CRYGD crystallin gamma D [Homo sapiens (human)] - Gene

Summary

Official Symbol: CRYGDprovided by HGNC
Official Full Name: crystallin gamma Dprovided by HGNC
Primary source: HGNC:HGNC:2411
See related: Ensembl:ENSG00000118231 MIM:123690; AllianceGenome:HGNC:2411
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CCP; PCC; CACA; CCA3; CRYG4; CTRCT4; cry-g-D
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. 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. [provided by RefSeq, Jul 2008]
Expression: Biased expression in ovary (RPKM 6.8) and bone marrow (RPKM 0.8) See more
Orthologs: all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 2q33.3

Exon count:: 3

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (208121607..208124524, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (208601624..208604541, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (208986331..208989248, complement)

Chromosome 2 - NC_000002.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cataract-causing mutations S78F and S78P of gammaD-crystallin decrease protein conformational stability and drive aggregation.
Title: Cataract-causing mutations S78F and S78P of γD-crystallin decrease protein conformational stability and drive aggregation.
Congenital coralliform cataract is the predominant consequence of a recurrent mutation in the CRYGD gene.
Title: Congenital coralliform cataract is the predominant consequence of a recurrent mutation in the CRYGD gene.
Insights to Human gammaD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations.
Title: Insights to Human γD-Crystallin Unfolding by NMR Spectroscopy and Molecular Dynamics Simulations.
Surface Exposed Free Cysteine Suppresses Crystallization of Human gammaD-Crystallin.
Title: Surface Exposed Free Cysteine Suppresses Crystallization of Human γD-Crystallin.
Assessing the Structures and Interactions of gammaD-Crystallin Deamidation Variants.
Title: Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.
Increased hydrophobicity of CRYGD p.(Ala159ProfsTer9): Suspected cause of congenital cataracts in a large Chinese family.
Title: Increased hydrophobicity of CRYGD p.(Ala159ProfsTer9): Suspected cause of congenital cataracts in a large Chinese family.
Cataract-Associated New Mutants S175G/H181Q of betaBeta2-Crystallin and P24S/S31G of gammaD-Crystallin Are Involved in Protein Aggregation by Structural Changes.
Title: Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes.
Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a gammaD-Crystallin Mutant.
Title: Temperature-Dependent Interactions Explain Normal and Inverted Solubility in a γD-Crystallin Mutant.
Kinetic Stability of Long-Lived Human Lens gamma-Crystallins and Their Isolated Double Greek Key Domains.
Title: Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.
The W42R variant assumes a distinct conformation in solution that leaves the Greek key domains of the native fold largely unaltered but lacks the hydrophobic interdomain interface that is key to the stability of wild-type gammaD-crystallin.
Title: Molecular Mechanism of Aggregation of the Cataract-Related γD-Crystallin W42R Variant from Multiscale Atomistic Simulations.

Submit: New GeneRIF Correction See all GeneRIFs (90)

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Cataract 4 multiple types MedGen: C3540850 OMIM: 115700 GeneReviews: Not available	Compare labs

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

NoName (e-PCR)
- UniSTS:481287

NoName (e-PCR)
- UniSTS:491190

RH71454 (e-PCR)
- UniSTS:22207

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of eye lens	IBA Inferred from Biological aspect of Ancestor more info
enables structural constituent of eye lens	NAS Non-traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to reactive oxygen species	IDA Inferred from Direct Assay more info	PubMed
involved_in lens development in camera-type eye	IBA Inferred from Biological aspect of Ancestor more info
involved_in lens development in camera-type eye	ISS Inferred from Sequence or Structural Similarity more info
involved_in lens fiber cell differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in visual perception	IBA Inferred from Biological aspect of Ancestor more info
involved_in visual perception	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

Go to the top of the page Help

Preferred Names: gamma-crystallin D

Names: gamma crystallin 4; gamma-D-crystallin

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.