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Protein

Alpha-crystallin A chain

Gene

Cryaa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.

Miscellaneous

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

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
  • unfolded protein binding Source: RGD

GO - Biological processi

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-binding, Zinc

Names & Taxonomyi

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

Organism-specific databases

RGDi2413 Cryaa

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_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) serineBy 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

GlyConnecti34
iPTMnetiP24623
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 Homo sapiens.

GO - Molecular functioni

  • identical protein binding Source: RGD
  • unfolded protein binding Source: RGD

Protein-protein interaction databases

BioGridi246457, 1 interactor
IntActiP24623, 1 interactor
MINTiP24623
STRINGi10116.ENSRNOP00000065714

Structurei

3D structure databases

ProteinModelPortaliP24623
SMRiP24623
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 185sHSPPROSITE-ProRule annotationAdd BLAST110

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00760000119238
HOVERGENiHBG054766
InParanoidiP24623
KOiK09541
OMAiGERQDDH
OrthoDBiEOG091G0USC
PhylomeDBiP24623

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:SF36 PTHR11527:SF36, 1 hit
PfamiView protein in Pfam
PF00525 Crystallin, 1 hit
PF00011 HSP20, 1 hit
PRINTSiPR00299 ACRYSTALLIN
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS01031 SHSP, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCRYAA_RAT
AccessioniPrimary (citable) accession number: P24623
Secondary accession number(s): P02490
, P02496, P82532, Q61444
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: April 25, 2018
This is version 132 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

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health