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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi100 – 1001Zinc 21 Publication
Metal bindingi102 – 1021Zinc 21 Publication
Metal bindingi107 – 1071Zinc 11 Publication
Metal bindingi115 – 1151Zinc 1By similarity

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

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-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

  • 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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Alpha-crystallin A chainPRO_0000125848Add
BLAST
Chaini1 – 172172Alpha-crystallin A(1-172)PRO_0000226605Add
BLAST
Chaini1 – 168168Alpha-crystallin A(1-168)PRO_0000423502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei6 – 61Deamidated glutamine; partialBy similarity
Glycosylationi11 – 111N-linked (Glc) (glycation)
Modified residuei21 – 211Omega-N-methylated arginineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei50 – 501Deamidated glutamine; partialBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Glycosylationi78 – 781N-linked (Glc) (glycation)
Modified residuei90 – 901Deamidated glutamine; partialBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei101 – 1011Deamidated asparagine; partialBy similarity
Modified residuei122 – 1221Phosphoserine1 Publication
Modified residuei123 – 1231Deamidated asparagine; partialBy similarity
Glycosylationi162 – 1621O-linked (GlcNAc)1 PublicationCAR_000056

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei70 – 701Not glycated
Sitei88 – 881Not glycated
Sitei99 – 991Not glycated
Sitei145 – 1451Not glycated
Sitei166 – 1661Not glycated

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02470.
PRIDEiP02470.

PTM databases

iPTMnetiP02470.
UniCarbKBiP02470.

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

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 666Combined sources
Beta strandi68 – 769Combined sources
Helixi82 – 843Combined sources
Beta strandi85 – 906Combined sources
Beta strandi93 – 10412Combined sources
Turni105 – 1073Combined sources
Beta strandi108 – 11912Combined sources
Beta strandi130 – 1334Combined sources
Beta strandi137 – 1459Combined sources
Turni150 – 1534Combined sources
Beta strandi154 – 1563Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP02470.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1637Important for oligomerization

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.
OMAiGPKVQSG.
OrthoDBiEOG7WHHBK.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-58566N.
STRINGi9913.ENSBTAP00000004073.

PTM databases

iPTMnetiP02470.
UniCarbKBiP02470.

Proteomic databases

PaxDbiP02470.
PRIDEiP02470.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1409.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02470.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG7WHHBK.
TreeFamiTF105049.

Miscellaneous databases

EvolutionaryTraceiP02470.
NextBioi20805639.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The amino-acid sequence of the alphaA2 chain of bovine alpha-crystallin."
    van der Ouderaa F.J., de Jong W.W., Bloemendal H.
    Eur. J. Biochem. 39:207-222(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Nucleotide sequence of a bovine lens alpha A-crystallin cDNA."
    Hay R.E., Petrash J.M.
    Biochem. Biophys. Res. Commun. 148:31-37(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Elucidation of the primary structures of proteins by mass spectrometry."
    Smith J.B., Thevenon-Emeric G., Simth D.L., Green B.
    Anal. Biochem. 193:118-124(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-122.
  4. "Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine."
    Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A., Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.
    J. Biol. Chem. 267:555-563(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-162.
  5. "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-11 AND LYS-78, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Identification of the in vivo truncation sites at the C-terminal region of alpha-A crystallin from aged bovine and human lens."
    Takemoto L.J.
    Curr. Eye Res. 14:837-841(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  7. "Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function."
    Laganowsky A., Benesch J.L., Landau M., Ding L., Sawaya M.R., Cascio D., Huang Q., Robinson C.V., Horwitz J., Eisenberg D.
    Protein Sci. 19:1031-1043(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 59-163 IN COMPLEX WITH ZINC, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiCRYAA_BOVIN
AccessioniPrimary (citable) accession number: P02470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 126 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.