LOCUS       NM_001289808             774 bp    mRNA    linear   PRI 15-OCT-2024
DEFINITION  Homo sapiens crystallin alpha B (CRYAB), transcript variant 3,
            mRNA.
ACCESSION   NM_001289808
VERSION     NM_001289808.2
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 774)
  AUTHORS   Wang,X., Chen,K., Yao,Y., Lin,Y., Yang,J., Zhu,Y. and Zhou,B.
  TITLE     TGFbeta1-Induced Fibrotic Responses of Conjunctival Fibroblasts
            through the Wnt/beta-Catenin/CRYAB Signaling Pathway
  JOURNAL   Am J Pathol 194 (9), 1764-1779 (2024)
   PUBMED   38879081
  REMARK    GeneRIF: TGFbeta1-Induced Fibrotic Responses of Conjunctival
            Fibroblasts through the Wnt/beta-Catenin/CRYAB Signaling Pathway.
REFERENCE   2  (bases 1 to 774)
  AUTHORS   Rodina,N., Hornung,S., Sarkar,R., Suladze,S., Peters,C.,
            Schmid,P.W.N., Niu,Z., Haslbeck,M., Buchner,J., Kapurniotu,A. and
            Reif,B.
  TITLE     Modulation of Alzheimer's Disease Abeta40 Fibril Polymorphism by
            the Small Heat Shock Protein alphaB-Crystallin
  JOURNAL   J Am Chem Soc 146 (28), 19077-19087 (2024)
   PUBMED   38973199
  REMARK    GeneRIF: Modulation of Alzheimer's Disease Abeta40 Fibril
            Polymorphism by the Small Heat Shock Protein alphaB-Crystallin.
REFERENCE   3  (bases 1 to 774)
  AUTHORS   Tian,B., Li,X., Li,W., Shi,Z., He,X., Wang,S., Zhu,X., Shi,N.,
            Li,Y., Wan,P. and Zhu,C.
  TITLE     CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1
  JOURNAL   Aging (Albany NY) 16 (10), 8965-8979 (2024)
   PUBMED   38787373
  REMARK    GeneRIF: CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1.
REFERENCE   4  (bases 1 to 774)
  AUTHORS   Zhang,C.L., Hu,Y., Wang,D.X., Yang,Q. and Chang,D.H.
  TITLE     [Research on the anti-tumor effects of CRYAB in prostate cancer]
  JOURNAL   Zhonghua Nan Ke Xue 29 (7), 579-286 (2023)
   PUBMED   38619403
  REMARK    GeneRIF: [Research on the anti-tumor effects of CRYAB in prostate
            cancer].
REFERENCE   5  (bases 1 to 774)
  AUTHORS   Derham,B.K. and Harding,J.J.
  TITLE     Alpha-crystallin as a molecular chaperone
  JOURNAL   Prog Retin Eye Res 18 (4), 463-509 (1999)
   PUBMED   10217480
  REMARK    GeneRIF: Alpha crystallin is a moonlighting protein that functions
            as a heat shock protein as well as a lens crystallin.
            Review article
REFERENCE   6  (bases 1 to 774)
  AUTHORS   Selcen,D. and Engel,A.G.
  TITLE     Myofibrillar Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301672
REFERENCE   7  (bases 1 to 774)
  AUTHORS   Ortwerth,B.J., Slight,S.H., Prabhakaram,M., Sun,Y. and Smith,J.B.
  TITLE     Site-specific glycation of lens crystallins by ascorbic acid
  JOURNAL   Biochim Biophys Acta 1117 (2), 207-215 (1992)
   PUBMED   1525182
REFERENCE   8  (bases 1 to 774)
  AUTHORS   Iwaki,A., Iwaki,T., Goldman,J.E., Ogomori,K., Tateishi,J. and
            Sakaki,Y.
  TITLE     Accumulation of alpha B-crystallin in brains of patients with
            Alexander's disease is not due to an abnormality of the 5'-flanking
            and coding sequence of the genomic DNA
  JOURNAL   Neurosci Lett 140 (1), 89-92 (1992)
   PUBMED   1407707
REFERENCE   9  (bases 1 to 774)
  AUTHORS   Kato,K., Shinohara,H., Goto,S., Inaguma,Y., Morishita,R. and
            Asano,T.
  TITLE     Copurification of small heat shock protein with alpha B crystallin
            from human skeletal muscle
  JOURNAL   J Biol Chem 267 (11), 7718-7725 (1992)
   PUBMED   1560006
REFERENCE   10 (bases 1 to 774)
  AUTHORS   Kramps,J.A., de Man,B.M. and de Jong,W.W.
  TITLE     The primary structure of the B2 chain of human alpha-crystallin
  JOURNAL   FEBS Lett 74 (1), 82-84 (1977)
   PUBMED   838078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE076509.1, BM721803.1,
            BC007008.1, BF339748.1 and AP000907.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 17, 2019 this sequence version replaced NM_001289808.1.
            
            Summary: Mammalian lens crystallins are divided into alpha, beta,
            and gamma families. Alpha crystallins are composed of two gene
            products: alpha-A and alpha-B, for acidic and basic, respectively.
            Alpha crystallins can be induced by heat shock and are members of
            the small heat shock protein (HSP20) family. They act as molecular
            chaperones although they do not renature proteins and release them
            in the fashion of a true chaperone; instead they hold them in large
            soluble aggregates. These heterogeneous aggregates consist of 30-40
            subunits; the alpha-A and alpha-B subunits have a 3:1 ratio,
            respectively. Two additional functions of alpha crystallins are an
            autokinase activity and participation in the intracellular
            architecture. The encoded protein has been identified as a
            moonlighting protein based on its ability to perform
            mechanistically distinct functions. Alpha-A and alpha-B gene
            products are differentially expressed; alpha-A is preferentially
            restricted to the lens and alpha-B is expressed widely in many
            tissues and organs. Elevated expression of alpha-B crystallin
            occurs in many neurological diseases; a missense mutation
            cosegregated in a family with a desmin-related myopathy.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2019].
            
            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 :: BC007008.1, BQ005860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000650687.2/
                                               ENSP00000499082.1
            multifunctional gene product(s) :: PMID: 10217480
            RefSeq Select criteria          :: based on manual assertion,
                                               conservation, expression,
                                               longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-300               BE076509.1         245-544
            301-415             BM721803.1         523-637
            416-715             BC007008.1         416-715
            716-718             BF339748.1         251-253
            719-774             AP000907.6         10181-10236         c
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     gene            1..774
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /note="crystallin alpha B"
                     /db_xref="GeneID:1410"
                     /db_xref="HGNC:HGNC:2389"
                     /db_xref="MIM:123590"
     exon            1..247
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /inference="alignment:Splign:2.1.0"
     CDS             47..574
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /note="isoform 1 is encoded by transcript variant 3;
                     heat-shock 20 kD like-protein; alpha-crystallin B chain;
                     heat shock protein beta-5; rosenthal fiber component;
                     renal carcinoma antigen NY-REN-27; epididymis secretory
                     protein Li 101; heat shock protein family B member 5"
                     /codon_start=1
                     /product="alpha-crystallin B chain isoform 1"
                     /protein_id="NP_001276737.1"
                     /db_xref="CCDS:CCDS8351.1"
                     /db_xref="GeneID:1410"
                     /db_xref="HGNC:HGNC:2389"
                     /db_xref="MIM:123590"
                     /translation="MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSL
                     SPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHG
                     KHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIP
                     ITREEKPAVTAAPKK"
     exon            248..370
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /inference="alignment:Splign:2.1.0"
     exon            371..774
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /inference="alignment:Splign:2.1.0"
     regulatory      692..697
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /note="hexamer: AATAAA"
     polyA_site      715
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /note="major polyA site"
     regulatory      752..757
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
                     /note="hexamer: AATAAA"
     polyA_site      774
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2"
ORIGIN      
        1 gaaggagctg accagccagc tgacccctca cactcaccta gccaccatgg acatcgccat
       61 ccaccacccc tggatccgcc gccccttctt tcctttccac tcccccagcc gcctctttga
      121 ccagttcttc ggagagcacc tgttggagtc tgatcttttc ccgacgtcta cttccctgag
      181 tcccttctac cttcggccac cctccttcct gcgggcaccc agctggtttg acactggact
      241 ctcagagatg cgcctggaga aggacaggtt ctctgtcaac ctggatgtga agcacttctc
      301 cccagaggaa ctcaaagtta aggtgttggg agatgtgatt gaggtgcatg gaaaacatga
      361 agagcgccag gatgaacatg gtttcatctc cagggagttc cacaggaaat accggatccc
      421 agctgatgta gaccctctca ccattacttc atccctgtca tctgatgggg tcctcactgt
      481 gaatggacca aggaaacagg tctctggccc tgagcgcacc attcccatca cccgtgaaga
      541 gaagcctgct gtcaccgcag cccccaagaa atagatgccc tttcttgaat tgcatttttt
      601 aaaacaagaa agtttcccca ccagtgaatg aaagtcttgt gactagtgct gaagcttatt
      661 aatgctaagg gcaggcccaa attatcaagc taataaaata tcattcagca acagataact
      721 gtcttgtgtt tgaatattcc acacactttt aaataaatat acagatacca caga
//
