LOCUS       NM_001118890             932 bp    mRNA    linear   PRI 04-APR-2024
DEFINITION  Homo sapiens glutaredoxin (GLRX), transcript variant 2, mRNA.
ACCESSION   NM_001118890
VERSION     NM_001118890.2
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  (bases 1 to 932)
  AUTHORS   Corteselli,E.M., Sharafi,M., Hondal,R., MacPherson,M., White,S.,
            Lam,Y.W., Gold,C., Manuel,A.M., van der Vliet,A., Schneebeli,S.T.,
            Anathy,V., Li,J. and Janssen-Heininger,Y.M.W.
  TITLE     Structural and functional fine mapping of cysteines in mammalian
            glutaredoxin reveal their differential oxidation susceptibility
  JOURNAL   Nat Commun 14 (1), 4550 (2023)
   PUBMED   37507364
  REMARK    GeneRIF: Structural and functional fine mapping of cysteines in
            mammalian glutaredoxin reveal their differential oxidation
            susceptibility.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 932)
  AUTHORS   Hanschmann,E.M., Wilms,C., Falk,L., Holubiec,M.I., Mennel,S.,
            Lillig,C.H. and Godoy,J.R.
  TITLE     Cytosolic glutaredoxin 1 is upregulated in AMD and controls retinal
            pigment epithelial cells proliferation via beta-catenin
  JOURNAL   Biochem Biophys Res Commun 618, 24-29 (2022)
   PUBMED   35714567
  REMARK    GeneRIF: Cytosolic glutaredoxin 1 is upregulated in AMD and
            controls retinal pigment epithelial cells proliferation via
            beta-catenin.
REFERENCE   3  (bases 1 to 932)
  AUTHORS   Watanabe,Y., Nakamura,T., Uematsu,M., Fujioka,D., Inomata,D.,
            Saito,Y., Horikoshi,T., Yoshizaki,T., Kobayashi,T., Nakamura,K. and
            Kugiyama,K.
  TITLE     Glutaredoxin-1 levels in plasma can predict future events in
            patients with cardiovascular diseases
  JOURNAL   Free Radic Biol Med 176, 241-245 (2021)
   PUBMED   34587543
  REMARK    GeneRIF: Glutaredoxin-1 levels in plasma can predict future events
            in patients with cardiovascular diseases.
REFERENCE   4  (bases 1 to 932)
  AUTHORS   Chatterji,A. and Sengupta,R.
  TITLE     Cellular S-denitrosylases: Potential role and interplay of
            Thioredoxin, TRP14, and Glutaredoxin systems in thiol-dependent
            protein denitrosylation
  JOURNAL   Int J Biochem Cell Biol 131, 105904 (2021)
   PUBMED   33359085
  REMARK    GeneRIF: Cellular S-denitrosylases: Potential role and interplay of
            Thioredoxin, TRP14, and Glutaredoxin systems in thiol-dependent
            protein denitrosylation.
            Review article
REFERENCE   5  (bases 1 to 932)
  AUTHORS   Chang,Y., Li,G., Zhai,Y., Huang,L., Feng,Y., Wang,D., Zhang,W. and
            Hu,H.
  TITLE     Redox Regulator GLRX Is Associated With Tumor Immunity in Glioma
  JOURNAL   Front Immunol 11, 580934 (2020)
   PUBMED   33329553
  REMARK    GeneRIF: Redox Regulator GLRX Is Associated With Tumor Immunity in
            Glioma.
            Publication Status: Online-Only
REFERENCE   6  (bases 1 to 932)
  AUTHORS   Padilla,C.A., Spyrou,G. and Holmgren,A.
  TITLE     High-level expression of fully active human glutaredoxin
            (thioltransferase) in E. coli and characterization of Cys7 to Ser
            mutant protein
  JOURNAL   FEBS Lett 378 (1), 69-73 (1996)
   PUBMED   8549805
REFERENCE   7  (bases 1 to 932)
  AUTHORS   Padilla,C.A., Martinez-Galisteo,E., Barcena,J.A., Spyrou,G. and
            Holmgren,A.
  TITLE     Purification from placenta, amino acid sequence, structure
            comparisons and cDNA cloning of human glutaredoxin
  JOURNAL   Eur J Biochem 227 (1-2), 27-34 (1995)
   PUBMED   7851394
REFERENCE   8  (bases 1 to 932)
  AUTHORS   Bandyopadhyay,S. and Gronostajski,R.M.
  TITLE     Identification of a conserved oxidation-sensitive cysteine residue
            in the NFI family of DNA-binding proteins
  JOURNAL   J Biol Chem 269 (47), 29949-29955 (1994)
   PUBMED   7961993
REFERENCE   9  (bases 1 to 932)
  AUTHORS   Fernando,M.R., Sumimoto,H., Nanri,H., Kawabata,S., Iwanaga,S.,
            Minakami,S., Fukumaki,Y. and Takeshige,K.
  TITLE     Cloning and sequencing of the cDNA encoding human glutaredoxin
  JOURNAL   Biochim Biophys Acta 1218 (2), 229-231 (1994)
   PUBMED   8018729
REFERENCE   10 (bases 1 to 932)
  AUTHORS   Papov,V.V., Gravina,S.A., Mieyal,J.J. and Biemann,K.
  TITLE     The primary structure and properties of thioltransferase
            (glutaredoxin) from human red blood cells
  JOURNAL   Protein Sci 3 (3), 428-434 (1994)
   PUBMED   8019414
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP196332.1, BC010965.1,
            D21238.1, AW792936.1 and AW128930.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NM_001118890.1.
            
            Summary: This gene encodes a member of the glutaredoxin family. The
            encoded protein is a cytoplasmic enzyme catalyzing the reversible
            reduction of glutathione-protein mixed disulfides. This enzyme
            highly contributes to the antioxidant defense system. It is crucial
            for several signalling pathways by controlling the
            S-glutathionylation status of signalling mediators. It is involved
            in beta-amyloid toxicity and Alzheimer's disease. Multiple
            alternatively spliced transcript variants encoding the same protein
            have been identified. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR,
            compared to variant 1. Variants 1-4 encode the same protein.
            
            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 :: SRR5189658.64138.1,
                                           SRR5189667.252130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237858.11/ ENSP00000237858.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-135               BP196332.1         148-282
            136-578             BC010965.1         140-582
            579-810             D21238.1           518-749
            811-852             AW792936.1         180-221
            853-932             AW128930.1         15-94               c
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q15"
     gene            1..932
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /note="glutaredoxin"
                     /db_xref="GeneID:2745"
                     /db_xref="HGNC:HGNC:4330"
                     /db_xref="MIM:600443"
     exon            1..271
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /inference="alignment:Splign:2.1.0"
     CDS             65..385
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /EC_number="1.8.4.1"
                     /note="TTase-1; thioltransferase-1"
                     /codon_start=1
                     /product="glutaredoxin-1"
                     /protein_id="NP_001112362.1"
                     /db_xref="CCDS:CCDS4078.1"
                     /db_xref="GeneID:2745"
                     /db_xref="HGNC:HGNC:4330"
                     /db_xref="MIM:600443"
                     /translation="MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLE
                     FVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQI
                     GALQ"
     exon            272..391
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /inference="alignment:Splign:2.1.0"
     exon            392..932
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /inference="alignment:Splign:2.1.0"
     regulatory      782..787
                     /regulatory_class="polyA_signal_sequence"
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /note="hexamer: AATAAA"
     polyA_site      803
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /note="major polyA site"
     regulatory      910..915
                     /regulatory_class="polyA_signal_sequence"
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
                     /note="hexamer: AATAAA"
     polyA_site      932
                     /gene="GLRX"
                     /gene_synonym="GRX; GRX1"
ORIGIN      
        1 gctcaatacc ccaagcaata cctgcaactg aggattcttc ccggggagac cgcagcccat
       61 cggcatggct caagagtttg tgaactgcaa aatccagcct gggaaggtgg ttgtgttcat
      121 caagcccacc tgcccgtact gcaggagggc ccaagagatc ctcagtcaat tgcccatcaa
      181 acaagggctt ctggaatttg tcgatatcac agccaccaac cacactaacg agattcaaga
      241 ttatttgcaa cagctcacgg gagcaagaac ggtgcctcga gtctttattg gtaaagattg
      301 tataggcgga tgcagtgatc tagtctcttt gcaacagagt ggggaactgc tgacgcggct
      361 aaagcagatt ggagctctgc agtaaccaca gatctcatag gaaatgttca acaattctgt
      421 gaaaggtcac aggacccaat tggagaaatc atatgaaaag catagttggt cttggtgtca
      481 tatggatcag aggcacaagt gcagaggctg tggtcatgcg gaacactctg ttatttaaga
      541 tggctatcca gataatcctg aacactgtgt atttatttta tttagactac cagcaaagat
      601 taaagcatga aatgtaaaac atctgataaa acttacagcc ccctacacca agagtgtatc
      661 tgtgaaagag ctcctacact ttgaaaactt aagaatccct tatcatgaag tttgcctgtt
      721 ctagaattgt aagattgtta atttccttca atctctagtg acaacactta atttcttttc
      781 taataaaaaa aacctataga tgattcagtg atttttgtcc aattcatttg catgttctca
      841 agacattaag gaatgttatg cgaaatacac taacttaaaa ctgtgtttat atttggccct
      901 gccattataa ataaagacac gtgctgctgt ca
//
