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P11844 (CRGA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-crystallin A
Alternative name(s):
Gamma-A-crystallin
Gamma-crystallin 5
Gene names
Name:CRYGA
Synonyms:CRYG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length174 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Contains 4 beta/gamma crystallin 'Greek key' domains.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainRepeat
   Molecular functionEye lens protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

visual perception

Non-traceable author statement Ref.4Ref.1. Source: UniProtKB

   Molecular_functionstructural constituent of eye lens

Non-traceable author statement Ref.4Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 174173Gamma-crystallin A
PRO_0000057585

Regions

Domain2 – 4039Beta/gamma crystallin 'Greek key' 1
Domain41 – 8343Beta/gamma crystallin 'Greek key' 2
Domain88 – 12841Beta/gamma crystallin 'Greek key' 3
Domain129 – 17143Beta/gamma crystallin 'Greek key' 4
Region84 – 874Connecting peptide

Natural variations

Natural variant1481P → L. Ref.1 Ref.5
VAR_021139

Secondary structure

.................................... 174
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11844 [UniParc].

Last modified May 29, 2007. Version 3.
Checksum: 99889A7641728090

FASTA17420,877
        10         20         30         40         50         60 
MGKITFYEDR DFQGRCYNCI SDCPNLRVYF SRCNSIRVDS GCWMLYERPN YQGHQYFLRR 

        70         80         90        100        110        120 
GKYPDYQHWM GLSDSVQSCR IIPHTSSHKL RLYERDDYRG LMSELTDDCA CVPELFRLPE 

       130        140        150        160        170 
IYSLHVLEGC WVLYEMPNYR GRQYLLRPGD YRRYHDWGGA DAKVGSLRRV TDLY 

« Hide

References

« Hide 'large scale' references
[1]"Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family."
Meakin S.O., Du R.P., Tsui L.-C., Breitman M.L.
Mol. Cell. Biol. 7:2671-2679(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-148.
[2]"Human gammaA-crystallin."
Wistow G.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[5]"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] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-148.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17316, M17315 Genomic DNA. Translation: AAA52108.1.
EF426311 mRNA. Translation: ABO14696.1.
AC016697 Genomic DNA. Translation: AAX93220.1.
CCDSCCDS33367.1.
PIRA26912.
RefSeqNP_055432.2. NM_014617.3.
UniGeneHs.122566.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LERmodel-A1-174[»]
ProteinModelPortalP11844.
SMRP11844. Positions 2-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000302105.

PTM databases

PhosphoSiteP11844.

Polymorphism databases

DMDM148887193.

Proteomic databases

PaxDbP11844.
PRIDEP11844.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304502; ENSP00000302105; ENSG00000168582.
GeneID1418.
KEGGhsa:1418.
UCSCuc002vcq.4. human.

Organism-specific databases

CTD1418.
GeneCardsGC02M209025.
HGNCHGNC:2408. CRYGA.
MIM123660. gene.
neXtProtNX_P11844.
PharmGKBPA26915.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321245.
HOGENOMHOG000234389.
HOVERGENHBG003364.
InParanoidP11844.
OMASCRAIPY.
OrthoDBEOG70CR7Z.
PhylomeDBP11844.

Gene expression databases

BgeeP11844.
CleanExHS_CRYGA.
GenevestigatorP11844.

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. SSF49695. 1 hit.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCRYGA.
GenomeRNAi1418.
NextBio5799.
PROP11844.
SOURCESearch...

Entry information

Entry nameCRGA_HUMAN
AccessionPrimary (citable) accession number: P11844
Secondary accession number(s): Q53ST5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM