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Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Contributes 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi102Zinc 1By similarity1
Metal bindingi123Zinc 2By similarity1
Metal bindingi125Zinc 2By similarity1
Metal bindingi130Zinc 1By similarity1
Metal bindingi138Zinc 1By similarity1

GO - Molecular functioni

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
Gene namesi
Name:CRYAA
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001258711 – 196Alpha-crystallin A chainAdd BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCurated1
Modified residuei6Deamidated glutamine; partialBy similarity1
Modified residuei21Omega-N-methylated arginineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei50Deamidated glutamine; partialBy similarity1
Modified residuei93N6-acetyllysineBy similarity1
Modified residuei122N6-acetyllysineBy similarity1
Modified residuei124Deamidated asparagine; partialBy similarity1
Modified residuei145PhosphoserineBy similarity1
Modified residuei146Deamidated asparagine; partialBy similarity1
Modified residuei170Deamidated glutamine; partialBy similarity1
Glycosylationi185O-linked (GlcNAc)By similarity1

Post-translational modificationi

Acetylation at Lys-93 seems to increase chaperone activity.By similarity
Undergoes age-dependent proteolytical cleavage at the C-terminus.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

PTM databases

UniCarbKBiP02497.

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP02497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOVERGENiHBG054766.
OrthoDBiEOG091G0USC.

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. 2 hits.
PTHR11527:SF36. PTHR11527:SF36. 2 hits.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P02497-1) [UniParc]FASTAAdd to basket
Also known as: Minor, Alpha-A(ins)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDVTIQHPWF KRALGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ
60 70 80 90 100
SLFRTVLDSG ISELMTHMWF VMHQPHAGNP KNNPIKVRSD RDKFVIFLDV
110 120 130 140 150
KHFSPEDLTV KVLEDFVEIH GKHNERQDDH GYISREFHRR YRLPSNVDQS
160 170 180 190
ALSCSLSADG MLTFSGPKVQ SGLDAGHSER AIPVSREEKP SSAPSS
Length:196
Mass (Da):22,503
Last modified:April 1, 1988 - v1
Checksum:i8A60E0DFA827FFB1
GO
Isoform 2 (identifier: P02497-2) [UniParc]FASTAAdd to basket
Also known as: Major

The sequence of this isoform differs from the canonical sequence as follows:
     64-86: Missing.

Show »
Length:173
Mass (Da):19,792
Checksum:iE146E3F488591F93
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01191564 – 86Missing in isoform 2. 1 PublicationAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02950 Genomic DNA. Translation: CAA26696.1.
X02951 Genomic DNA. Translation: CAA26697.1.
PIRiA02900. CYHYAM.
D94432. CYHYA.
I48183.
RefSeqiXP_005070744.1. XM_005070687.2. [P02497-1]
XP_005070745.1. XM_005070688.2. [P02497-2]

Genome annotation databases

GeneIDi101828899.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02950 Genomic DNA. Translation: CAA26696.1.
X02951 Genomic DNA. Translation: CAA26697.1.
PIRiA02900. CYHYAM.
D94432. CYHYA.
I48183.
RefSeqiXP_005070744.1. XM_005070687.2. [P02497-1]
XP_005070745.1. XM_005070688.2. [P02497-2]

3D structure databases

ProteinModelPortaliP02497.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

UniCarbKBiP02497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101828899.

Organism-specific databases

CTDi1409.

Phylogenomic databases

HOVERGENiHBG054766.
OrthoDBiEOG091G0USC.

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. 2 hits.
PTHR11527:SF36. PTHR11527:SF36. 2 hits.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRYAA_MESAU
AccessioniPrimary (citable) accession number: P02497
Secondary accession number(s): P02490, P82532, Q61444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: September 7, 2016
This is version 98 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

Direct protein sequencing

Documents

  1. 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.