ID   AMPD1_MOUSE             Reviewed;         745 AA.
AC   Q3V1D3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=AMP deaminase 1;
DE            EC=3.5.4.6;
DE   AltName: Full=Myoadenylate deaminase;
DE   AltName: Full=AMP deaminase isoform M;
GN   Name=Ampd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy
CC       metabolism.
CC   -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from AMP: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
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DR   EMBL; AK132524; BAE21218.1; -; mRNA.
DR   IPI; IPI00625079; -.
DR   UniGene; Mm.331272; -.
DR   PhosphoSite; Q3V1D3; -.
DR   Ensembl; ENSMUSG00000070385; Mus musculus.
DR   MGI; MGI:88015; Ampd1.
DR   HOVERGEN; Q3V1D3; -.
DR   BRENDA; 3.5.4.6; 244.
DR   ArrayExpress; Q3V1D3; -.
DR   Bgee; Q3V1D3; -.
DR   CleanEx; MM_AMPD1; -.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:EC.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:InterPro.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynt...; IEA:InterPro.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006329; AMP_deaminase.
DR   InterPro; IPR016297; AMP_deaminase_met.
DR   Pfam; PF00962; A_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Nucleotide metabolism.
FT   CHAIN         1    745       AMP deaminase 1.
FT                                /FTId=PRO_0000269718.
FT   ACT_SITE    361    361       By similarity.
FT   ACT_SITE    571    571       By similarity.
FT   ACT_SITE    647    647       By similarity.
FT   ACT_SITE    648    648       By similarity.
SQ   SEQUENCE   745 AA;  86019 MW;  D0ED4058BFD446DA CRC64;
     MPLFKLTGQG KQIDDAMRSF AEKVFASEVK DEGGRHEISP FDVDEICPIS LHEMQAHIFH
     MENLSMDGRR KRRFQGRKTV NLSIPQSETS STKLSHIEEF ISSSPTYESV PDFQRVQITG
     DYASGVTVED FEVVCKGLYR ALCIREKYMQ KSFQRFPKTP SKYLRNIDGE ALVGNESFYP
     VFTPPPKKGE DPFRTEDLPA NLGYHLKMKA GVIYIYPDEA AANRDDPKPY PYPNLDDFLD
     DMNFLLALIA QGPVKTYAHR RLKFLSSKFQ VHQMLNEMDE LKELKNNPHR DFYNCRKVDT
     HIHAAACMNQ KHLLRFIKKS YHIDADRVVY STKEKSLTLK ELFAKLNMHP YDLTVDSLDV
     HAGRQTFQRF DKFNDKYNPV GASELRDLYL KTDNYINGEY FATIIKEVGA DLVEAKYQHA
     EPRLSIYGRS PDEWNKLSSW FVCNRIYCPN MTWMIQVPRI YDVFRSKNFL PHFGKMLENI
     FLPVFEATIN PQAHPDLSVF LKHITGFDSV DDESKHSGHM FSSKSPKPEE WTMGNNPSYT
     YYAYYMYANI TVLNSLRKER GMNTFLFRPH CGEAGALTHL MTAFMIADNI SHGLNLKKSP
     VLQYLFFLAQ IPIAMSPLSN NSLFLEYAKN PFLDFLQKGL MISLSTDDPM QFHFTKEPLM
     EEYAIAAQVF KLSTCDMCEV ARNSVLQCGI SHEEKAKFLG NNYLEEGPVG NDIRRTNVAQ
     IRMAYRYETW CYELNLIAEG LKATE
//