LOCUS       NM_017541                844 bp    mRNA    linear   PRI 09-JUL-2024
DEFINITION  Homo sapiens crystallin gamma S (CRYGS), mRNA.
ACCESSION   NM_017541
VERSION     NM_017541.4
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 844)
  AUTHORS   Zhu,S., Xi,Y., Xu,J., Hu,L., Luo,C., Yao,K. and Chen,X.
  TITLE     The 18th amino acid glycine plays an essential role in maintaining
            the structural stabilities of gammaS-crystallin linking with
            congenital cataract
  JOURNAL   Int J Biol Macromol 251, 126339 (2023)
   PUBMED   37586630
  REMARK    GeneRIF: The 18th amino acid glycine plays an essential role in
            maintaining the structural stabilities of gammaS-crystallin linking
            with congenital cataract.
REFERENCE   2  (bases 1 to 844)
  AUTHORS   Vendra,V.P.R., Ostrowski,C., Dyba,M.A., Tarasov,S.G. and
            Hejtmancik,J.F.
  TITLE     Human gammaS-Crystallin Mutation F10_Y11delinsLN in the First Greek
            Key Pair Destabilizes and Impairs Tight Packing Causing Cortical
            Lamellar Cataract
  JOURNAL   Int J Mol Sci 24 (18), 14332 (2023)
   PUBMED   37762633
  REMARK    GeneRIF: Human gammaS-Crystallin Mutation F10_Y11delinsLN in the
            First Greek Key Pair Destabilizes and Impairs Tight Packing Causing
            Cortical Lamellar Cataract.
            Publication Status: Online-Only
REFERENCE   3  (bases 1 to 844)
  AUTHORS   Norton-Baker,B., Rocha,M.A., Granger-Jones,J., Fishman,D.A. and
            Martin,R.W.
  TITLE     Human gammaS-Crystallin Resists Unfolding Despite Extensive
            Chemical Modification from Exposure to Ionizing Radiation
  JOURNAL   J Phys Chem B 126 (3), 679-690 (2022)
   PUBMED   35021623
  REMARK    GeneRIF: Human gammaS-Crystallin Resists Unfolding Despite
            Extensive Chemical Modification from Exposure to Ionizing
            Radiation.
REFERENCE   4  (bases 1 to 844)
  AUTHORS   Wang,K.J., Liao,X.Y., Lin,K., Xi,Y.B., Wang,S., Wan,X.H. and
            Yan,Y.B.
  TITLE     A novel F30S mutation in gammaS-crystallin causes autosomal
            dominant congenital nuclear cataract by increasing susceptibility
            to stresses
  JOURNAL   Int J Biol Macromol 172, 475-482 (2021)
   PUBMED   33454329
  REMARK    GeneRIF: A novel F30S mutation in gammaS-crystallin causes
            autosomal dominant congenital nuclear cataract by increasing
            susceptibility to stresses.
REFERENCE   5  (bases 1 to 844)
  AUTHORS   He,Y., Kang,J. and Song,J.
  TITLE     ATP differentially antagonizes the crowding-induced destabilization
            of human gammaS-crystallin and its four cataract-causing mutants
  JOURNAL   Biochem Biophys Res Commun 533 (4), 913-918 (2020)
   PUBMED   33004175
  REMARK    GeneRIF: ATP differentially antagonizes the crowding-induced
            destabilization of human gammaS-crystallin and its four
            cataract-causing mutants.
REFERENCE   6  (bases 1 to 844)
  AUTHORS   Smith,J.B., Yang,Z., Lin,P., Zaidi,Z., Abbasi,A. and Russell,P.
  TITLE     The complete sequence of human lens gamma s-crystallin
  JOURNAL   Biochem J 307 (Pt 2) (Pt 2), 407-410 (1995)
   PUBMED   7733876
REFERENCE   7  (bases 1 to 844)
  AUTHORS   Zarina,S., Slingsby,C., Jaenicke,R., Zaidi,Z.H., Driessen,H. and
            Srinivasan,N.
  TITLE     Three-dimensional model and quaternary structure of the human eye
            lens protein gamma S-crystallin based on beta- and gamma-crystallin
            X-ray coordinates and ultracentrifugation
  JOURNAL   Protein Sci 3 (10), 1840-1846 (1994)
   PUBMED   7849599
REFERENCE   8  (bases 1 to 844)
  AUTHORS   Zarina,S., Abbasi,A. and Zaidi,Z.H.
  TITLE     Primary structure of beta s-crystallin from human lens
  JOURNAL   Biochem J 287 (Pt 2) (Pt 2), 375-381 (1992)
   PUBMED   1445197
REFERENCE   9  (bases 1 to 844)
  AUTHORS   Brakenhoff,R.H., Aarts,H.J., Reek,F.H., Lubsen,N.H. and
            Schoenmakers,J.G.
  TITLE     Human gamma-crystallin genes. A gene family on its way to
            extinction
  JOURNAL   J Mol Biol 216 (3), 519-532 (1990)
   PUBMED   2258929
REFERENCE   10 (bases 1 to 844)
  AUTHORS   Meakin,S.O., Du,R.P., Tsui,L.C. and Breitman,M.L.
  TITLE     Gamma-crystallins of the human eye lens: expression analysis of
            five members of the gene family
  JOURNAL   Mol Cell Biol 7 (8), 2671-2679 (1987)
   PUBMED   3670288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BY794952.2, BC069478.1 and
            BF726415.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NM_017541.3.
            
            Summary: Crystallins are separated into two classes:
            taxon-specific, or enzyme, and ubiquitous. The latter class
            constitutes the major proteins of vertebrate eye lens and maintains
            the transparency and refractive index of the lens. Since lens
            central fiber cells lose their nuclei during development, these
            crystallins are made and then retained throughout life, making them
            extremely stable proteins. Mammalian lens crystallins are divided
            into alpha, beta, and gamma families; beta and gamma crystallins
            are also considered as a superfamily. Alpha and beta families are
            further divided into acidic and basic groups. Seven protein regions
            exist in crystallins: four homologous motifs, a connecting peptide,
            and N- and C-terminal extensions. Gamma-crystallins are a
            homogeneous group of highly symmetrical, monomeric proteins
            typically lacking connecting peptides and terminal extensions. They
            are differentially regulated after early development. This gene
            encodes a protein initially considered to be a beta-crystallin but
            the encoded protein is monomeric and has greater sequence
            similarity to other gamma-crystallins. This gene encodes the most
            significant gamma-crystallin in adult eye lens tissue. Whether due
            to aging or mutations in specific genes, gamma-crystallins have
            been involved in cataract formation. [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 :: BY794952.2, AF161703.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307944.6/ ENSP00000312099.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-4                 BY794952.2         72-75
            5-667               BC069478.1         1-663
            668-844             BF726415.1         418-594
FEATURES             Location/Qualifiers
     source          1..844
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.3"
     gene            1..844
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /note="crystallin gamma S"
                     /db_xref="GeneID:1427"
                     /db_xref="HGNC:HGNC:2417"
                     /db_xref="MIM:123730"
     exon            1..75
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /inference="alignment:Splign:2.1.0"
     CDS             55..591
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /note="crystallin, gamma 8; beta-crystallin S"
                     /codon_start=1
                     /product="gamma-crystallin S"
                     /protein_id="NP_060011.1"
                     /db_xref="CCDS:CCDS3275.1"
                     /db_xref="GeneID:1427"
                     /db_xref="HGNC:HGNC:2417"
                     /db_xref="MIM:123730"
                     /translation="MSKTGTKITFYEDKNFQGRRYDCDCDCADFHTYLSRCNSIKVEG
                     GTWAVYERPNFAGYMYILPQGEYPEYQRWMGLNDRLSSCRAVHLPSGGQYKIQIFEKG
                     DFSGQMYETTEDCPSIMEQFHMREIHSCKVLEGVWIFYELPNYRGRQYLLDKKEYRKP
                     IDWGAASPAVQSFRRIVE"
     exon            76..318
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /inference="alignment:Splign:2.1.0"
     exon            319..844
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /inference="alignment:Splign:2.1.0"
     regulatory      664..669
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /note="hexamer: AATAAA"
     polyA_site      688
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /note="major polyA site"
     regulatory      825..830
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
                     /note="hexamer: ATTAAA"
     polyA_site      844
                     /gene="CRYGS"
                     /gene_synonym="CRYG8; CTRCT20"
ORIGIN      
        1 gtagccattc ctgaatttct ttcagcactg ggaaaaccag tctatgcacc aaaaatgtct
       61 aaaactggaa ccaagattac tttctatgaa gacaaaaatt ttcaaggccg tcgctatgac
      121 tgtgattgcg actgtgcaga tttccacaca tacctaagtc gctgcaactc cattaaagtg
      181 gaaggaggca cctgggctgt ttatgaaagg cccaactttg ctgggtacat gtacatctta
      241 ccacagggag agtaccctga ataccagcgt tggatgggcc tcaacgaccg cctcagctcc
      301 tgcagagctg ttcatctgcc tagtggaggc cagtataaga ttcagatctt tgagaaaggg
      361 gattttagtg gtcagatgta tgaaaccacc gaagattgcc cttccatcat ggagcaattt
      421 cacatgcgag agatccactc ctgtaaggtg ctggagggtg tctggatttt ctatgagcta
      481 cccaactacc gtggcaggca gtacctcctg gacaagaagg agtaccggaa gcccatcgat
      541 tggggtgcag cctccccagc tgtccagtct ttccgccgca ttgtggagta atgacatgaa
      601 tggggccata ttcttcctgg ggcccaaatg ctggctggcc ttgtggtcca aataggcatc
      661 atcaataaaa cagttggcat gcatcccact gctgactata atgcctctcc ttaaatgctt
      721 ctagggacca gcaatacagt gctcgccaca gtgggcagtc acacaaagct acccatctgc
      781 cagatcacca atctagatct ttgtgccaaa caaaatgaga tctcattaaa aggttagaaa
      841 gtca
//
