AMPD3_MOUSE
ID AMPD3_MOUSE Reviewed; 766 AA.
AC O08739; O88692; Q8CFR4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=AMP deaminase 3;
DE EC=3.5.4.6;
DE AltName: Full=AMP deaminase H-type;
DE AltName: Full=AMP deaminase isoform E;
DE AltName: Full=Heart-type AMPD;
GN Name=Ampd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=9321472; DOI=10.1007/s003359900562;
RA Sermsuvitayawong K., Wang X., Nagabukuro A., Matsuda Y., Morisaki H.,
RA Toyama K., Mukai T., Morisaki T.;
RT "Genomic organization of Ampd3, heart-type AMPD gene, located in mouse
RT chromosome 7.";
RL Mamm. Genome 8:767-769(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found in heart, lung brain, spleen, kidney and to a
CC lesser extent in liver.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
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DR EMBL; D85596; BAA19933.1; -; mRNA.
DR EMBL; D88994; BAA32548.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK133465; BAE21671.1; -; mRNA.
DR EMBL; CH466531; EDL16988.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16989.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16990.1; -; Genomic_DNA.
DR EMBL; BC040366; AAH40366.1; -; mRNA.
DR EMBL; BC056380; AAH56380.1; -; mRNA.
DR CCDS; CCDS21747.1; -.
DR RefSeq; NP_001263230.1; NM_001276301.1.
DR RefSeq; NP_033797.2; NM_009667.3.
DR RefSeq; XP_006507282.1; XM_006507219.3.
DR RefSeq; XP_006507285.1; XM_006507222.3.
DR AlphaFoldDB; O08739; -.
DR SMR; O08739; -.
DR BioGRID; 198091; 5.
DR IntAct; O08739; 2.
DR STRING; 10090.ENSMUSP00000005829; -.
DR iPTMnet; O08739; -.
DR PhosphoSitePlus; O08739; -.
DR SwissPalm; O08739; -.
DR EPD; O08739; -.
DR jPOST; O08739; -.
DR MaxQB; O08739; -.
DR PaxDb; O08739; -.
DR PeptideAtlas; O08739; -.
DR PRIDE; O08739; -.
DR ProteomicsDB; 296351; -.
DR Antibodypedia; 42354; 308 antibodies from 33 providers.
DR DNASU; 11717; -.
DR Ensembl; ENSMUST00000005829; ENSMUSP00000005829; ENSMUSG00000005686.
DR Ensembl; ENSMUST00000170374; ENSMUSP00000130495; ENSMUSG00000005686.
DR GeneID; 11717; -.
DR KEGG; mmu:11717; -.
DR UCSC; uc009jfl.2; mouse.
DR CTD; 272; -.
DR MGI; MGI:1096344; Ampd3.
DR VEuPathDB; HostDB:ENSMUSG00000005686; -.
DR eggNOG; KOG1096; Eukaryota.
DR GeneTree; ENSGT00950000183011; -.
DR HOGENOM; CLU_003782_4_0_1; -.
DR InParanoid; O08739; -.
DR OMA; RKERGMC; -.
DR OrthoDB; 49756at2759; -.
DR PhylomeDB; O08739; -.
DR TreeFam; TF300439; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-74217; Purine salvage.
DR UniPathway; UPA00591; UER00663.
DR BioGRID-ORCS; 11717; 2 hits in 71 CRISPR screens.
DR PRO; PR:O08739; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O08739; protein.
DR Bgee; ENSMUSG00000005686; Expressed in decidua and 225 other tissues.
DR ExpressionAtlas; O08739; baseline and differential.
DR Genevisible; O08739; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003876; F:AMP deaminase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046032; P:ADP catabolic process; IMP:MGI.
DR GO; GO:0046031; P:ADP metabolic process; IMP:CACAO.
DR GO; GO:0006196; P:AMP catabolic process; IMP:MGI.
DR GO; GO:0046033; P:AMP metabolic process; IMP:CACAO.
DR GO; GO:0046034; P:ATP metabolic process; IMP:CACAO.
DR GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:CACAO.
DR GO; GO:0046039; P:GTP metabolic process; IMP:CACAO.
DR GO; GO:0006188; P:IMP biosynthetic process; IDA:MGI.
DR GO; GO:0032264; P:IMP salvage; IMP:MGI.
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 Hydrolase; Metal-binding; Nucleotide metabolism; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..766
FT /note="AMP deaminase 3"
FT /id="PRO_0000194411"
FT REGION 89..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 607
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 387..392
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 662
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 663..666
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01432"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01432"
FT CONFLICT 251
FT /note="E -> K (in Ref. 1; BAA19933)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="N -> K (in Ref. 1; BAA19933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 88652 MW; 94991133B18B8AA5 CRC64;
MPRQFPKLNM SDLDEHVRLL AEKVFAKVLR EEDSKDVMSL FTVPEDCPIG QKEAKERELQ
KELAEQKSVE TAKRKKSFKM IRSQSLSLQM PTQQDWKGPP TASPAMSPAT PLVPGATSKP
GPAPYAMPEY QRVTISGDYC AGITVEDYEQ AAKSLAKALM IREKYARLAY HRFPRTTAQY
LAHQGESVPL EEGLPDFHPP PLPQEDPYCL DDAPPNLGYL VRMHGGVLFV YDNQTMLERQ
EPHSLPYPDL ETYIVDMSHI LALITDGPTK TYCHRRLNFL ESKFSLHEML NEMSEFKELK
SNPHRDFYNV RKVDTHIHAA ACMNQKHLLR FIKHTYQTEP DRTVAEKLGR KITLRQVFDS
LHMDPYDLTV DSLDVHAGRQ TFHRFDKFNS KYNPVGASEL RDLYLKTENY LGGEYFARMV
KEVARELEDS KYQYSEPRLS IYGRSPKEWS SLARWFIQHK VYSPNMRWII QVPRIYDIFR
SKKLLPNFGK MLENIFLPLF KATINPQDHR ELHLFLKYVT GFDSVDDESK HSDHMFSDKS
PSPDLWTSEQ NPPYSYYLYY MYANIMVLNN LRRERGLSTF LFRPHCGEAG SITHLVSAFL
TADNISHGLL LKKSPVLQYL YYLAQIPIAM SPLSNNSLFL EYSKNPLREF LHKGLHVSLS
TDDPMQFHYT KEALMEEYAI AAQVWKLSTC DLCEIARNSV LQSGLSHQEK QKFLGQNYYK
EGPEGNDIRK TNVAQIRMAF RYETLCNELS FLSDAMKSEE ITALTK
