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Protein

Gamma-crystallin B

Gene

CRYGB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-crystallin B
Alternative name(s):
Gamma-B-crystallin
Gamma-crystallin II
Gene namesi
Name:CRYGB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 175174Gamma-crystallin BPRO_0000057581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi3 – 31N-linked (Glc) (glycation); in vitro
Disulfide bondi19 ↔ 231 Publication

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein

Proteomic databases

PaxDbiP02526.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009553.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Helixi10 – 123Combined sources
Beta strandi13 – 197Combined sources
Turni27 – 293Combined sources
Beta strandi34 – 418Combined sources
Beta strandi43 – 486Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 587Combined sources
Beta strandi60 – 656Combined sources
Helixi66 – 694Combined sources
Beta strandi72 – 743Combined sources
Beta strandi78 – 814Combined sources
Beta strandi90 – 967Combined sources
Turni97 – 993Combined sources
Beta strandi100 – 1067Combined sources
Helixi113 – 1175Combined sources
Beta strandi124 – 1307Combined sources
Beta strandi132 – 1376Combined sources
Turni138 – 1403Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi149 – 1524Combined sources
Helixi155 – 1584Combined sources
Beta strandi167 – 1704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMMX-ray1.20A2-175[»]
1DSLX-ray1.55A88-175[»]
1GAMX-ray2.60A/B88-173[»]
1GCSX-ray2.00A2-175[»]
1I5IX-ray2.40A2-175[»]
4GCRX-ray1.47A2-175[»]
4W9AX-ray1.38A1-175[»]
4W9BX-ray1.28A1-175[»]
ProteinModelPortaliP02526.
SMRiP02526. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02526.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 4039Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini41 – 8343Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini89 – 12941Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini130 – 17243Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 885Connecting peptide

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
Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IWCR. Eukaryota.
ENOG411298R. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP02526.
OMAiFRGQMSE.
OrthoDBiEOG70CR7Z.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02526-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKITFYEDR GFQGHCYECS SDCPNLQPYF SRCNSIRVDS GCWMLYERPN
60 70 80 90 100
YQGHQYFLRR GDYPDYQQWM GFNDSIRSCR LIPQHTGTFR MRIYERDDFR
110 120 130 140 150
GQMSEITDDC PSLQDRFHLT EVHSLNVLEG SWVLYEMPSY RGRQYLLRPG
160 170
EYRRYLDWGA MNAKVGSLRR VMDFY
Length:175
Mass (Da):21,097
Last modified:January 23, 2007 - v2
Checksum:i0CF283DA837CC593
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201T → S in CAA25518 (PubMed:6092016).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01036 mRNA. Translation: CAA25518.1.
M16894 mRNA. Translation: AAA30476.1.
EF208024 mRNA. Translation: ABM97504.1.
PIRiA29655. CYBOG.
RefSeqiNP_001013612.1. NM_001013594.1.
UniGeneiBt.399.

Genome annotation databases

EnsembliENSBTAT00000009553; ENSBTAP00000009553; ENSBTAG00000021770.
GeneIDi281720.
KEGGibta:281720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01036 mRNA. Translation: CAA25518.1.
M16894 mRNA. Translation: AAA30476.1.
EF208024 mRNA. Translation: ABM97504.1.
PIRiA29655. CYBOG.
RefSeqiNP_001013612.1. NM_001013594.1.
UniGeneiBt.399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AMMX-ray1.20A2-175[»]
1DSLX-ray1.55A88-175[»]
1GAMX-ray2.60A/B88-173[»]
1GCSX-ray2.00A2-175[»]
1I5IX-ray2.40A2-175[»]
4GCRX-ray1.47A2-175[»]
4W9AX-ray1.38A1-175[»]
4W9BX-ray1.28A1-175[»]
ProteinModelPortaliP02526.
SMRiP02526. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009553.

Proteomic databases

PaxDbiP02526.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009553; ENSBTAP00000009553; ENSBTAG00000021770.
GeneIDi281720.
KEGGibta:281720.

Organism-specific databases

CTDi1419.

Phylogenomic databases

eggNOGiENOG410IWCR. Eukaryota.
ENOG411298R. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234389.
HOVERGENiHBG003364.
InParanoidiP02526.
OMAiFRGQMSE.
OrthoDBiEOG70CR7Z.

Miscellaneous databases

EvolutionaryTraceiP02526.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26.
  5. 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] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-3, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-57.

Entry informationi

Entry nameiCRGB_BOVIN
AccessioniPrimary (citable) accession number: P02526
Secondary accession number(s): A2TJU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.