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Protein

Alpha-crystallin A chain

Gene

CRYAA

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

Functioni

Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi79Zinc 1By similarity1
Metal bindingi100Zinc 21 Publication1
Metal bindingi102Zinc 21 Publication1
Metal bindingi107Zinc 11 Publication1
Metal bindingi115Zinc 1By similarity1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • structural constituent of eye lens Source: UniProtKB-KW
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin A chain
Cleaved into the following 2 chains:
Gene namesi
Name:CRYAA
Synonyms:CRYA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001258481 – 173Alpha-crystallin A chainAdd BLAST173
ChainiPRO_00002266051 – 172Alpha-crystallin A(1-172)Add BLAST172
ChainiPRO_00004235021 – 168Alpha-crystallin A(1-168)Add BLAST168

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei6Deamidated glutamine; partialBy similarity1
Glycosylationi11N-linked (Glc) (glycation) lysine1
Modified residuei21Omega-N-methylated arginineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei50Deamidated glutamine; partialBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Glycosylationi78N-linked (Glc) (glycation) lysine1
Modified residuei90Deamidated glutamine; partialBy similarity1
Modified residuei99N6-acetyllysineBy similarity1
Modified residuei101Deamidated asparagine; partialBy similarity1
Modified residuei122Phosphoserine1 Publication1
Modified residuei123Deamidated asparagine; partialBy similarity1
GlycosylationiCAR_000056162O-linked (GlcNAc) serine1 Publication1

Post-translational modificationi

Acetylation at Lys-70 seems to increase chaperone activity.By similarity
Undergoes age-dependent proteolytical cleavage at the C-terminus.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei70Not glycated1
Sitei88Not glycated1
Sitei99Not glycated1
Sitei145Not glycated1
Sitei166Not glycated1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02470.
PRIDEiP02470.

PTM databases

iPTMnetiP02470.
UniCarbKBiP02470.

Expressioni

Gene expression databases

BgeeiENSBTAG00000003134.

Interactioni

Subunit structurei

Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and higher homooligomers.1 Publication

GO - Molecular functioni

  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-58566N.
STRINGi9913.ENSBTAP00000004073.

Structurei

Secondary structure

1173
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi61 – 66Combined sources6
Beta strandi68 – 76Combined sources9
Helixi82 – 84Combined sources3
Beta strandi85 – 90Combined sources6
Beta strandi93 – 104Combined sources12
Turni105 – 107Combined sources3
Beta strandi108 – 119Combined sources12
Beta strandi130 – 133Combined sources4
Beta strandi137 – 145Combined sources9
Turni150 – 153Combined sources4
Beta strandi154 – 156Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3L1EX-ray1.15A59-163[»]
3L1FX-ray1.53A62-163[»]
DisProtiDP00981.
ProteinModelPortaliP02470.
SMRiP02470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02470.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 162sHSPPROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni157 – 163Important for oligomerization7

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02470.
KOiK09541.
OMAiGERQDDH.
OrthoDBiEOG091G0USC.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF205. PTHR11527:SF205. 1 hit.
PfamiView protein in Pfam
PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiView protein in PROSITE
PS01031. SHSP. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02470-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ
60 70 80 90 100
SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ EDFVEIHGKH
110 120 130 140 150
NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FSGPKIPSGV
160 170
DAGHSERAIP VSREEKPSSA PSS
Length:173
Mass (Da):19,790
Last modified:July 21, 1986 - v1
Checksum:i7796ED1B71864478
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26142 mRNA. Translation: AAA30471.1.
PIRiA29656. CYBOA.
RefSeqiNP_776714.1. NM_174289.2.
UniGeneiBt.397.

Genome annotation databases

EnsembliENSBTAT00000004073; ENSBTAP00000004073; ENSBTAG00000003134.
GeneIDi281718.
KEGGibta:281718.

Similar proteinsi

Entry informationi

Entry nameiCRYAA_BOVIN
AccessioniPrimary (citable) accession number: P02470
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 30, 2017
This is version 134 of the entry and version 1 of the sequence. See 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