LOCUS       NM_004045                471 bp    mRNA    linear   PRI 12-NOV-2024
DEFINITION  Homo sapiens antioxidant 1 copper chaperone (ATOX1), mRNA.
ACCESSION   NM_004045
VERSION     NM_004045.4
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  (bases 1 to 471)
  AUTHORS   Kuchur,O.A., Pogodaeva,S.S., Shcherbakova,A.V. and Tsymbal,S.A.
  TITLE     Atox1-cyclin D1 loop activity is critical for survival of tumor
            cells with inactivated TP53
  JOURNAL   Biosci Rep 44 (6) (2024)
   PUBMED   38813981
  REMARK    GeneRIF: Atox1-cyclin D1 loop activity is critical for survival of
            tumor cells with inactivated TP53.
REFERENCE   2  (bases 1 to 471)
  AUTHORS   Deng,R., Zhu,L., Jiang,J., Chen,J. and Li,H.
  TITLE     Cuproptosis-related gene LIPT1 as a prognostic indicator in
            non-small cell lung cancer: Functional involvement and regulation
            of ATOX1 expression
  JOURNAL   Biomol Biomed 24 (3), 647-658 (2024)
   PUBMED   38041690
  REMARK    GeneRIF: Cuproptosis-related gene LIPT1 as a prognostic indicator
            in non-small cell lung cancer: Functional involvement and
            regulation of ATOX1 expression.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 471)
  AUTHORS   Schwartz,R., Ruthstein,S. and Major,D.T.
  TITLE     Copper coordination states affect the flexibility of copper
            Metallochaperone Atox1: Insights from molecular dynamics
            simulations
  JOURNAL   Protein Sci 31 (12), e4464 (2022)
   PUBMED   36208051
  REMARK    GeneRIF: Copper coordination states affect the flexibility of
            copper Metallochaperone Atox1: Insights from molecular dynamics
            simulations.
REFERENCE   4  (bases 1 to 471)
  AUTHORS   Mangini,V., Belviso,B.D., Nardella,M.I., Natile,G., Arnesano,F. and
            Caliandro,R.
  TITLE     Crystal Structure of the Human Copper Chaperone ATOX1 Bound to Zinc
            Ion
  JOURNAL   Biomolecules 12 (10), 1494 (2022)
   PUBMED   36291703
  REMARK    GeneRIF: Crystal Structure of the Human Copper Chaperone ATOX1
            Bound to Zinc Ion.
            Publication Status: Online-Only
REFERENCE   5  (bases 1 to 471)
  AUTHORS   Zhang,X., Walke,G.R., Horvath,I., Kumar,R., Blockhuys,S.,
            Holgersson,S., Walton,P.H. and Wittung-Stafshede,P.
  TITLE     Memo1 binds reduced copper ions, interacts with copper chaperone
            Atox1, and protects against copper-mediated redox activity in vitro
  JOURNAL   Proc Natl Acad Sci U S A 119 (37), e2206905119 (2022)
   PUBMED   36067318
  REMARK    GeneRIF: Memo1 binds reduced copper ions, interacts with copper
            chaperone Atox1, and protects against copper-mediated redox
            activity in vitro.
REFERENCE   6  (bases 1 to 471)
  AUTHORS   Wernimont,A.K., Huffman,D.L., Lamb,A.L., O'Halloran,T.V. and
            Rosenzweig,A.C.
  TITLE     Structural basis for copper transfer by the metallochaperone for
            the Menkes/Wilson disease proteins
  JOURNAL   Nat Struct Biol 7 (9), 766-771 (2000)
   PUBMED   10966647
REFERENCE   7  (bases 1 to 471)
  AUTHORS   Hamza,I., Schaefer,M., Klomp,L.W. and Gitlin,J.D.
  TITLE     Interaction of the copper chaperone HAH1 with the Wilson disease
            protein is essential for copper homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 96 (23), 13363-13368 (1999)
   PUBMED   10557326
REFERENCE   8  (bases 1 to 471)
  AUTHORS   Larin,D., Mekios,C., Das,K., Ross,B., Yang,A.S. and Gilliam,T.C.
  TITLE     Characterization of the interaction between the Wilson and Menkes
            disease proteins and the cytoplasmic copper chaperone, HAH1p
  JOURNAL   J Biol Chem 274 (40), 28497-28504 (1999)
   PUBMED   10497213
REFERENCE   9  (bases 1 to 471)
  AUTHORS   Hung,I.H., Casareno,R.L., Labesse,G., Mathews,F.S. and Gitlin,J.D.
  TITLE     HAH1 is a copper-binding protein with distinct amino acid residues
            mediating copper homeostasis and antioxidant defense
  JOURNAL   J Biol Chem 273 (3), 1749-1754 (1998)
   PUBMED   9430722
REFERENCE   10 (bases 1 to 471)
  AUTHORS   Klomp,L.W., Lin,S.J., Yuan,D.S., Klausner,R.D., Culotta,V.C. and
            Gitlin,J.D.
  TITLE     Identification and functional expression of HAH1, a novel human
            gene involved in copper homeostasis
  JOURNAL   J Biol Chem 272 (14), 9221-9226 (1997)
   PUBMED   9083055
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI599233.1 and CN280769.1.
            
            On Nov 22, 2018 this sequence version replaced NM_004045.3.
            
            Summary: This gene encodes a copper chaperone that plays a role in
            copper homeostasis by binding and transporting cytosolic copper to
            ATPase proteins in the trans-Golgi network for later incorporation
            to the ceruloplasmin. This protein also functions as an antioxidant
            against superoxide and hydrogen peroxide, and therefore, may play a
            significant role in cancer carcinogenesis. Because of its
            cytogenetic location, this gene represents a candidate gene for
            5q-syndrome. [provided by RefSeq, Jul 2008].
            
            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 :: BI598370.1, BI599233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313115.11/ ENSP00000316854.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-291               BI599233.1         27-317
            292-471             CN280769.1         287-466
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     gene            1..471
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /note="antioxidant 1 copper chaperone"
                     /db_xref="GeneID:475"
                     /db_xref="HGNC:HGNC:798"
                     /db_xref="MIM:602270"
     exon            1..86
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /inference="alignment:Splign:2.1.0"
     CDS             81..287
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /EC_number="6.2.1.2"
                     /note="metal transport protein ATX1; ATX1 antioxidant
                     protein 1 homolog"
                     /codon_start=1
                     /product="copper transport protein ATOX1"
                     /protein_id="NP_004036.1"
                     /db_xref="CCDS:CCDS47317.1"
                     /db_xref="GeneID:475"
                     /db_xref="HGNC:HGNC:798"
                     /db_xref="MIM:602270"
                     /translation="MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIES
                     EHSMDTLLATLKKTGKTVSYLGLE"
     exon            87..162
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /inference="alignment:Splign:2.1.0"
     exon            163..333
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /inference="alignment:Splign:2.1.0"
     exon            334..471
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      446..451
                     /regulatory_class="polyA_signal_sequence"
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /note="hexamer: AATAAA"
     polyA_site      471
                     /gene="ATOX1"
                     /gene_synonym="ATX1; HAH1"
                     /note="major polyA site"
ORIGIN      
        1 agccgaaccc gccctccgaa tccagagagg cgctgctgac accgccgcca caccgccgcc
       61 acaccgccgc tgcctcagtc atgccgaagc acgagttctc tgtggacatg acctgtggag
      121 gctgtgctga agctgtctct cgggtcctca ataagcttgg aggagttaag tatgacattg
      181 acctgcccaa caagaaggtc tgcattgaat ctgagcacag catggacact ctgcttgcaa
      241 ccctgaagaa aacaggaaag actgtttcct accttggcct tgagtagcag gggcctggtc
      301 cccacagccc acaggatgga ccaaaggggg caggatgctg atcctcccgc tggcttccag
      361 acagacctgg gacttggcag tcatgccggg tgatggtgtt cctgcggaga ccctcagttg
      421 tcctattcct tcctagcttc cctgcaataa aatcaagctg cttttgttgg a
//
