Alpha-crystallin B chain - Bos taurus (Bovine)

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P02510 (CRYAB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-crystallin B chain

Alternative name(s):
Alpha(B)-crystallin

Gene names

Name:	CRYAB
Synonyms:	CRYA2

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Subunit structure	Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles By similarity.
Tissue specificity	Lens as well as other tissues.
Post-translational modification	It is not known whether either Lys-90, or Lys-92, or both are glycated.
Sequence similarities	Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Chaperone Eye lens protein
PTM	Acetylation Glycation Glycoprotein Methylation Oxidation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process involved in morphogenesis Inferred from electronic annotation. Source: Compara lens development in camera-type eye Inferred from electronic annotation. Source: Compara muscle organ development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: AgBase negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of gene expression Inferred from electronic annotation. Source: Compara negative regulation of intracellular transport Inferred from sequence or structural similarity. Source: AgBase protein homooligomerization Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara tubulin complex assembly Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 175

175

Alpha-crystallin B chain

PRO_0000125906

Sites

Metal binding

104

Zinc By similarity

Metal binding

111

Zinc By similarity

Metal binding

119

Zinc By similarity

Site

Susceptible to oxidation By similarity

Site

Susceptible to oxidation By similarity

Site

Susceptible to oxidation By similarity

Site

Not glycated

Site

Not glycated

Site

103

Not glycated

Site

121

Not glycated

Site

150

Not glycated

Site

166

Not glycated

Site

174

Not glycated

Site

175

Not glycated

Amino acid modifications

Modified residue

N-acetylmethionine Ref.1

Modified residue

Phosphoserine Ref.7 Ref.8

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Phosphoserine Ref.6 Ref.7 Ref.8

Modified residue

Omega-N-methylated arginine By similarity

Modified residue

Phosphoserine Ref.6 Ref.8

Modified residue

N6-acetyllysine; alternate By similarity

Modified residue

166

N6-acetyllysine By similarity

Glycosylation

N-linked (Glc) (glycation) Probable

Glycosylation

N-linked (Glc) (glycation); alternate Probable

Sequences

Sequence

Length

Mass (Da)

Tools

P02510 [UniParc].

Last modified November 1, 1991. Version 2.
Checksum: E0CFBBA8D6DE82B2
Show »

FASTA

175

20,037

        10         20         30         40         50         60 
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR PPSFLRAPSW 

        70         80         90        100        110        120 
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 

       130        140        150        160        170 
KYRIPADVDP LAITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The amino-acids sequence of the alphaB2 chain of bovine alpha-crystallin." van der Ouderaa F.J., de Jong W.W., Hilderink A., Bloemendal H. Eur. J. Biochem. 49:157-168(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	de Jong W.W. Submitted (NOV-1991) to UniProtKB Cited for: SEQUENCE REVISION TO 80.
[3]	Kelley P.B., Abraham E.C., Zhao H.R., Shroff N.P., Cherian M., Thomas J.J. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Testis.
[5]	"Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein." Merck K.B., Horwitz J., Kersten M., Overkamp P., Gaestel M., Bloemendal H., de Jong W.W. Mol. Biol. Rep. 18:209-215(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-175.
[6]	"The phosphorylation sites of the B2 chain of bovine alpha-crystallin." Chiesa R., Gawinowicz-Kolks M.A., Kleiman N.J., Spector A. Biochem. Biophys. Res. Commun. 144:1340-1347(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-45 AND SER-59.
[7]	"The in vivo phosphorylation sites of bovine alpha B-crystallin." Voorter C.E.M., de Haard-Hoekman W.A., Roersma E.S., Meyer H.E., Bloemendal H., de Jong W.W. FEBS Lett. 259:50-52(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-19 AND SER-45.
[8]	"Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry." Smith J.B., Sun Y., Smith D.L., Green B. Protein Sci. 1:601-608(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 80, PHOSPHORYLATION AT SER-19; SER-45 AND SER-59.
[9]	"Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose." Abraham E.C., Cherian M., Smith J.B. Biochem. Biophys. Res. Commun. 201:1451-1456(1994) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCATION AT LYS-90 AND LYS-92, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF029793 mRNA. Translation: AAB95323.2. BC102745 mRNA. Translation: AAI02746.1.
IPI	IPI00688530.
PIR	CYBOAB. A42446.
RefSeq	NP_776715.1. NM_174290.2.
UniGene	Bt.88059.
3D structure databases
ProteinModelPortal	P02510.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-43761N.
MINT	MINT-1486058.
STRING	9913.ENSBTAP00000000556.
PTM databases
GlycoSuiteDB	P02510.
2D gel databases
UCD-2DPAGE	P02510.
Proteomic databases
PaxDb	P02510.
PRIDE	P02510.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000000556; ENSBTAP00000000556; ENSBTAG00000000434.
GeneID	281719.
KEGG	bta:281719.
Organism-specific databases
CTD	1410.
Phylogenomic databases
eggNOG	NOG246790.
GeneTree	ENSGT00550000074302.
HOGENOM	HOG000233954.
HOVERGEN	HBG054766.
InParanoid	P02510.
KO	K09542.
OMA	GPRKQAP.
OrthoDB	EOG4G1MHK.
Family and domain databases
InterPro	IPR002068. a-crystallin/Hsp20_dom. IPR001436. Alpha-crystallin/HSP. IPR012273. Alpha-crystallin_B. IPR003090. Alpha-crystallin_N. IPR008978. HSP20-like_chaperone. [Graphical view]
PANTHER	PTHR11527:SF37. PTHR11527:SF37. 1 hit.
Pfam	PF00525. Crystallin. 1 hit. PF00011. HSP20. 1 hit. [Graphical view]
PIRSF	PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTS	PR00299. ACRYSTALLIN.
SUPFAM	SSF49764. HSP20_chap. 1 hit.
PROSITE	PS01031. HSP20. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20805640.

Entry information

Entry name

CRYAB_BOVIN

Accession

Primary (citable) accession number: P02510
Secondary accession number(s): O46508, Q3SZQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1991
Last modified:	April 3, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents