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Protein

Gamma-crystallin D

Gene

CRYGD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Crystallins are the dominant structural components of the vertebrate eye lens.

GO - Molecular functioni

  • structural constituent of eye lens Source: UniProtKB

GO - Biological processi

  • cellular response to reactive oxygen species Source: UniProtKB
  • lens development in camera-type eye Source: UniProtKB
  • lens fiber cell differentiation Source: UniProtKB
  • visual perception Source: UniProtKB

Keywordsi

Molecular functionEye lens protein
Biological processSensory transduction, Vision

Enzyme and pathway databases

SIGNORiP07320.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-crystallin D
Alternative name(s):
Gamma-D-crystallin
Gamma-crystallin 4
Gene namesi
Name:CRYGD
Synonyms:CRYG4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000118231.4.
HGNCiHGNC:2411. CRYGD.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Involvement in diseasei

Cataract 4, multiple types (CTRCT4)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT4 includes crystalline aculeiform, congenital cerulean and non-nuclear polymorphic cataracts, among others. Crystalline aculeiform cataract is characterized by fiberglass-like or needle-like crystals projecting in different directions, through or close to the axial region of the lens. Non-nuclear polymorphic cataract is a partial opacity with variable location between the fetal nucleus of the lens and the equator. The fetal nucleus is normal. The opacities are irregular and look similar to a bunch of grapes and may be present simultaneously in different lens layers. Congenital cerulean cataract is characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract.
See also OMIM:115700
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01073315R → C in CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation. 2 PublicationsCorresponds to variant dbSNP:rs121909595Ensembl.1
Natural variantiVAR_03495524P → S in CTRCT4; lowered solubility. 2 PublicationsCorresponds to variant dbSNP:rs28931605Ensembl.1
Natural variantiVAR_02114524P → T in CTRCT4; lowered solubility. 3 PublicationsCorresponds to variant dbSNP:rs28931605Ensembl.1
Natural variantiVAR_01073437R → S in CTRCT4; very low solubility; crystallizes spontaneously. 2 PublicationsCorresponds to variant dbSNP:rs121909597Ensembl.1
Natural variantiVAR_06482943W → R in CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation. 1 Publication1
Natural variantiVAR_01073559R → H in CTRCT4; lowered solubility; crystallizes easily. 3 PublicationsCorresponds to variant dbSNP:rs121909596Ensembl.1
Natural variantiVAR_034956107E → A in CTRCT4. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24 – 25PN → TK: Wild-type solubility. 2
Mutagenesisi24P → TP: Wild-type solubility. 1 Publication1
Mutagenesisi24P → V: Slightly lowered solubility. 1 Publication1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi1421.
MalaCardsiCRYGD.
MIMi115700. phenotype.
OpenTargetsiENSG00000118231.
Orphaneti1377. Cataract-microcornea syndrome.
98989. Cerulean cataract.
98986. Coppock-like cataract.
98990. Coralliform cataract.
98991. Nuclear cataract.
98995. Zonular cataract.
PharmGKBiPA26918.

Polymorphism and mutation databases

BioMutaiCRYGD.
DMDMi2506321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575882 – 174Gamma-crystallin DAdd BLAST173

Proteomic databases

EPDiP07320.
MaxQBiP07320.
PaxDbiP07320.
PeptideAtlasiP07320.
PRIDEiP07320.

PTM databases

iPTMnetiP07320.
PhosphoSitePlusiP07320.

Expressioni

Gene expression databases

BgeeiENSG00000118231.
CleanExiHS_CRYGD.
ExpressionAtlasiP07320. baseline and differential.
GenevisibleiP07320. HS.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107811. 5 interactors.
DIPiDIP-46208N.
IntActiP07320. 2 interactors.
MINTiMINT-8303016.
STRINGi9606.ENSP00000264376.

Structurei

Secondary structure

1174
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Helixi10 – 12Combined sources3
Beta strandi13 – 21Combined sources9
Turni27 – 29Combined sources3
Beta strandi34 – 48Combined sources15
Turni49 – 51Combined sources3
Beta strandi52 – 58Combined sources7
Beta strandi60 – 65Combined sources6
Helixi66 – 69Combined sources4
Beta strandi72 – 74Combined sources3
Beta strandi78 – 82Combined sources5
Beta strandi89 – 95Combined sources7
Helixi96 – 98Combined sources3
Beta strandi99 – 107Combined sources9
Helixi112 – 114Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi123 – 129Combined sources7
Beta strandi131 – 136Combined sources6
Turni137 – 139Combined sources3
Beta strandi140 – 146Combined sources7
Beta strandi148 – 151Combined sources4
Helixi154 – 157Combined sources4
Beta strandi166 – 169Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H4AX-ray1.15X2-174[»]
1HK0X-ray1.25X2-174[»]
1LD0model-A1-174[»]
2G98X-ray2.20A/B2-174[»]
2KFBNMR-A2-174[»]
2KLJOther-A2-174[»]
4GR7X-ray1.70A/X2-174[»]
4JGFX-ray2.50A/B2-172[»]
ProteinModelPortaliP07320.
SMRiP07320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 40Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST39
Domaini41 – 83Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST43
Domaini88 – 128Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST41
Domaini129 – 171Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 87Connecting peptide4

Domaini

Has a two-domain beta-structure, folded into four very similar Greek key motifs.

Sequence similaritiesi

Belongs to the beta/gamma-crystallin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IWCR. Eukaryota.
ENOG411298R. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP07320.
OMAiQMIEITE.
OrthoDBiEOG091G0L2P.
PhylomeDBiP07320.

Family and domain databases

InterProiView protein in InterPro
IPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
PfamiView protein in Pfam
PF00030. Crystall. 2 hits.
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiView protein in SMART
SM00247. XTALbg. 2 hits.
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiView protein in PROSITE
PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07320-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKITLYEDR GFQGRHYECS SDHPNLQPYL SRCNSARVDS GCWMLYEQPN
60 70 80 90 100
YSGLQYFLRR GDYADHQQWM GLSDSVRSCR LIPHSGSHRI RLYEREDYRG
110 120 130 140 150
QMIEFTEDCS CLQDRFRFNE IHSLNVLEGS WVLYELSNYR GRQYLLMPGD
160 170
YRRYQDWGAT NARVGSLRRV IDFS
Length:174
Mass (Da):20,738
Last modified:January 23, 2007 - v3
Checksum:i437EC83FD79F12E4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01073315R → C in CTRCT4; progressive punctate cataract with early onset; causes disulfide-linked oligomers formation with consequent protein aggregation and precipitation. 2 PublicationsCorresponds to variant dbSNP:rs121909595Ensembl.1
Natural variantiVAR_03495524P → S in CTRCT4; lowered solubility. 2 PublicationsCorresponds to variant dbSNP:rs28931605Ensembl.1
Natural variantiVAR_02114524P → T in CTRCT4; lowered solubility. 3 PublicationsCorresponds to variant dbSNP:rs28931605Ensembl.1
Natural variantiVAR_01073437R → S in CTRCT4; very low solubility; crystallizes spontaneously. 2 PublicationsCorresponds to variant dbSNP:rs121909597Ensembl.1
Natural variantiVAR_06482943W → R in CTRCT4; much less stable than the wild-type protein; more prone to aggregate when subjected to environmental stresses such as heat and UV irradiation. 1 Publication1
Natural variantiVAR_01073559R → H in CTRCT4; lowered solubility; crystallizes easily. 3 PublicationsCorresponds to variant dbSNP:rs121909596Ensembl.1
Natural variantiVAR_021146102M → V2 Publications1
Natural variantiVAR_034956107E → A in CTRCT4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03006, K03005 Genomic DNA. Translation: AAA52112.1.
U66583 mRNA. Translation: AAB38686.1.
AC093698 Genomic DNA. Translation: AAY24041.1.
BC117338 mRNA. Translation: AAI17339.1.
BC117340 mRNA. Translation: AAI17341.1.
CCDSiCCDS2378.1.
PIRiI77413.
RefSeqiNP_008822.2. NM_006891.3.
UniGeneiHs.546247.

Genome annotation databases

EnsembliENST00000264376; ENSP00000264376; ENSG00000118231.
GeneIDi1421.
KEGGihsa:1421.
UCSCiuc002vcn.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCRGD_HUMAN
AccessioniPrimary (citable) accession number: P07320
Secondary accession number(s): Q17RF7, Q53R51, Q99681
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 184 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families