AMPD2_RAT
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 03-AUG-2022, entry version 145.
DE RecName: Full=AMP deaminase 2;
DE EC=3.5.4.6;
DE AltName: Full=AMP deaminase isoform L;
GN Name=Ampd2;
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}.
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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; Q02356; -.
DR PRIDE; Q02356; -.
DR Ensembl; ENSRNOT00000026051; ENSRNOP00000026051; ENSRNOG00000019240.
DR GeneID; 362015; -.
DR KEGG; rno:362015; -.
DR UCSC; RGD:2110; rat.
DR CTD; 271; -.
DR RGD; 2110; Ampd2.
DR eggNOG; KOG1096; Eukaryota.
DR GeneTree; ENSGT00950000183011; -.
DR InParanoid; Q02356; -.
DR OMA; ESPPYSY; -.
DR OrthoDB; 49756at2759; -.
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 tissues.
DR ExpressionAtlas; Q02356; baseline and differential.
DR Genevisible; Q02356; RN.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029749; AMPD2.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF3; PTHR11359:SF3; 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 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
