LOCUS       NM_000454                895 bp    mRNA    linear   PRI 12-NOV-2024
DEFINITION  Homo sapiens superoxide dismutase 1 (SOD1), mRNA.
ACCESSION   NM_000454
VERSION     NM_000454.5
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 895)
  AUTHORS   Wang,P.S., Yang,X.X., Wei,Q., Lv,Y.T., Wu,Z.Y. and Li,H.F.
  TITLE     Clinical characterization and founder effect analysis in Chinese
            amyotrophic lateral sclerosis patients with SOD1 common variants
  JOURNAL   Ann Med 56 (1), 2407522 (2024)
   PUBMED   39351695
  REMARK    GeneRIF: Clinical characterization and founder effect analysis in
            Chinese amyotrophic lateral sclerosis patients with SOD1 common
            variants.
REFERENCE   2  (bases 1 to 895)
  AUTHORS   Martinez,P., Silva,M., Abarzua,S., Tevy,M.F., Jaimovich,E.,
            Constantine-Paton,M., Bustos,F.J. and van Zundert,B.
  TITLE     Skeletal myotubes expressing ALS mutant SOD1 induce pathogenic
            changes, impair mitochondrial axonal transport, and trigger
            motoneuron death
  JOURNAL   Mol Med 30 (1), 185 (2024)
   PUBMED   39455931
  REMARK    GeneRIF: Skeletal myotubes expressing ALS mutant SOD1 induce
            pathogenic changes, impair mitochondrial axonal transport, and
            trigger motoneuron death.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 895)
  AUTHORS   Tabuchi,R., Momozawa,Y., Hayashi,Y., Noma,H., Ichijo,H. and
            Fujisawa,T.
  TITLE     SoDCoD: a comprehensive database of Cu/Zn superoxide dismutase
            conformational diversity caused by ALS-linked gene mutations and
            other perturbations
  JOURNAL   Database (Oxford) 2024, 0 (2024)
   PUBMED   39126203
  REMARK    GeneRIF: SoDCoD: a comprehensive database of Cu/Zn superoxide
            dismutase conformational diversity caused by ALS-linked gene
            mutations and other perturbations.
REFERENCE   4  (bases 1 to 895)
  AUTHORS   Zhang,L., Hsu,J.I., Braekeleer,E.D., Chen,C.W., Patel,T.D.,
            Martell,A.G., Guzman,A.G., Wohlan,K., Waldvogel,S.M., Uryu,H.,
            Tovy,A., Callen,E., Murdaugh,R.L., Richard,R., Jansen,S.,
            Vissers,L., de Vries,B.B.A., Nussenzweig,A., Huang,S., Coarfa,C.,
            Anastas,J., Takahashi,K., Vassiliou,G. and Goodell,M.A.
  TITLE     SOD1 is a synthetic-lethal target in PPM1D-mutant leukemia cells
  JOURNAL   Elife 12, 91611 (2024)
   PUBMED   38896450
  REMARK    GeneRIF: SOD1 is a synthetic-lethal target in PPM1D-mutant leukemia
            cells.
            Publication Status: Online-Only
REFERENCE   5  (bases 1 to 895)
  AUTHORS   Azkargorta,M., Bregon-Villahoz,M., Escobes,I., Ibanez-Perez,J.,
            Iloro,I., Iglesias,M., Diez-Zapirain,M., Rabanal,A., Prieto,B.,
            Moragues,M.D., Matorras,R. and Elortza,F.
  TITLE     In-depth proteomics and natural peptidomics analyses reveal
            antibacterial peptides in human endometrial fluid
  JOURNAL   J Proteomics 216, 103652 (2020)
   PUBMED   31958637
  REMARK    GeneRIF: SOD1 displays antimicrobial activity against E. coli, E.
            faecalis, S. aureus, S. aureus MRSA LPV+, S. agalactiae, and yeast
            C. krusei.
REFERENCE   6  (bases 1 to 895)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   7  (bases 1 to 895)
  AUTHORS   Crapo,J.D., Oury,T., Rabouille,C., Slot,J.W. and Chang,L.Y.
  TITLE     Copper,zinc superoxide dismutase is primarily a cytosolic protein
            in human cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (21), 10405-10409 (1992)
   PUBMED   1332049
REFERENCE   8  (bases 1 to 895)
  AUTHORS   Parge,H.E., Hallewell,R.A. and Tainer,J.A.
  TITLE     Atomic structures of wild-type and thermostable mutant recombinant
            human Cu,Zn superoxide dismutase
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 6109-6113 (1992)
   PUBMED   1463506
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Nov 15;89(22):11106]
REFERENCE   9  (bases 1 to 895)
  AUTHORS   Kajihara,J., Enomoto,M., Nishijima,K., Yabuuchi,M. and Katoh,K.
  TITLE     Comparison of properties between human recombinant and placental
            copper-zinc SOD
  JOURNAL   J Biochem 104 (5), 851-854 (1988)
   PUBMED   2853161
REFERENCE   10 (bases 14 to 573)
  AUTHORS   Sherman,L., Dafni,N., Lieman-Hurwitz,J. and Groner,Y.
  TITLE     Nucleotide sequence and expression of human chromosome 21-encoded
            superoxide dismutase mRNA
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 80 (18), 5465-5469 (1983)
   PUBMED   6577438
REFERENCE   11 (bases 1 to 895)
  AUTHORS   Philip,T., Fraisse,J., Sinet,P.M., Lauras,B., Robert,J.M. and
            Freycon,F.
  TITLE     Confirmation of the assignment of the human SODS gene to chromosome
            21q22
  JOURNAL   Cytogenet Cell Genet 22 (1-6), 521-523 (1978)
   PUBMED   752535
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV756797.1, BC001034.1,
            X02317.1 and CA448539.1.
            
            On Dec 4, 2019 this sequence version replaced NM_000454.4.
            
            Summary: The protein encoded by this gene binds copper and zinc
            ions and is one of two isozymes responsible for destroying free
            superoxide radicals in the body. The encoded isozyme is a soluble
            cytoplasmic protein, acting as a homodimer to convert
            naturally-occuring but harmful superoxide radicals to molecular
            oxygen and hydrogen peroxide. The other isozyme is a mitochondrial
            protein. In addition, this protein contains an antimicrobial
            peptide that displays antibacterial, antifungal, and anti-MRSA
            activity against E. coli, E. faecalis, S. aureus, S. aureus MRSA
            LPV+, S. agalactiae, and yeast C. krusei. Mutations in this gene
            have been implicated as causes of familial amyotrophic lateral
            sclerosis. Rare transcript variants have been reported for this
            gene. [provided by RefSeq, Jul 2020].
            
            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 :: BI547103.1, BX359175.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000270142.11/
                                                  ENSP00000270142.7
            Protein has antimicrobial activity :: PMID: 31958637
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-10                AV756797.1         96-105
            11-13               BC001034.1         1-3
            14-885              X02317.1           1-872
            886-895             CA448539.1         16-25               c
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     gene            1..895
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /note="superoxide dismutase 1"
                     /db_xref="GeneID:6647"
                     /db_xref="HGNC:HGNC:11179"
                     /db_xref="MIM:147450"
     exon            1..149
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /inference="alignment:Splign:2.1.0"
     CDS             78..542
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /EC_number="1.15.1.1"
                     /note="indophenoloxidase A; SOD, soluble; superoxide
                     dismutase, cystolic; Cu/Zn superoxide dismutase;
                     epididymis secretory protein Li 44; superoxide dismutase
                     1, soluble"
                     /codon_start=1
                     /product="superoxide dismutase [Cu-Zn]"
                     /protein_id="NP_000445.1"
                     /db_xref="CCDS:CCDS33536.1"
                     /db_xref="GeneID:6647"
                     /db_xref="HGNC:HGNC:11179"
                     /db_xref="MIM:147450"
                     /translation="MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLH
                     GFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIED
                     SVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ"
     exon            150..246
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /inference="alignment:Splign:2.1.0"
     exon            247..316
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /inference="alignment:Splign:2.1.0"
     exon            317..434
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /inference="alignment:Splign:2.1.0"
     exon            435..895
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /inference="alignment:Splign:2.1.0"
     regulatory      620..625
                     /regulatory_class="polyA_signal_sequence"
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /note="hexamer: ATTAAA"
     polyA_site      641
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /note="major polyA site"
     regulatory      869..874
                     /regulatory_class="polyA_signal_sequence"
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
                     /note="hexamer: ATTAAA"
     polyA_site      895
                     /gene="SOD1"
                     /gene_synonym="ALS; ALS1; HEL-S-44; homodimer; hSod1;
                     IPOA; SOD; STAHP"
ORIGIN      
        1 gcgtcgtagt ctcctgcagc gtctggggtt tccgttgcag tcctcggaac caggacctcg
       61 gcgtggccta gcgagttatg gcgacgaagg ccgtgtgcgt gctgaagggc gacggcccag
      121 tgcagggcat catcaatttc gagcagaagg aaagtaatgg accagtgaag gtgtggggaa
      181 gcattaaagg actgactgaa ggcctgcatg gattccatgt tcatgagttt ggagataata
      241 cagcaggctg taccagtgca ggtcctcact ttaatcctct atccagaaaa cacggtgggc
      301 caaaggatga agagaggcat gttggagact tgggcaatgt gactgctgac aaagatggtg
      361 tggccgatgt gtctattgaa gattctgtga tctcactctc aggagaccat tgcatcattg
      421 gccgcacact ggtggtccat gaaaaagcag atgacttggg caaaggtgga aatgaagaaa
      481 gtacaaagac aggaaacgct ggaagtcgtt tggcttgtgg tgtaattggg atcgcccaat
      541 aaacattccc ttggatgtag tctgaggccc cttaactcat ctgttatcct gctagctgta
      601 gaaatgtatc ctgataaaca ttaaacactg taatcttaaa agtgtaattg tgtgactttt
      661 tcagagttgc tttaaagtac ctgtagtgag aaactgattt atgatcactt ggaagatttg
      721 tatagtttta taaaactcag ttaaaatgtc tgtttcaatg acctgtattt tgccagactt
      781 aaatcacaga tgggtattaa acttgtcaga atttctttgt cattcaagcc tgtgaataaa
      841 aaccctgtat ggcacttatt atgaggctat taaaagaatc caaattcaaa ctaaa
//
