LOCUS       NP_001355738             825 aa            linear   PRI 20-FEB-2025
DEFINITION  AMP deaminase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001355738 NP_001244289
VERSION     NP_001355738.1
DBSOURCE    REFSEQ: accession NM_001368809.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Flores-Mendez,M., Ohl,L., Roule,T., Zhou,Y., Tintos-Hernandez,J.A.,
            Walsh,K., Ortiz-Gonzalez,X.R. and Akizu,N.
  TITLE     IMPDH2 filaments protect from neurodegeneration in AMPD2 deficiency
  JOURNAL   EMBO Rep 25 (9), 3990-4012 (2024)
   PUBMED   39075237
  REMARK    GeneRIF: IMPDH2 filaments protect from neurodegeneration in AMPD2
            deficiency.
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Gilboa,T., Elefant,N., Meiner,V. and Hacohen,N.
  TITLE     Delineating the phenotype and genetic basis of AMPD2-related
            pontocerebellar hypoplasia
  JOURNAL   Neurogenetics 24 (1), 61-66 (2023)
   PUBMED   36445597
  REMARK    GeneRIF: Delineating the phenotype and genetic basis of
            AMPD2-related pontocerebellar hypoplasia.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Van den Bergh,F. and Sabina,R.L.
  TITLE     Characterization of human AMP deaminase 2 (AMPD2) gene expression
            reveals alternative transcripts encoding variable N-terminal
            extensions of isoform L
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 401-410 (1995)
   PUBMED   8526848
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Hedera,P.
  TITLE     Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Mahnke-Zizelman,D.K. and Sabina,R.L.
  TITLE     Cloning of human AMP deaminase isoform E cDNAs. Evidence for a
            third AMPD gene exhibiting alternatively spliced 5'-exons
  JOURNAL   J Biol Chem 267 (29), 20866-20877 (1992)
   PUBMED   1400401
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355310.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 1, 2019 this sequence version replaced NP_001244289.1.
            
            Summary: The protein encoded by this gene is important in purine
            metabolism by converting AMP to IMP. The encoded protein, which
            acts as a homotetramer, is one of three AMP deaminases found in
            mammals. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 4
            both encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314494.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            MANE Ensembl match               :: ENST00000528667.7/
                                                ENSP00000436541.2
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation, expression,
                                                longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..825
                     /product="AMP deaminase 2 isoform 1"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L);
                     AMP deaminase 2"
                     /calculated_mol_wt=94759
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01433.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            45
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Region          163..806
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..825
                     /gene="AMPD2"
                     /gene_synonym="AMPD; PCH9; SPG63"
                     /coded_by="NM_001368809.2:705..3182"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS805.2"
                     /db_xref="GeneID:271"
                     /db_xref="HGNC:HGNC:469"
                     /db_xref="MIM:102771"
ORIGIN      
        1 masypsgsgk pkakypfkkr aslqastaap eargglgapp lqsarslpgp apclkhfpld
       61 lrtsmdgkck eiaeelftrs laeselrsap yefpeespie qleerrqrle rqisqdvkle
      121 pdillrakqd flktdsdsdl qlykeqgegq gdrslrerdv lerefqrvti sgeekcgvpf
      181 tdlldaaksv vralfireky malslqsfcp ttrrylqqla ekpletrtye qgpdtpvsad
      241 apvhppaleq hpyehcepst mpgdlglglr mvrgvvhvyt rrepdehcse velpypdlqe
      301 fvadvnvlma liingpiksf cyrrlqylss kfqmhvllne mkelaaqkkv phrdfynirk
      361 vdthihassc mnqkhllrfi kramkrhlee ivhveqgreq tlrevfesmn ltaydlsvdt
      421 ldvhadrntf hrfdkfnaky npigesvlre ifiktdnrvs gkyfahiike vmsdleesky
      481 qnaelrlsiy grsrdewdkl arwavmhrvh spnvrwlvqv prlfdvyrtk gqlanfqeml
      541 eniflplfea tvhpashpel hlflehvdgf dsvddeskpe nhvfnlespl peawveednp
      601 pyayylyytf anmamlnhlr rqrgfhtfvl rphcgeagpi hhlvsafmla enishglllr
      661 kapvlqylyy laqigiamsp lsnnslflsy hrnplpeyls rglmvslstd dplqfhftke
      721 plmeeysiat qvwklsscdm celarnsvlm sgfshkvksh wlgpnytkeg pegndirrtn
      781 vpdirvgyry etlcqelali tqavqsemle tipeeagitm spgpq
//
