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Reviewed, UniProtKB/Swiss-Prot P02526 (CRGB_BOVIN)

Last modified November 4, 2008. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Gamma-crystallin B
Alternative name(s):
    Gamma-B-crystallin
    Gamma-crystallin II
Gene names
Name: CRYGB
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

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

   Cellular componentEye lens protein
   DomainRepeat
   PTMGlycation
Glycoprotein
Oxidation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Molecular functionstructural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 175174Gamma-crystallin B
PRO_0000057581

Regions

Domain2 – 4039Beta/gamma crystallin 'Greek key' 1
Domain41 – 8343Beta/gamma crystallin 'Greek key' 2
Domain89 – 12941Beta/gamma crystallin 'Greek key' 3
Domain130 – 17243Beta/gamma crystallin 'Greek key' 4
Region84 – 885Connecting peptide

Sites

Site691Susceptible to oxidation By similarity
Site701Susceptible to oxidation By similarity

Amino acid modifications

Modified residue631Phosphotyrosine By similarity
Modified residue661Phosphotyrosine By similarity
Glycosylation31N-linked (Glc) (glycation); in vitro
Disulfide bond19 ↔ 23

Experimental info

Sequence conflict1201T → S in CAA25518. Ref.2

Secondary structure

...................................... 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02526-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0CF283DA837CC593

FASTA17521,097
        10         20         30         40         50         60 
MGKITFYEDR GFQGHCYECS SDCPNLQPYF SRCNSIRVDS GCWMLYERPN YQGHQYFLRR 

        70         80         90        100        110        120 
GDYPDYQQWM GFNDSIRSCR LIPQHTGTFR MRIYERDDFR GQMSEITDDC PSLQDRFHLT 

       130        140        150        160        170 
EVHSLNVLEG SWVLYEMPSY RGRQYLLRPG EYRRYLDWGA MNAKVGSLRR VMDFY 

« Hide

References

[1]"cDNA clones encoding bovine gamma-crystallins."
Hay R.E., Woods W.D., Church R.L., Petrash J.M.
Biochem. Biophys. Res. Commun. 146:332-338(1987) [PubMed: 3606621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete nucleotide sequence of a cDNA derived from calf lens gamma-crystallin mRNA: presence of Alu I-like DNA sequences."
Bhat S.P., Spector A.
DNA 3:287-295(1984) [PubMed: 6092016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[3]Wistow G.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[4]"Physicochemical characterization of gamma-crystallins from bovine lens -- hydrodynamic and biochemical properties."
Chiou S.H., Azari P., Himmel M.E.
J. Protein Chem. 7:67-80(1988) [PubMed: 3255364] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[5]"The disulfide content of calf gamma-crystallin."
McDermott M.J., Gawinowicz-Kolks M.A., Chiesa R., Spector A.
Arch. Biochem. Biophys. 262:609-619(1988) [PubMed: 3364984] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26, DISULFIDE BOND.
[6]"Identification of the glycation site of lens gamma B-crystallin by fast atom bombardment tandem mass spectrometry."
Smith J.B., Hanson S.R., Cerny R.L., Zhao H.R., Abraham E.C.
Anal. Biochem. 243:186-189(1996) [PubMed: 8954545] [Abstract]
Cited for: GLYCATION AT LYS-3, MASS SPECTROMETRY.
[7]"The molecular structure and stability of the eye lens: X-ray analysis of gamma-crystallin II."
Blundell T.L., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., Wistow G.
Nature 289:771-777(1981) [PubMed: 7464942] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SEQUENCE REVISION.
[8]"X-ray analysis of the eye lens protein gamma-II crystallin at 1.9-A resolution."
Wistow G., Turnell B., Summers L., Slingsby C., Moss D., Miller L., Lindley P., Blundell T.L.
J. Mol. Biol. 170:175-202(1983) [PubMed: 6631960] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[9]"Structure of the bovine eye lens protein gammaB (gammaII)-crystallin at 1.47 A."
Najmudin S., Nalini V., Dreissen H.P.C., Slingsby C., Blundell T.L., Moss D.S., Lindley P.F.
Acta Crystallogr. D 49:223-233(1993) [PubMed: 15299528] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS).
[10]"An eye lens protein-water structure: 1.2-A resolution structure of gammaB-crystallin at 150 K."
Kumaraswamy V.S., Lindley P.F., Slingsby C., Glover I.D.
Acta Crystallogr. D 52:611-622(1996) [PubMed: 15299624] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
[11]"X-ray structures of three interface mutants of gammaB-crystallin from bovine eye lens."
Palme S., Jaenicke R., Slingsby C.
Protein Sci. 7:611-618(1998) [PubMed: 9541393] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[12]"Unusual domain pairing in a mutant of bovine lens gammaB-crystallin."
Palme S., Jaenicke R., Slingsby C.
J. Mol. Biol. 279:1053-1059(1998) [PubMed: 9642083] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-57.
+Additional computationally mapped references.

Cross-references

Sequence databases

X01036 mRNA. Translation: CAA25518.1.
M16894 mRNA. Translation: AAA30476.1.
EF208024 mRNA. Translation: ABM97504.1.
PIRCYBOG. A29655.
RefSeqNP_001013612.1.
UniGeneBt.399

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AMMX-ray1.20A1-175[»]
1DSLX-ray1.55A88-175[»]
1GAMX-ray2.60A/B88-173[»]
1GCSX-ray2.00A1-175[»]
1I5IX-ray2.40A1-175[»]
4GCRX-ray1.47A1-175[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000021770. Bos taurus. [Contig view]
GeneID281720.
KEGGbta:281720.

Phylogenomic databases

HOVERGENP02526.

Family and domain databases

InterProIPR001064. Crystallin.
[Graphical view]
Gene3DG3DSA:2.60.20.10. Crystallin. 2 hits.
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP02526.

Entry information

Entry nameCRGB_BOVIN
AccessionPrimary (citable) accession number: P02526
Secondary accession number(s): A2TJU8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 4, 2008
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents