CRYGS

Protein-coding gene in the species Homo sapiens
CRYGS
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1HA4, 2M3T, 2M3U

Identifiers
AliasesCRYGS, CRYG8, CTRCT20, crystallin gamma S
External IDsOMIM: 123730 MGI: 1298216 HomoloGene: 40695 GeneCards: CRYGS
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CRYGS
Genomic location for CRYGS
Band3q27.3Start186,538,441 bp[1]
End186,546,702 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for CRYGS
Genomic location for CRYGS
Band16 B1|16 13.66 cMStart22,623,953 bp[2]
End22,630,327 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • anterior segment of eyeball

  • lens

  • cerebellar hemisphere

  • right lobe of liver

  • spleen

  • body of pancreas

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • right uterine tube

  • tibial nerve
Top expressed in
  • corneal stroma

  • ciliary body

  • retinal pigment epithelium

  • conjunctival fornix

  • iris

  • morula

  • sciatic nerve

  • entorhinal cortex

  • extraocular muscle

  • sexually immature organism
More reference expression data
BioGPS
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1427

12970

Ensembl

ENSG00000213139

ENSMUSG00000033501

UniProt

P22914

O35486

RefSeq (mRNA)

NM_017541

NM_009967

RefSeq (protein)

NP_060011

NP_034097

Location (UCSC)Chr 3: 186.54 – 186.55 MbChr 16: 22.62 – 22.63 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene.[5]

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.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000213139 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033501 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: CRYGS crystallin, gamma S".

External links

Further reading

  • Graw J (1998). "The crystallins: genes, proteins and diseases". Biol. Chem. 378 (11): 1331–48. doi:10.1515/bchm.1997.378.11.1299. PMID 9426193.
  • Slingsby C, Clout NJ (2000). "Structure of the crystallins". Eye. 13 ( Pt 3b) (3): 395–402. doi:10.1038/eye.1999.113. PMID 10627816.
  • Zarina S, Abbasi A, Zaidi ZH (1992). "Primary structure of beta s-crystallin from human lens". Biochem. J. 287 (Pt 2): 375–81. doi:10.1042/bj2870375. PMC 1133175. PMID 1445197.
  • Brakenhoff RH, Aarts HJ, Reek FH, et al. (1991). "Human gamma-crystallin genes. A gene family on its way to extinction". J. Mol. Biol. 216 (3): 519–32. doi:10.1016/0022-2836(90)90380-5. PMID 2258929.
  • Meakin SO, Du RP, Tsui LC, Breitman ML (1987). "Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family". Mol. Cell. Biol. 7 (8): 2671–9. doi:10.1128/mcb.7.8.2671. PMC 367883. PMID 3670288.
  • Smith JB, Yang Z, Lin P, et al. (1995). "The complete sequence of human lens gamma s-crystallin". Biochem. J. 307 (Pt 2): 407–10. doi:10.1042/bj3070407. PMC 1136663. PMID 7733876.
  • Zarina S, Slingsby C, Jaenicke R, et al. (1995). "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". Protein Sci. 3 (10): 1840–6. doi:10.1002/pro.5560031023. PMC 2142617. PMID 7849599.
  • Lampi KJ, Ma Z, Shih M, et al. (1997). "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens". J. Biol. Chem. 272 (4): 2268–75. doi:10.1074/jbc.272.4.2268. PMID 8999933.
  • Wistow G, Sardarian L, Gan W, Wyatt MK (2000). "The human gene for gammaS-crystallin: alternative transcripts and expressed sequences from the first intron". Mol. Vis. 6: 79–84. PMID 10837510.
  • Purkiss AG, Bateman OA, Goodfellow JM, et al. (2002). "The X-ray crystal structure of human gamma S-crystallin C-terminal domain". J. Biol. Chem. 277 (6): 4199–205. doi:10.1074/jbc.M110083200. PMID 11706012.
  • MacCoss MJ, McDonald WH, Saraf A, et al. (2002). "Shotgun identification of protein modifications from protein complexes and lens tissue". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7900–5. Bibcode:2002PNAS...99.7900M. doi:10.1073/pnas.122231399. PMC 122992. PMID 12060738.
  • Lapko VN, Purkiss AG, Smith DL, Smith JB (2002). "Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure". Biochemistry. 41 (27): 8638–48. doi:10.1021/bi015924t. PMID 12093281.
  • Lapko VN, Smith DL, Smith JB (2003). "S-methylated cysteines in human lens gamma S-crystallins". Biochemistry. 41 (50): 14645–51. doi:10.1021/bi0267700. PMID 12475213.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Annunziata O, Ogun O, Benedek GB (2003). "Observation of liquid–liquid phase separation for eye lens γS-crystallin". Proc. Natl. Acad. Sci. U.S.A. 100 (3): 970–4. Bibcode:2003PNAS..100..970A. doi:10.1073/pnas.242746499. PMC 298710. PMID 12529503.
  • Craghill J, Cronshaw AD, Harding JJ (2004). "The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens". Biochem. J. 379 (Pt 3): 595–600. doi:10.1042/BJ20031367. PMC 1224128. PMID 14763903.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Sun H, Ma Z, Li Y, et al. (2006). "Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans". J. Med. Genet. 42 (9): 706–10. doi:10.1136/jmg.2004.028274. PMC 1736139. PMID 16141006.
  • v
  • t
  • e
  • 1a7h: GAMMA S CRYSTALLIN C-TERMINAL DOMAIN
    1a7h: GAMMA S CRYSTALLIN C-TERMINAL DOMAIN
  • 1ha4: GAMMAS CRYSTALLIN C TERMINAL DOMAIN FROM HOMO SAPIENS
    1ha4: GAMMAS CRYSTALLIN C TERMINAL DOMAIN FROM HOMO SAPIENS


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