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P24623

- CRYAA_RAT

UniProt

P24623 - CRYAA_RAT

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Protein

Alpha-crystallin A chain

Gene

Cryaa

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc 1By similarity
Metal bindingi123 – 1231Zinc 2By similarity
Metal bindingi125 – 1251Zinc 2By similarity
Metal bindingi130 – 1301Zinc 1By similarity
Metal bindingi138 – 1381Zinc 1By similarity

GO - Molecular functioni

  1. identical protein binding Source: RGD
  2. metal ion binding Source: UniProtKB-KW
  3. structural constituent of eye lens Source: RGD

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. apoptotic process involved in morphogenesis Source: Ensembl
  3. embryonic camera-type eye morphogenesis Source: Ensembl
  4. lens development in camera-type eye Source: RGD
  5. lens fiber cell morphogenesis Source: Ensembl
  6. microtubule-based process Source: Ensembl
  7. mitochondrion organization Source: Ensembl
  8. negative regulation of apoptotic process Source: Ensembl
  9. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  10. negative regulation of gene expression Source: Ensembl
  11. positive regulation of cell growth Source: Ensembl
  12. positive regulation of protein phosphorylation Source: Ensembl
  13. protein folding Source: RGD
  14. protein homooligomerization Source: RGD
  15. response to drug Source: RGD
  16. response to glucocorticoid Source: RGD
  17. response to hydrogen peroxide Source: RGD
  18. response to hypoxia Source: Ensembl
  19. response to lead ion Source: RGD
  20. response to UV-A Source: Ensembl
  21. tubulin complex assembly Source: Ensembl
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
ProteomesiUP000002494: 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

  1. cytoplasm Source: RGD
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Alpha-crystallin A chainPRO_0000125883Add
BLAST
Chaini1 – 191191Alpha-crystallin A(1-168)PRO_0000423505Add
BLAST
Chaini1 – 188188Alpha-crystallin A(1-165)PRO_0000423506Add
BLAST
Chaini1 – 186186Alpha-crystallin A(1-163)PRO_0000423507Add
BLAST
Chaini1 – 185185Alpha-crystallin A(1-162)PRO_0000423508Add
BLAST
Chaini1 – 180180Alpha-crystallin A(1-157)PRO_0000423509Add
BLAST
Chaini1 – 179179Alpha-crystallin A(1-156)PRO_0000423510Add
BLAST
Chaini1 – 174174Alpha-crystallin A(1-151)PRO_0000423511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei6 – 61Deamidated glutamine; partialBy similarity
Modified residuei21 – 211Omega-N-methylated arginineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei50 – 501Deamidated glutamine; partialBy similarity
Modified residuei93 – 931N6-acetyllysineBy similarity
Modified residuei122 – 1221N6-acetyllysineBy similarity
Modified residuei124 – 1241Deamidated asparagine; partialBy similarity
Modified residuei145 – 1451PhosphoserineBy similarity
Modified residuei146 – 1461Deamidated asparagine; partialBy similarity
Modified residuei170 – 1701Deamidated glutamine; partialBy similarity
Glycosylationi185 – 1851O-linked (GlcNAc)By similarity

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

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

ExpressionAtlasiP24623. baseline.
GenevestigatoriP24623.

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.

Protein-protein interaction databases

BioGridi246457. 1 interaction.
IntActiP24623. 1 interaction.
MINTiMINT-8303018.

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

GeneTreeiENSGT00760000119238.
HOVERGENiHBG054766.
InParanoidiP24623.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG7WHHBK.
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.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527: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]

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471V → M in AAA40645. (PubMed:1429679)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei64 – 8623Missing in isoform 2. 4 PublicationsVSP_011917Add
BLAST

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 .
PIRi A02892. CYRTA.
A02899. CYRTAM.
S07530.
RefSeqi NP_001276666.1. NM_001289737.1. [P24623-1 ]
NP_036666.2. NM_012534.4. [P24623-2 ]
UniGenei Rn.127769.

3D structure databases

ProteinModelPortali P24623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246457. 1 interaction.
IntActi P24623. 1 interaction.
MINTi MINT-8303018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000071248 ; ENSRNOP00000067332 ; ENSRNOG00000047175 . [P24623-2 ]
ENSRNOT00000075545 ; ENSRNOP00000065714 ; ENSRNOG00000047175 . [P24623-1 ]
GeneIDi 24273.
KEGGi rno:24273.

Organism-specific databases

CTDi 1409.
RGDi 2413. Cryaa.

Phylogenomic databases

GeneTreei ENSGT00760000119238.
HOVERGENi HBG054766.
InParanoidi P24623.
KOi K09541.
OMAi GPKVQSG.
OrthoDBi EOG7WHHBK.
PhylomeDBi P24623.

Miscellaneous databases

NextBioi 602845.
PROi P24623.

Gene expression databases

ExpressionAtlasi P24623. baseline.
Genevestigatori P24623.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
PANTHERi PTHR11527:SF36. PTHR11527:SF36. 1 hit.
Pfami PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The alternative splicing product alpha Ains-crystallin is structurally equivalent to alpha A and alpha B subunits in the rat alpha-crystallin aggregate."
    Hendriks W., Weetink H., Voorter C.E.M., Sander J., Bloemendal H., de Jong W.W.
    Biochim. Biophys. Acta 1037:58-65(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORMS 1 AND 2).
  2. "Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin inhibits bacterial growth."
    Bhat S.P., Nandy P., Srinivasan A., Cheng D., Sitay A.
    Protein Eng. 9:713-718(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: Sprague-Dawley.
    Tissue: Lens.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-196 (ISOFORM 2).
  4. "Alpha A-crystallin is expressed in non-ocular tissues."
    Srinivasan A.N., Nagineni C.N., Bhat S.P.
    J. Biol. Chem. 267:23337-23341(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 113-195 (ISOFORM 2), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Eye and Spleen.
  5. "Rat alpha-crystallin A chain with an insertion of 22 residues."
    Cohen L.H., Westerhuis L.W., de Jong W.W., Bloemendal H.
    Eur. J. Biochem. 89:259-266(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT MET-1.
  6. "Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses."
    Thampi P., Hassan A., Smith J.B., Abraham E.C.
    Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.
  7. "Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens."
    Ueda Y., Fukiage C., Shih M., Shearer T.R., David L.L.
    Mol. Cell. Proteomics 1:357-365(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.

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: October 29, 2014
This is version 110 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

External Data

Dasty 3