Q7M2W6 (CRYAB_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-crystallin B chain

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

Gene names

Name:

CRYAB

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
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 Glycoprotein Methylation Oxidation Phosphoprotein
Technical term	Complete proteome 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 electronic annotation. Source: Compara 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 electronic annotation. Source: Compara 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_0000252666
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 By similarity
	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
	Glycosylation	170	1	O-linked (GlcNAc) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7M2W6 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: EE372A30D83E9752	FASTA	175	20,129
	10 20 30 40 50 60 MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYFR PPSFLRAPSW 70 80 90 100 110 120 IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 130 140 150 160 170 KYRIPADVDP LTITSSLSSD GVLTVNGPRR QASGPERTIP ITREEKPAVT AAPKK

References

[1]	"Characterization, cloning, and expression of porcine alpha B crystallin." Liao J.H., Hung C.C., Lee J.S., Wu S.H., Chiou S.H. Biochem. Biophys. Res. Commun. 244:131-137(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.

Cross-references

Sequence databases
PIR	JC5971.
RefSeq	XP_003357342.1. XM_003357294.1.
3D structure databases
ProteinModelPortal	Q7M2W6.
ModBase	Search...
Proteomic databases
PaxDb	Q7M2W6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000016389; ENSSSCP00000015948; ENSSSCG00000015025.
GeneID	100519789.
KEGG	ssc:100519789.
Organism-specific databases
CTD	1410.
Phylogenomic databases
eggNOG	NOG246790.
GeneTree	ENSGT00550000074302.
HOGENOM	HOG000233954.
HOVERGEN	HBG054766.
KO	K09542.
OMA	GPRKQAP.
OrthoDB	EOG4G1MHK.
Gene expression databases
ArrayExpress	Q7M2W6.
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...

Entry information

Entry name

CRYAB_PIG

Accession

Primary (citable) accession number: Q7M2W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	December 15, 2003
Last modified:	April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program