Reviewed, UniProtKB/Swiss-Prot P07315 (CRGC_HUMAN)

Names and origin

Protein names

Recommended name:
    Gamma-crystallin C
Alternative name(s):
    Gamma-C-crystallin
    Gamma-crystallin 2-1
    Gamma-crystallin 3

Gene names

Name:	CRYGC
Synonyms:	CRYG3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Crystallins are the dominant structural components of the vertebrate eye lens.
Subunit structure	Monomer By similarity.
Domain	Has a two-domain beta-structure, folded into four very similar Greek key motifs.
Involvement in disease	Defects in CRYGC are a cause of autosomal dominant cataract [MIM:604219]. Cataract is an opacification of the eye lens that frequently results in visual impairment or blindness during infancy and early childhood. Defects in CRYGC are the cause of variable zonular pulverulent cataract [MIM:123680]. Defects in CRYGC are a cause of Coppock-like cataract (CCL) [MIM:604307]. The Coppock cataract refers to a congenital pulverulent disk-like opacity involving the embryonal and fetal nucleus with many tiny white dots in the lamellar portion of the lens. It is usually bilateral and dominantly inherited. Crystallins do not turn over as the lens ages, providing ample opportunity for post-translational modifications or oxidations. These modifications may change crystallin solubility properties and favor senile cataract.
Sequence similarities	Belongs to the beta/gamma-crystallin family. Contains 4 beta/gamma crystallin 'Greek key' domains.
Mass spectrometry	Molecular weight is 20747±0.2 Da from positions 2 - 174. Determined by ESI. Ref.8

Ontologies

Keywords
Cellular component	Eye lens protein
Coding sequence diversity	Polymorphism
Disease	Cataract Disease mutation
Domain	Repeat
PTM	Methylation Oxidation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	structural constituent of eye lens Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 174

173

Gamma-crystallin C

Regions

Domain

2 – 40

39

Beta/gamma crystallin 'Greek key' 1

Domain

41 – 83

43

Beta/gamma crystallin 'Greek key' 2

Domain

88 – 128

41

Beta/gamma crystallin 'Greek key' 3

Domain

129 – 171

43

Beta/gamma crystallin 'Greek key' 4

Region

84 – 87

4

Connecting peptide

Sites

Site

56

1

Susceptible to oxidation

Site

69

1

Susceptible to oxidation

Site

70

1

Susceptible to oxidation

Site

131

1

Susceptible to oxidation

Amino acid modifications

Modified residue

23

1

S-methylcysteine

Modified residue

63

1

Phosphotyrosine

Modified residue

66

1

Phosphotyrosine

Natural variations

Natural variant

5

1

T → P in CCL; interactions between Pro-5 mutants themselves were unchanged versus wild-type CRYGC indicating that homogeneous interaction sites or domains differ from those used in heterogeneous interactions.

Natural variant

6

1

F → L: dbSNP rs2242072.

Natural variant

48

1

R → H

Natural variant

169

1

R → W in cataract; congenital lamellar.

Secondary structure

1

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174

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Helix

9 – 11

3

Beta strand

12 – 20

9

Turn

26 – 28

3

Beta strand

33 – 47

15

Turn

48 – 50

3

Beta strand

51 – 57

7

Beta strand

59 – 65

7

Helix

66 – 68

3

Beta strand

71 – 73

3

Beta strand

77 – 81

5

Beta strand

88 – 94

7

Turn

95 – 97

3

Beta strand

98 – 101

4

Helix

111 – 115

5

Beta strand

122 – 128

7

Beta strand

130 – 135

6

Turn

136 – 138

3

Beta strand

139 – 145

7

Beta strand

147 – 150

4

Helix

153 – 156

4

Beta strand

165 – 168

4

Sequences

	Sequence		Length	Mass (Da)
	P07315-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B01DC167171A7668	FASTA	174	20,879
	10 20 30 40 50 60 MGKITFYEDR AFQGRSYETT TDCPNLQPYF SRCNSIRVES GCWMLYERPN YQGQQYLLRR 70 80 90 100 110 120 GEYPDYQQWM GLSDSIRSCC LIPQTVSHRL RLYEREDHKG LMMELSEDCP SIQDRFHLSE 130 140 150 160 170 IRSLHVLEGC WVLYELPNYR GRQYLLRPQE YRRCQDWGAM DAKAGSLRRV VDLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two human gamma-crystallin genes are linked and riddled with Alu-repeats." den Dunnen J.T., Moormann R.J.M., Cremers F.P.M., Schoenmakers J.G.G. Gene 38:197-204(1985) [PubMed: 4065573] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural and evolutionary relationships among five members of the human gamma-crystallin gene family." Meakin S.O., Breitman M.L., Tsui L.-C. Mol. Cell. Biol. 5:1408-1414(1985) [PubMed: 4033658] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide sequence of the rat gamma-crystallin gene region and comparison with an orthologous human region." den Dunnen J.T., van Neck J.W., Cremers F.P.M., Lubsen N.H., Schoenmakers J.G.G. Gene 78:201-213(1989) [PubMed: 2777080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning and expression of human lens crystallins." Petrash J.M., Mathur S., Manoharan M., Andley U.P. Invest. Ophthalmol. Vis. Sci. 36:S882-S882(1995) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens." Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L. J. Biol. Chem. 272:2268-2275(1997) [PubMed: 8999933] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26.
[7]	"Shotgun identification of protein modifications from protein complexes and lens tissue." MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M., Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I., Yates J.R. III Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002) [PubMed: 12060738] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND TYR-66, SUSCEPTIBILITY TO OXIDATION, MASS SPECTROMETRY.
[8]	"Methylation and carbamylation of human gamma-crystallins." Lapko V.N., Smith D.L., Smith J.B. Protein Sci. 12:1762-1774(2003) [PubMed: 12876325] [Abstract] Cited for: METHYLATION AT CYS-23, MASS SPECTROMETRY.
[9]	"Homology models of human gamma-crystallins: structural study of the extensive charge network in gamma-crystallins." Salim A., Zaidi Z.H. Biochem. Biophys. Res. Commun. 300:624-630(2003) [PubMed: 12507494] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[10]	"The gamma-crystallins and human cataracts: a puzzle made clearer." Heon E., Priston M., Schorderet D.F., Billingsley G.D., Girard P.O., Lubsen N., Munier F.L. Am. J. Hum. Genet. 65:1261-1267(1999) [PubMed: 10521291] [Abstract] Cited for: VARIANT CCL PRO-5.
[11]	Erratum Heon E., Priston M., Schorderet D.F., Billingsley G.D., Girard P.O., Lubsen N., Munier F.L. Am. J. Hum. Genet. 66:753-753(2000)
[12]	"A 5-base insertion in the gammaC-crystallin gene is associated with autosomal dominant variable zonular pulverulent cataract." Ren Z., Li A., Shastry B.S., Padma T., Ayyagari R., Scott M.H., Parks M.M., Kaiser-Kupfer M.I., Hejtmancik J.F. Hum. Genet. 106:531-537(2000) [PubMed: 10914683] [Abstract] Cited for: INVOLVEMENT IN VARIABLE ZONULAR PULVERULENT CATARACT.
[13]	"Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts." Santhiya S.T., Shyam Manohar M., Rawlley D., Vijayalakshmi P., Namperumalsamy P., Gopinath P.M., Loester J., Graw J. J. Med. Genet. 39:352-358(2002) [PubMed: 12011157] [Abstract] Cited for: VARIANT CATARACT TRP-169, VARIANT HIS-48.
[14]	"Alteration of protein-protein interactions of congenital cataract crystallin mutants." Fu L., Liang J.J.-N. Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003) [PubMed: 12601044] [Abstract] Cited for: CHARACTERIZATION OF VARIANT CCL PRO-5.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M11973, M11972 Genomic DNA. Translation: AAA52114.1.
K03004, K03003 Genomic DNA. Translation: AAA52111.1.
M19364 Genomic DNA. Translation: AAA52110.1.
U66582 mRNA. Translation: AAC50899.1.
BC074954 mRNA. Translation: AAH74954.1.
BC074955 mRNA. Translation: AAH74955.1.

PIR

CYHUG2. B24520.

RefSeq

NP_066269.1.

UniGene

Hs.72910

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LFE	model	-	A	1-174	[»]

SMR

P07315. Positions 2-174.

ModBase

Search...

PTM databases

PhosphoSite

P07315.

Proteomic databases

PeptideAtlas

P07315.

Genome annotation databases

Ensembl

ENSG00000163254. Homo sapiens. [Contig view]

GeneID

1420.

KEGG

hsa:1420.

Organism-specific databases

H-InvDB

HIX0029985.

HGNC

HGNC:2410. CRYGC.

MIM

123680. gene+phenotype.
604219. phenotype.
604307. phenotype.

Orphanet

91492. Cataract, congenital, non-syndromic.

PharmGKB

PA26917.

GenAtlas

Search...

GeneCards

Search...

GeneLynx

Search...

Phylogenomic databases

HOGENOM

P07315.

HOVERGEN

P07315.

Gene expression databases

ArrayExpress

P07315.

CleanEx

HS_CRYGC.

GermOnline

ENSG00000163254. Homo sapiens.

Family and domain databases

InterPro

IPR001064. Crystallin.
[Graphical view]

Gene3D

G3DSA:2.60.20.10. Crystallin. 2 hits.

Pfam

PF00030. Crystall. 2 hits.
[Graphical view]

PRINTS

PR01367. BGCRYSTALLIN.

SMART

SM00247. XTALbg. 2 hits.
[Graphical view]

PROSITE

PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]

ProDom

P07315.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

SOURCE

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ProtoNet

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Entry information

Entry name

CRGC_HUMAN

Accession

Primary (citable) accession number: P07315

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	July 22, 2008
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)