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{{Infobox_gene}}
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'''Crystallin, gamma C''', also known as '''CRYGC''', is a [[protein]] which in humans is encoded by the ''CRYGC'' [[gene]].<ref name="pmid4065573">{{cite journal | vauthors = den Dunnen JT, Moormann RJ, Cremers FP, Schoenmakers JG | title = Two human gamma-crystallin genes are linked and riddled with Alu-repeats | journal = Gene | volume = 38 | issue = 1-3 | pages = 197–204 | year = 1985 | pmid = 4065573 | doi = 10.1016/0378-1119(85)90218-5| url = | issn = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CRYGC crystallin, gamma C| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1420| accessdate = }}</ref>
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== Function ==
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
[[Crystallin]]s are separated into two classes: [[taxon]]-specific, or [[enzyme]], and ubiquitous. The latter class constitutes the major [[protein]]s 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, [[monomer]]ic proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three [[pseudogene]]s (gamma-E, gamma-F, gamma-G) are organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in [[cataract]] formation.<ref name="entrez" />
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Crystallin, gamma C
| HGNCid = 2410
| Symbol = CRYGC
| AltSymbols =; CCL; CRYG3
| OMIM = 123680
| ECnumber = 
| Homologene = 36281
| MGIid = 88523
| GeneAtlas_image1 = PBB_GE_CRYGC_207531_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0001654 |text = eye development}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1420
    | Hs_Ensembl = ENSG00000163254
    | Hs_RefseqProtein = NP_066269
    | Hs_RefseqmRNA = NM_020989
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 208701108
    | Hs_GenLoc_end = 208702872
    | Hs_Uniprot = P07315
    | Mm_EntrezGene = 12966
    | Mm_Ensembl = ENSMUSG00000025952
    | Mm_RefseqmRNA = NM_007775
    | Mm_RefseqProtein = NP_031801
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 65005810
    | Mm_GenLoc_end = 65007787
    | Mm_Uniprot = Q61597
  }}
}}
'''Crystallin, gamma C''', also known as '''CRYGC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGC crystallin, gamma C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1420| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
CRYGC has been shown to [[Protein-protein interaction|interact]] with [[CRYBB2]],<ref name=pmid11700327>{{cite journal |last=Fu |first=Ling |author2=Liang Jack J-N |date=Feb 2002 |title=Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay |journal=J. Biol. Chem. |volume=277 |issue=6 |pages=4255–60 |publisher= |location = United States| issn = 0021-9258| pmid = 11700327 |doi = 10.1074/jbc.M110027200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[CRYAA]]<ref name=pmid11700327/> and [[CRYAB]].<ref name=pmid11700327/>
| section_title =  
| summary_text = 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. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.<ref name="entrez">{{cite web | title = Entrez Gene: CRYGC crystallin, gamma C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1420| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CRYGC}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Graw J |title=The crystallins: genes, proteins and diseases. |journal=Biol. Chem. |volume=378 |issue= 11 |pages= 1331-48 |year= 1998 |pmid= 9426193 |doi=  }}
*{{cite journal  | author=Graw J |title=The crystallins: genes, proteins and diseases. |journal=Biol. Chem. |volume=378 |issue= 11 |pages= 1331–48 |year= 1998 |pmid= 9426193 |doi=  10.1515/bchm.1997.378.11.1299}}
*{{cite journal  | author=Slingsby C, Clout NJ |title=Structure of the crystallins. |journal=Eye (London, England) |volume=13 ( Pt 3b) |issue=  |pages= 395-402 |year= 2000 |pmid= 10627816 |doi=  }}
*{{cite journal  | vauthors=Slingsby C, Clout NJ |title=Structure of the crystallins. | series=13 |journal=Eye (London, England) |volume=( Pt 3b) |issue=  |pages= 395–402 |year= 2000 |pmid= 10627816 |doi=  10.1038/eye.1999.113}}
*{{cite journal  | author=Hearne CM, Todd JA |title=Trinucleotide repeat polymorphism at the CRYG1 locus. |journal=Nucleic Acids Res. |volume=19 |issue= 19 |pages= 5450 |year= 1991 |pmid= 1923840 |doi=  }}
*{{cite journal  | vauthors=Hearne CM, Todd JA |title=Trinucleotide repeat polymorphism at the CRYG1 locus. |journal=Nucleic Acids Res. |volume=19 |issue= 19 |pages= 5450 |year= 1991 |pmid= 1923840 |doi= 10.1093/nar/19.19.5450-a| pmc=328932 }}
*{{cite journal  | author=Brakenhoff RH, Aarts HJ, Reek FH, ''et al.'' |title=Human gamma-crystallin genes. A gene family on its way to extinction. |journal=J. Mol. Biol. |volume=216 |issue= 3 |pages= 519-32 |year= 1991 |pmid= 2258929 |doi=  }}
*{{cite journal  | vauthors=Brakenhoff RH, Aarts HJ, Reek FH |title=Human gamma-crystallin genes. A gene family on its way to extinction. |journal=J. Mol. Biol. |volume=216 |issue= 3 |pages= 519–32 |year= 1991 |pmid= 2258929 |doi=10.1016/0022-2836(90)90380-5 |display-authors=etal}}
*{{cite journal  | author=den Dunnen JT, van Neck JW, Cremers FP, ''et al.'' |title=Nucleotide sequence of the rat gamma-crystallin gene region and comparison with an orthologous human region. |journal=Gene |volume=78 |issue= 2 |pages= 201-13 |year= 1989 |pmid= 2777080 |doi=  }}
*{{cite journal  | vauthors=den Dunnen JT, van Neck JW, Cremers FP |title=Nucleotide sequence of the rat gamma-crystallin gene region and comparison with an orthologous human region. |journal=Gene |volume=78 |issue= 2 |pages= 201–13 |year= 1989 |pmid= 2777080 |doi=10.1016/0378-1119(89)90223-0 |display-authors=etal}}
*{{cite journal  | author=Shiloh Y, Donlon T, Bruns G, ''et al.'' |title=Assignment of the human gamma-crystallin gene cluster (CRYG) to the long arm of chromosome 2, region q33-36. |journal=Hum. Genet. |volume=73 |issue= 1 |pages= 17-9 |year= 1986 |pmid= 3011643 |doi=  }}
*{{cite journal  | vauthors=Shiloh Y, Donlon T, Bruns G |title=Assignment of the human gamma-crystallin gene cluster (CRYG) to the long arm of chromosome 2, region q33-36. |journal=Hum. Genet. |volume=73 |issue= 1 |pages= 17–9 |year= 1986 |pmid= 3011643 |doi=10.1007/BF00292656 |display-authors=etal}}
*{{cite journal  | author=Lubsen NH, Renwick JH, Tsui LC, ''et al.'' |title=A locus for a human hereditary cataract is closely linked to the gamma-crystallin gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 489-92 |year= 1987 |pmid= 3025877 |doi=  }}
*{{cite journal  | vauthors=Lubsen NH, Renwick JH, Tsui LC |title=A locus for a human hereditary cataract is closely linked to the gamma-crystallin gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 489–92 |year= 1987 |pmid= 3025877 |doi=10.1073/pnas.84.2.489  | pmc=304234 |display-authors=etal|bibcode=1987PNAS...84..489L}}
*{{cite journal  | author=Meakin SO, Du RP, Tsui LC, Breitman ML |title=Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family. |journal=Mol. Cell. Biol. |volume=7 |issue= 8 |pages= 2671-9 |year= 1987 |pmid= 3670288 |doi=  }}
*{{cite journal  | vauthors=Meakin SO, Du RP, Tsui LC, Breitman ML |title=Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family. |journal=Mol. Cell. Biol. |volume=7 |issue= 8 |pages= 2671–9 |year= 1987 |pmid= 3670288 |doi= | pmc=367883 }}
*{{cite journal  | author=Meakin SO, Breitman ML, Tsui LC |title=Structural and evolutionary relationships among five members of the human gamma-crystallin gene family. |journal=Mol. Cell. Biol. |volume=5 |issue= 6 |pages= 1408-14 |year= 1985 |pmid= 4033658 |doi=  }}
*{{cite journal  | vauthors=Meakin SO, Breitman ML, Tsui LC |title=Structural and evolutionary relationships among five members of the human gamma-crystallin gene family. |journal=Mol. Cell. Biol. |volume=5 |issue= 6 |pages= 1408–14 |year= 1985 |pmid= 4033658 |doi= | pmc=366871 }}
*{{cite journal  | author=den Dunnen JT, Moormann RJ, Cremers FP, Schoenmakers JG |title=Two human gamma-crystallin genes are linked and riddled with Alu-repeats. |journal=Gene |volume=38 |issue= 1-3 |pages= 197-204 |year= 1986 |pmid= 4065573 |doi=  }}
*{{cite journal  | vauthors=den Dunnen JT, Moormann RJ, Cremers FP, Schoenmakers JG |title=Two human gamma-crystallin genes are linked and riddled with Alu-repeats. |journal=Gene |volume=38 |issue= 1-3 |pages= 197–204 |year= 1986 |pmid= 4065573 |doi=10.1016/0378-1119(85)90218-5 }}
*{{cite journal  | author=Andley UP, Mathur S, Griest TA, Petrash JM |title=Cloning, expression, and chaperone-like activity of human alphaA-crystallin. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 31973-80 |year= 1997 |pmid= 8943244 |doi=  }}
*{{cite journal  | vauthors=Andley UP, Mathur S, Griest TA, Petrash JM |title=Cloning, expression, and chaperone-like activity of human alphaA-crystallin. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 31973–80 |year= 1997 |pmid= 8943244 |doi=10.1074/jbc.271.50.31973 }}
*{{cite journal  | author=Lampi KJ, Ma Z, Shih M, ''et al.'' |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268-75 |year= 1997 |pmid= 8999933 |doi=  }}
*{{cite journal  | vauthors=Lampi KJ, Ma Z, Shih M |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268–75 |year= 1997 |pmid= 8999933 |doi=10.1074/jbc.272.4.2268 |display-authors=etal}}
*{{cite journal  | author=Héon E, Priston M, Schorderet DF, ''et al.'' |title=The gamma-crystallins and human cataracts: a puzzle made clearer. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1261-7 |year= 1999 |pmid= 10521291 |doi=  }}
*{{cite journal  | vauthors=Héon E, Priston M, Schorderet DF |title=The gamma-crystallins and human cataracts: a puzzle made clearer. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1261–7 |year= 1999 |pmid= 10521291 |doi=10.1086/302619 | pmc=1288278  |display-authors=etal}}
*{{cite journal  | author=Ren Z, Li A, Shastry BS, ''et al.'' |title=A 5-base insertion in the gammaC-crystallin gene is associated with autosomal dominant variable zonular pulverulent cataract. |journal=Hum. Genet. |volume=106 |issue= 5 |pages= 531-7 |year= 2000 |pmid= 10914683 |doi=  }}
*{{cite journal  | vauthors=Ren Z, Li A, Shastry BS |title=A 5-base insertion in the gammaC-crystallin gene is associated with autosomal dominant variable zonular pulverulent cataract. |journal=Hum. Genet. |volume=106 |issue= 5 |pages= 531–7 |year= 2000 |pmid= 10914683 |doi=10.1007/s004390050021 |display-authors=etal}}
*{{cite journal  | author=Fu L, Liang JJ |title=Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4255-60 |year= 2002 |pmid= 11700327 |doi= 10.1074/jbc.M110027200 }}
*{{cite journal  | vauthors=Fu L, Liang JJ |title=Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4255–60 |year= 2002 |pmid= 11700327 |doi= 10.1074/jbc.M110027200 }}
*{{cite journal  | author=Fu L, Liang JJ |title=Conformational change and destabilization of cataract gammaC-crystallin T5P mutant. |journal=FEBS Lett. |volume=513 |issue= 2-3 |pages= 213-6 |year= 2002 |pmid= 11904153 |doi=  }}
*{{cite journal  | vauthors=Fu L, Liang JJ |title=Conformational change and destabilization of cataract gammaC-crystallin T5P mutant. |journal=FEBS Lett. |volume=513 |issue= 2-3 |pages= 213–6 |year= 2002 |pmid= 11904153 |doi=10.1016/S0014-5793(02)02313-X }}
*{{cite journal  | author=Santhiya ST, Shyam Manohar M, Rawlley D, ''et al.'' |title=Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts. |journal=J. Med. Genet. |volume=39 |issue= 5 |pages= 352-8 |year= 2002 |pmid= 12011157 |doi=  }}
*{{cite journal  | vauthors=Santhiya ST, Shyam Manohar M, Rawlley D |title=Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts. |journal=J. Med. Genet. |volume=39 |issue= 5 |pages= 352–8 |year= 2002 |pmid= 12011157 |doi=10.1136/jmg.39.5.352  | pmc=1735119 |display-authors=etal}}
*{{cite journal  | author=MacCoss MJ, McDonald WH, Saraf A, ''et al.'' |title=Shotgun identification of protein modifications from protein complexes and lens tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900-5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399 }}
*{{cite journal  | vauthors=MacCoss MJ, McDonald WH, Saraf A |title=Shotgun identification of protein modifications from protein complexes and lens tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900–5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399 | pmc=122992 |display-authors=etal|bibcode=2002PNAS...99.7900M }}
}}
}}
{{refend}}
{{refend}}
{{Eye proteins}}
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Latest revision as of 01:25, 23 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Crystallin, gamma C, also known as CRYGC, is a protein which in humans is encoded by the CRYGC gene.[1][2]

Function

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. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.[2]

Interactions

CRYGC has been shown to interact with CRYBB2,[3] CRYAA[3] and CRYAB.[3]

References

  1. ↑ den Dunnen JT, Moormann RJ, Cremers FP, Schoenmakers JG (1985). "Two human gamma-crystallin genes are linked and riddled with Alu-repeats". Gene. 38 (1–3): 197–204. doi:10.1016/0378-1119(85)90218-5. PMID 4065573.
  2. ↑ 2.0 2.1 "Entrez Gene: CRYGC crystallin, gamma C".
  3. ↑ 3.0 3.1 3.2 Fu, Ling; Liang Jack J-N (Feb 2002). "Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay". J. Biol. Chem. United States. 277 (6): 4255–60. doi:10.1074/jbc.M110027200. ISSN 0021-9258. PMID 11700327.

External links

Further reading



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