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000018656; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003876; F:AMP deaminase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032036; F:myosin heavy chain binding; IDA:RGD.
DR   GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR   GO; GO:0032263; P:GMP salvage; ISO:RGD.
DR   GO; GO:0006188; P:IMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032264; P:IMP salvage; ISO:RGD.
DR   GO; GO:0010033; P:response to organic substance; IDA: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:SF1; AMP DEAMINASE 1; 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; P10759; RN.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..747
FT                   /note="AMP deaminase 1"
FT                   /id="PRO_0000194405"
FT   ACT_SITE        594
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         575
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         649
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         650..653
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         81
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         216
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MUTAGEN         388
FT                   /note="R->W: Loss of AMP deaminase activity."
FT                   /evidence="ECO:0000269|PubMed:11102975"
FT   MUTAGEN         425
FT                   /note="R->H: Loss of AMP deaminase activity."
FT                   /evidence="ECO:0000269|PubMed:11102975"
SQ   SEQUENCE   747 AA;  86432 MW;  C8928B67F2DD9478 CRC64;
     MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LREMQAHIFH
     MENLSMSMDG RRKRRFQGRK TVNLSIPQSE TSSTKLSHIE EFISSSPTYE SVPDFQRVQI
     TGDYASGVTV EDFEVVCKGL YRALCIREKY MQKSFQRFPK TPSKYLRNID GEALVAIESF
     YPVFTPPPKK GEDPFRREDL PANLGYHLKM KGGVIYIYPD EAAASRDEPK PYPYPNLDDF
     LDDMNFLLAL IAQGPVKTYT HRRLKFLSSK FQVHQMLNEM DELKELKNNP HRDFYNCRKV
     DTHIHAAACM NQKHLLRFIK KSYHIDADRV VYSTKEKNLT LKELFAQLNM HPYDLTVDSL
     DVHAGRQTFQ RFDKFNDKYN PVGASELRDL YLKTDNYING EYFATIIKEV GADLVDAKYQ
     HAEPRLSIYG RSPDEWSKLS SWFVGNRIYC PNMTWMIQVP RIYDVFRSKN FLPHFGKMLE
     NIFLPVFEAT INPQTHPDLS VFLKHITGFD SVDDESKHSG HMFSSKSPKP EEWTMENNPS
     YTYYAYYMYA NIMVLNCLRK ERGMNTFLFR PHCGEAGALT HLMTAFMIAD NISHGLNLKK
     SPVLQYLFFL AQIPIAMSPL SNNSLFLEYA KNPFLDFLQK GLMISLSTDD PMQFHFTKEP
     LMEEYAIAAQ VFKLSTCDMC EVARNSVLQC GISHEEKAKF LGNNYLEEGP VGNDIRRTNV
     AQIRMAYRYE TWCYELNLIA EGLKSTE
//