P23927 (CRYAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-crystallin B chain

Alternative name(s):
Alpha(B)-crystallin
P23

Gene names

Name:	Cryab
Synonyms:	Crya2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.6
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.
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 Methylation Oxidation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara apoptotic process involved in morphogenesis Inferred from genetic interaction PubMed 16439475. Source: MGI glucose metabolic process Inferred from electronic annotation. Source: Compara lens development in camera-type eye Inferred from genetic interaction PubMed 16439475. Source: MGI microtubule polymerization or depolymerization Inferred from electronic annotation. Source: Compara muscle organ development Inferred from genetic interaction PubMed 11687538. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 18191123. Source: MGI negative regulation of cell growth Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from genetic interaction PubMed 16439475. Source: MGI negative regulation of gene expression Inferred from mutant phenotype PubMed 17893660. Source: MGI negative regulation of intracellular transport Inferred from electronic annotation. Source: Compara negative regulation of reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from mutant phenotype PubMed 17438522. Source: MGI response to hypoxia Inferred from mutant phenotype PubMed 18191123. Source: MGI stress-activated MAPK cascade Inferred from electronic annotation. Source: Compara tubulin complex assembly Inferred from mutant phenotype PubMed 16675842. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara Z disc Inferred from direct assay PubMed 14627610. Source: MGI actin filament bundle Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 18191123. Source: MGI microtubule cytoskeleton Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 18191123. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from direct assay PubMed 14627610. Source: MGI
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 Traceable author statement PubMed 12546709. Source: MGI
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_0000125910
Sites
	Metal binding	104	1	Zinc By similarity
	Metal binding	111	1	Zinc By similarity
	Metal binding	119	1	Zinc By similarity
	Site	48	1	Susceptible to oxidation By similarity
	Site	60	1	Susceptible to oxidation By similarity
	Site	68	1	Susceptible to oxidation By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Probable
	Modified residue	19	1	Phosphoserine By similarity
	Modified residue	22	1	Omega-N-methylated arginine By similarity
	Modified residue	45	1	Phosphoserine By similarity
	Modified residue	50	1	Omega-N-methylated arginine By similarity
	Modified residue	59	1	Phosphoserine By similarity
	Modified residue	92	1	N6-acetyllysine By similarity
	Modified residue	166	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23927 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 46702976C008EFD3	FASTA	175	20,069
	10 20 30 40 50 60 MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW 70 80 90 100 110 120 IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 130 140 150 160 170 KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts." Klemenz R., Froehli E., Aoyama A., Hoffmann S., Simpson R.J., Moritz R.L., Schaeffer R. Mol. Cell. Biol. 11:803-812(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10 AND 68-81.
[2]	"Structure and alternate tissue-preferred transcription initiation of the mouse alpha B-crystallin/small heat shock protein gene." Frederikse P.H., Dubin R.A., Haynes J.I., Piatigorsky J. Nucleic Acids Res. 22:5686-5694(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Lung.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[4]	"Expression of the murine alpha B-crystallin gene is not restricted to the lens." Dubin R.A., Wawrousek E.F., Piatigorsky J. Mol. Cell. Biol. 9:1083-1091(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[5]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 12-22 AND 124-149, MASS SPECTROMETRY. Tissue: Hippocampus.
[6]	"Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27." Liu C., Gilmont R.R., Benndorf R., Welsh M.J. J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPBAP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M63170 mRNA. Translation: AAA37472.1. M73741 Genomic DNA. Translation: AAA67045.1. BC010768 mRNA. Translation: AAH10768.1. M25770 Genomic DNA. Translation: AAA37133.1.
IPI	IPI00138274.
PIR	A39608.
RefSeq	NP_034094.1. NM_009964.2.
UniGene	Mm.178.
3D structure databases
ProteinModelPortal	P23927.
SMR	P23927. Positions 1-175.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31060N.
IntAct	P23927. 9 interactions.
PTM databases
PhosphoSite	P23927.
2D gel databases
SWISS-2DPAGE	P23927.
Proteomic databases
PaxDb	P23927.
PRIDE	P23927.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
GeneID	12955.
KEGG	mmu:12955.
Organism-specific databases
CTD	1410.
MGI	MGI:88516. Cryab.
Phylogenomic databases
eggNOG	NOG246790.
HOGENOM	HOG000233954.
HOVERGEN	HBG054766.
InParanoid	P23927.
KO	K09542.
OMA	GPRKQAP.
OrthoDB	EOG4G1MHK.
Gene expression databases
ArrayExpress	P23927.
Bgee	P23927.
CleanEx	MM_CRYAB.
Genevestigator	P23927.
GermOnline	ENSMUSG00000032060. Mus musculus.
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
ChiTaRS	CRYAB. mouse.
NextBio	282674.
SOURCE	Search...

Entry information

Entry name

CRYAB_MOUSE

Accession

Primary (citable) accession number: P23927
Secondary accession number(s): Q64325

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	July 15, 1999
Last modified:	April 3, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program