AMPD1_RAT
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 03-AUG-2022, entry version 144.
DE RecName: Full=AMP deaminase 1;
DE EC=3.5.4.6;
DE AltName: Full=AMP deaminase isoform M;
DE AltName: Full=Myoadenylate deaminase;
GN Name=Ampd1;
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 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 -!- 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}.
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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; P10759; -.
DR Ensembl; ENSRNOT00000112496; ENSRNOP00000080039; ENSRNOG00000018656.
DR GeneID; 25028; -.
DR KEGG; rno:25028; -.
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 OMA; MYVYNDA; -.
DR OrthoDB; 49756at2759; -.
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 tissues.
DR Genevisible; P10759; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003876; F:AMP deaminase activity; ISO:RGD.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029770; AMPD1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF1; PTHR11359:SF1; 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 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"
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
