ADAL_MOUSE
ID ADAL_MOUSE Reviewed; 360 AA.
AC Q80SY6; A2ARU3; A2ARU4; Q8BLN3; Q8BX67; Q9D4Q6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Adenosine deaminase-like protein;
DE EC=3.5.4.-;
GN Name=Adal;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, Spinal cord, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 4).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of the free cytosolic methylated
CC adenosine nucleotide N(6)-methyl-AMP (N6-mAMP) to produce inositol
CC monophosphate (IMP) and methylamine. Is required for the catabolism of
CC cytosolic N6-mAMP, which is derived from the degradation of mRNA
CC containing N6-methylated adenine (m6A). {ECO:0000250|UniProtKB:Q6DHV7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N(6)-methyl-AMP = IMP + methylamine;
CC Xref=Rhea:RHEA:16001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:59338, ChEBI:CHEBI:144842;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16002;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6DHV7};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q6DHV7};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6DHV7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80SY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80SY6-2; Sequence=VSP_024822;
CC Name=3;
CC IsoId=Q80SY6-3; Sequence=VSP_024823, VSP_024824;
CC Name=4;
CC IsoId=Q80SY6-4; Sequence=VSP_024825;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Adenosine and AMP deaminases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM18206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK016299; BAB30184.1; -; mRNA.
DR EMBL; AK044025; BAC31744.1; -; mRNA.
DR EMBL; AK048809; BAC33464.1; -; mRNA.
DR EMBL; AK049697; BAC33880.1; -; mRNA.
DR EMBL; AL845479; CAM18204.1; -; Genomic_DNA.
DR EMBL; AL845479; CAM18205.1; -; Genomic_DNA.
DR EMBL; AL845479; CAM18206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845479; CAM18207.1; -; Genomic_DNA.
DR EMBL; BC050879; AAH50879.1; -; mRNA.
DR EMBL; BC052048; AAH52048.1; -; mRNA.
DR CCDS; CCDS16633.1; -. [Q80SY6-1]
DR CCDS; CCDS71121.1; -. [Q80SY6-2]
DR CCDS; CCDS89543.1; -. [Q80SY6-4]
DR RefSeq; NP_001277740.1; NM_001290811.1. [Q80SY6-2]
DR RefSeq; NP_001277741.1; NM_001290812.1.
DR RefSeq; NP_083751.1; NM_029475.2. [Q80SY6-1]
DR RefSeq; XP_006500414.1; XM_006500351.2. [Q80SY6-1]
DR RefSeq; XP_006500415.1; XM_006500352.2. [Q80SY6-1]
DR RefSeq; XP_006500416.1; XM_006500353.3. [Q80SY6-1]
DR RefSeq; XP_006500421.1; XM_006500358.2.
DR RefSeq; XP_006500422.1; XM_006500359.2. [Q80SY6-4]
DR RefSeq; XP_006500423.1; XM_006500360.2. [Q80SY6-4]
DR AlphaFoldDB; Q80SY6; -.
DR SMR; Q80SY6; -.
DR STRING; 10090.ENSMUSP00000113052; -.
DR PhosphoSitePlus; Q80SY6; -.
DR EPD; Q80SY6; -.
DR MaxQB; Q80SY6; -.
DR PaxDb; Q80SY6; -.
DR PeptideAtlas; Q80SY6; -.
DR PRIDE; Q80SY6; -.
DR ProteomicsDB; 285610; -. [Q80SY6-1]
DR ProteomicsDB; 285611; -. [Q80SY6-2]
DR ProteomicsDB; 285612; -. [Q80SY6-3]
DR ProteomicsDB; 285613; -. [Q80SY6-4]
DR Antibodypedia; 23863; 92 antibodies from 16 providers.
DR Ensembl; ENSMUST00000028702; ENSMUSP00000028702; ENSMUSG00000027259. [Q80SY6-2]
DR Ensembl; ENSMUST00000066155; ENSMUSP00000067133; ENSMUSG00000027259. [Q80SY6-1]
DR Ensembl; ENSMUST00000110662; ENSMUSP00000106290; ENSMUSG00000027259. [Q80SY6-4]
DR Ensembl; ENSMUST00000119031; ENSMUSP00000113052; ENSMUSG00000027259. [Q80SY6-1]
DR GeneID; 75894; -.
DR KEGG; mmu:75894; -.
DR UCSC; uc008lxo.1; mouse. [Q80SY6-3]
DR UCSC; uc008lxp.2; mouse. [Q80SY6-1]
DR CTD; 161823; -.
DR MGI; MGI:1923144; Adal.
DR VEuPathDB; HostDB:ENSMUSG00000027259; -.
DR eggNOG; KOG1097; Eukaryota.
DR GeneTree; ENSGT00950000183113; -.
DR HOGENOM; CLU_039228_3_0_1; -.
DR InParanoid; Q80SY6; -.
DR OMA; RPQFKPY; -.
DR OrthoDB; 981145at2759; -.
DR PhylomeDB; Q80SY6; -.
DR TreeFam; TF314270; -.
DR Reactome; R-MMU-2161541; Abacavir metabolism.
DR Reactome; R-MMU-74217; Purine salvage.
DR BioGRID-ORCS; 75894; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Adal; mouse.
DR PRO; PR:Q80SY6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80SY6; protein.
DR Bgee; ENSMUSG00000027259; Expressed in otolith organ and 225 other tissues.
DR ExpressionAtlas; Q80SY6; baseline and differential.
DR Genevisible; Q80SY6; MM.
DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0062154; F:N6-mAMP deaminase activity; IEA:RHEA.
DR GO; GO:0006154; P:adenosine catabolic process; IBA:GO_Central.
DR GO; GO:0046103; P:inosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001365; A_deaminase_dom.
DR InterPro; IPR006330; Ado/ade_deaminase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11409; PTHR11409; 1.
DR Pfam; PF00962; A_deaminase; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Metal-binding; Nucleotide metabolism;
KW Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Adenosine deaminase-like protein"
FT /id="PRO_0000285091"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 25
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 27
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 73
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 105..108
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 147
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 180
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 210
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 292
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT BINDING 293
FT /ligand="N(6)-methyl-AMP"
FT /ligand_id="ChEBI:CHEBI:144842"
FT /evidence="ECO:0000250|UniProtKB:Q8LPL7"
FT SITE 231
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P03958"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_024825"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024822"
FT VAR_SEQ 86..114
FT /note="TKDVIKEFADDGVKYLELRSTPREENATG -> RHRGRLKWRDFPQQCTANL
FT AHVLWLSSTL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024823"
FT VAR_SEQ 115..360
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024824"
FT CONFLICT Q80SY6-3:39
FT /note="I -> T (in Ref. 1; BAC31744)"
FT /evidence="ECO:0000305"
FT CONFLICT Q80SY6-3:103
FT /note="N -> H (in Ref. 1; BAC31744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41001 MW; 525AEBD0EF7D217D CRC64;
MEAGQQWPGK TDFYLQLPKV ELHAHLNGSI SSSTMKKLIA KKPHLNVHGH MTMIDKGKKR
TLQECFQMFQ VIHQLTTSAE DILMVTKDVI KEFADDGVKY LELRSTPREE NATGMTRKTY
VESVLEGIKQ CKQENLDIDV RYLMAIDRRG GPTIARETVE LAKEFFLSTE NTVLGLDLSG
DPTIGQANDF LEPLLEAKKA GLKLALHLAE IPNREKENQM LLSLLPDRIG HGTFLSASEA
GALDQVDFVR QHQIPLELCL TSNIKSQTVP SYDQHHFGFW YSIAHPSVIC TDDKGVFATY
LSQEYQLAAE TFNLTPFQVW DLSYESINYI FACDNTRSEL RKRWTHLKQK VLNCNEVNYF
