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Protein

Alpha-crystallin A chain

Gene

Cryaa

Organism
Rattus norvegicus (Rat)
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. Isoform 1 is capable of inhibiting bacterial growth in the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. C-terminal truncated forms alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) have lower chaperone activity.

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

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Cryaa
Synonyms:Crya1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2413. Cryaa.

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001258831 – 196Alpha-crystallin A chainAdd BLAST196
ChainiPRO_00004235051 – 191Alpha-crystallin A(1-168)Add BLAST191
ChainiPRO_00004235061 – 188Alpha-crystallin A(1-165)Add BLAST188
ChainiPRO_00004235071 – 186Alpha-crystallin A(1-163)Add BLAST186
ChainiPRO_00004235081 – 185Alpha-crystallin A(1-162)Add BLAST185
ChainiPRO_00004235091 – 180Alpha-crystallin A(1-157)Add BLAST180
ChainiPRO_00004235101 – 179Alpha-crystallin A(1-156)Add BLAST179
ChainiPRO_00004235111 – 174Alpha-crystallin A(1-151)Add BLAST174

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
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. Cleavage by m-calpain produces specifically alpha-crystallin A(1-162), cleavage by Capn3/Lp82 produces specifically alpha-crystallin A(1-168) which is the major truncated form during normal maturation and induced cataract formation.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP24623.

PTM databases

UniCarbKBiP24623.

Expressioni

Tissue specificityi

Highly expressed in eye lens. Also expressed in non-lenticular tissues such as brain, spleen, liver, lung, skin, small intestine and a several epithelial and fibroblast cell lines with highest levels in spleen.1 Publication

Gene expression databases

BgeeiENSRNOG00000047175.
ExpressionAtlasiP24623. baseline and differential.
GenevisibleiP24623. RN.

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 homooligomers (By similarity). Age-dependent C-terminal truncation affects oligomerization. Whereas alpha-crystallin A(1-168) behaves unchanged, specifically alpha-crystallin A(1-162), alpha-crystallin A(1-157) and alpha-crystallin A(1-151) show decreased oligomerization.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYGDP073202EBI-7673244,EBI-7673124From a different organism.

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

BioGridi246457. 1 interactor.
IntActiP24623. 1 interactor.
MINTiMINT-8303018.
STRINGi10116.ENSRNOP00000065714.

Structurei

3D structure databases

ProteinModelPortaliP24623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOVERGENiHBG054766.
InParanoidiP24623.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG091G0USC.
PhylomeDBiP24623.

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.

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

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

Isoform 1 (identifier: P24623-1) [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 KNNPGKVRSD RDKFVIFLDV
110 120 130 140 150
KHFSPEDLTV KVLEDFVEIH GKHNERQDDH GYISREFHRR YRLPSNVDQS
160 170 180 190
ALSCSLSADG MLTFSGPKVQ SGLDAGHSER AIPVSREEKP SSAPSS
Length:196
Mass (Da):22,447
Last modified:March 1, 1992 - v1
Checksum:iD0C0E0DFA82D551C
GO
Isoform 2 (identifier: P24623-2) [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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147V → M in AAA40645 (PubMed:1429679).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01191764 – 86Missing in isoform 2. 4 PublicationsAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47921 mRNA. Translation: AAA93366.1.
U47922 mRNA. Translation: AAA93367.1.
V01219 mRNA. Translation: CAA24530.1.
M96949 mRNA. Translation: AAA40644.1.
M96950 mRNA. Translation: AAA40645.1.
PIRiA02892. CYRTA.
A02899. CYRTAM.
S07530.
RefSeqiNP_001276666.1. NM_001289737.1. [P24623-1]
NP_036666.2. NM_012534.4. [P24623-2]
UniGeneiRn.127769.

Genome annotation databases

EnsembliENSRNOT00000071248; ENSRNOP00000067332; ENSRNOG00000047175. [P24623-2]
ENSRNOT00000075545; ENSRNOP00000065714; ENSRNOG00000047175. [P24623-1]
GeneIDi24273.
KEGGirno:24273.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U47921 mRNA. Translation: AAA93366.1.
U47922 mRNA. Translation: AAA93367.1.
V01219 mRNA. Translation: CAA24530.1.
M96949 mRNA. Translation: AAA40644.1.
M96950 mRNA. Translation: AAA40645.1.
PIRiA02892. CYRTA.
A02899. CYRTAM.
S07530.
RefSeqiNP_001276666.1. NM_001289737.1. [P24623-1]
NP_036666.2. NM_012534.4. [P24623-2]
UniGeneiRn.127769.

3D structure databases

ProteinModelPortaliP24623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246457. 1 interactor.
IntActiP24623. 1 interactor.
MINTiMINT-8303018.
STRINGi10116.ENSRNOP00000065714.

PTM databases

UniCarbKBiP24623.

Proteomic databases

PaxDbiP24623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071248; ENSRNOP00000067332; ENSRNOG00000047175. [P24623-2]
ENSRNOT00000075545; ENSRNOP00000065714; ENSRNOG00000047175. [P24623-1]
GeneIDi24273.
KEGGirno:24273.

Organism-specific databases

CTDi1409.
RGDi2413. Cryaa.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOVERGENiHBG054766.
InParanoidiP24623.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG091G0USC.
PhylomeDBiP24623.

Miscellaneous databases

PROiP24623.

Gene expression databases

BgeeiENSRNOG00000047175.
ExpressionAtlasiP24623. baseline and differential.
GenevisibleiP24623. RN.

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_RAT
AccessioniPrimary (citable) accession number: P24623
Secondary accession number(s): P02490
, P02496, P82532, Q61444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: September 7, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Lenses of streptozotocin-induced diabetic rats show increased levels of C-terminal truncated forms.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.