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P02522 (CRBB2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-crystallin B2
Alternative name(s):
Beta-B2 crystallin
Beta-crystallin Bp
Gene names
Name:CRYBB2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length205 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.

Subunit structure

Homo/heterodimer, or complexes of higher order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 205204Beta-crystallin B2
PRO_0000057552

Regions

Domain17 – 5640Beta/gamma crystallin 'Greek key' 1
Domain57 – 10145Beta/gamma crystallin 'Greek key' 2
Domain107 – 14842Beta/gamma crystallin 'Greek key' 3
Domain149 – 19143Beta/gamma crystallin 'Greek key' 4
Region2 – 1615N-terminal arm
Region102 – 1065Connecting peptide
Region193 – 20513C-terminal arm

Sites

Site181Not glycated
Site421Not glycated
Site591Susceptible to oxidation By similarity
Site1221Susceptible to oxidation By similarity
Site1511Susceptible to oxidation By similarity

Amino acid modifications

Modified residue21N-acetylalanine
Modified residue421N6-methylated lysine By similarity
Modified residue681N6-methylated lysine By similarity
Modified residue761N6-acetyllysine By similarity
Modified residue1181Phosphothreonine By similarity
Modified residue1211N6-acetyllysine; alternate By similarity
Modified residue1211N6-methylated lysine; alternate By similarity
Glycosylation111N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation481N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation681N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation761N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1011N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1081N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1201N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1211N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1401N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1681N-linked (Glc) (glycation); in vitro Ref.3
Glycosylation1721N-linked (Glc) (glycation); in vitro Ref.3

Experimental info

Sequence conflict41D → N AA sequence Ref.1
Sequence conflict61Q → E AA sequence Ref.1
Sequence conflict281Q → H AA sequence Ref.1
Sequence conflict321H → Q AA sequence Ref.1
Sequence conflict36 – 372GP → PG AA sequence Ref.1
Sequence conflict401N → C AA sequence Ref.1

Secondary structure

1 ...................................... 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02522 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9613C228491E3C8C

FASTA20523,298
        10         20         30         40         50         60 
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV 

        70         80         90        100        110        120 
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKIT LYENPNFTGK 

       130        140        150        160        170        180 
KMEVIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSGDFGAP 

       190        200 
QPQVQSVRRI RDMQWHQRGA FHPSS

« Hide

References

[1]"Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin."
Driessen H.P.C., Herbrink P., Bloemendal H., de Jong W.W.
Eur. J. Biochem. 121:83-91(1981) [PubMed: 7035168] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-205.
[2]"Nucleotide sequence for the cDNA of the bovine beta B2 crystallin and assignment of the orthologous human locus to chromosome 22."
Hogg D., Gorin M.B., Heinzmann C., Zollmann S., Mohandas T., Klisak I., Sparkes R.S., Breitman M., Tsui L.-C., Horwitz J.
Curr. Eye Res. 6:1335-1342(1987) [PubMed: 3427982] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Sites of glycation of beta B2-crystallin by glucose and fructose."
Zhao H.R., Smith J.B., Jiang X.Y., Abraham E.C.
Biochem. Biophys. Res. Commun. 229:128-133(1996) [PubMed: 8954094] [Abstract]
Cited for: GLYCATION AT LYS-11; LYS-48; LYS-68; LYS-76; LYS-101; LYS-108; LYS-120; LYS-121; LYS-140; LYS-168 AND LYS-172, ABSENCE OF GLYCATION AT LYS-18 AND LYS-42, MASS SPECTROMETRY.
[4]"X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins."
Bax B., Lapatto R., Nalini V., Driessen H.P.C., Lindley P.F., Mahadevan D., Blundell T.L., Slingsby C.
Nature 347:776-780(1990) [PubMed: 2234050] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SEQUENCE REVISION.
[5]"1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions."
Carver J.A., Cooper P.G., Truscott R.J.
Eur. J. Biochem. 213:313-320(1993) [PubMed: 8477703] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22466 mRNA. Translation: AAA30472.1.
IPIIPI00696387.
PIRCYBOB. A54730.
RefSeqNP_777232.1. NM_174807.1.
UniGeneBt.398.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BLBX-ray3.30A/B/C/D2-204[»]
2BB2X-ray2.10A15-195[»]
ProteinModelPortalP02522.
SMRP02522. Positions 9-195.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000005341; ENSBTAP00000005341; ENSBTAG00000004088.
GeneID287011.
KEGGbta:287011.

Organism-specific databases

CTD1415.

Phylogenomic databases

eggNOGmaNOG10808.
GeneTreeENSGT00560000076861.
HOVERGENHBG003364.
InParanoidP02522.
OMAKETGMEK.
OrthoDBEOG44F6B3.
PhylomeDBP02522.

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
Gene3DG3DSA:2.60.20.10. Crystallin. 2 hits.
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. G_crystallin_SF. 1 hit.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCRBB2_BOVIN
AccessionPrimary (citable) accession number: P02522
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 21, 2011
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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