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P05813 (CRBA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Crystallins are the dominant structural components of the vertebrate eye lens.

Subunit structure

Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms By similarity.

Domain

Has a two-domain beta-structure, folded into four very similar Greek key motifs.

Post-translational modification

Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.

S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.

Isoform A1 initiator methionine is removed. The new N-terminal amino acid is then N-acetylated.

Involvement in disease

Cataract 10, multiple types (CTRCT10) [MIM:600881]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.5

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Contains 4 beta/gamma crystallin 'Greek key' domains.

Mass spectrometry

Molecular mass is 25192±3 Da from positions 1 - 215. Determined by ESI. Ref.3

Molecular mass is 25192 Da from positions 1 - 215. Determined by ESI. Ref.6

Molecular mass is 23101±3 Da from positions 19 - 215. Determined by ESI. Ref.3

Molecular mass is 23102 Da from positions 19 - 215. Determined by ESI. Ref.6

Molecular mass is 22646 Da from positions 23 - 215. Determined by ESI. Ref.6

Molecular mass is 22351 Da from positions 26 - 215. Determined by ESI. Ref.6

Molecular mass is 22294 Da from positions 27 - 215. Determined by ESI. Ref.6

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRYABP025112EBI-7043337,EBI-739060

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform A3 (identifier: P05813-1)

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.
Isoform A1 (identifier: P05813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Beta-crystallin A3
PRO_0000006331
Chain23 – 215193Beta-crystallin A3, isoform A1, Delta4 form
PRO_0000226692
Chain26 – 215190Beta-crystallin A3, isoform A1, Delta7 form
PRO_0000226693
Chain27 – 215189Beta-crystallin A3, isoform A1, Delta8 form
PRO_0000226694

Regions

Domain31 – 7040Beta/gamma crystallin 'Greek key' 1
Domain71 – 11747Beta/gamma crystallin 'Greek key' 2
Domain124 – 16542Beta/gamma crystallin 'Greek key' 3
Domain166 – 21449Beta/gamma crystallin 'Greek key' 4
Region1 – 3030N-terminal arm
Region118 – 1236Connecting peptide

Sites

Site1261Susceptible to oxidation

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue821S-glutathionyl cysteine; alternate
Modified residue821S-methylcysteine; alternate
Modified residue1171S-glutathionyl cysteine; alternate
Modified residue1171S-methylcysteine; alternate Ref.6

Natural variations

Alternative sequence1 – 1717Missing in isoform A1.
VSP_018710

Experimental info

Sequence conflict1071I → M in AAA52107. Ref.1
Sequence conflict1161I → F in AAA52107. Ref.1
Sequence conflict172 – 1743QYP → HYL in AAA52107. Ref.1
Sequence conflict1841E → K in AAA52107. Ref.1
Sequence conflict1891G → E in AAA52107. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform A3 [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: C544564835688A19

FASTA21525,150
        10         20         30         40         50         60 
METQAEQQEL ETLPTTKMAQ TNPTPGSLGP WKITIYDQEN FQGKRMEFTS SCPNVSERSF 

        70         80         90        100        110        120 
DNVRSLKVES GAWIGYEHTS FCGQQFILER GEYPRWDAWS GSNAYHIERL MSFRPICSAN 

       130        140        150        160        170        180 
HKESKMTIFE KENFIGRQWE ISDDYPSLQA MGWFNNEVGS MKIQSGAWVC YQYPGYRGYQ 

       190        200        210 
YILECDHHGG DYKHWREWGS HAQTSQIQSI RRIQQ 

« Hide

Isoform A1 [UniParc].

Checksum: 95954586F78B1B4C
Show »

FASTA19823,191

References

« Hide 'large scale' references
[1]"Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily."
Hogg D., Tsui L.-C., Gorin M., Breitman M.L.
J. Biol. Chem. 261:12420-12427(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-215, PROTEIN SEQUENCE OF 23-30 AND 197-211, MASS SPECTROMETRY.
[4]"Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene."
Kannabiran C., Rogan P.K., Olmos L., Basti S., Rao G.N., Kaiser-Kupfer M., Hejtmancik J.F.
Mol. Vis. 4:21-21(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CTRCT10.
[5]"Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract."
Reddy M.A., Bateman O.A., Chakarova C., Ferris J., Berry V., Lomas E., Sarra R., Smith M.A., Moore A.T., Bhattacharya S.S., Slingsby C.
Hum. Mol. Genet. 13:945-953(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CTRCT10.
[6]"Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation."
Lapko V.N., Cerny R.L., Smith D.L., Smith J.B.
Protein Sci. 14:45-54(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS, METHYLATION AT CYS-117, GLUTATHIONYLATION, MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Eye disease Crystallin, beta-A1 (CRYBA1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14306 expand/collapse EMBL AC list , M14301, M14302, M14303, M14304, M14305 Genomic DNA. Translation: AAA52107.1.
BC069537 mRNA. Translation: AAH69537.1.
BC113693 mRNA. Translation: AAI13694.1.
U59058 mRNA. Translation: AAC50971.1.
PIRCYHUB3. A25202.
RefSeqNP_005199.2. NM_005208.4.
UniGeneHs.46275.

3D structure databases

ProteinModelPortalP05813.
SMRP05813. Positions 27-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107801. 3 interactions.
IntActP05813. 4 interactions.
MINTMINT-3388142.
STRING9606.ENSP00000225387.

PTM databases

PhosphoSiteP05813.

Polymorphism databases

DMDM2506317.

Proteomic databases

PaxDbP05813.
PRIDEP05813.

Protocols and materials databases

DNASU1411.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225387; ENSP00000225387; ENSG00000108255. [P05813-1]
GeneID1411.
KEGGhsa:1411.
UCSCuc002hdw.3. human. [P05813-1]

Organism-specific databases

CTD1411.
GeneCardsGC17P027573.
HGNCHGNC:2394. CRYBA1.
MIM123610. gene.
600881. phenotype.
neXtProtNX_P05813.
Orphanet98985. Cataract with Y-shaped suture opacities.
98995. Zonular cataract.
PharmGKBPA26908.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47808.
HOGENOMHOG000234388.
HOVERGENHBG003364.
InParanoidP05813.
OMAWEISDDY.
OrthoDBEOG7K9K40.
PhylomeDBP05813.
TreeFamTF331401.

Gene expression databases

BgeeP05813.
CleanExHS_CRYBA1.
GenevestigatorP05813.

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. SSF49695. 1 hit.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCrystallin,_beta_A1.
GenomeRNAi1411.
NextBio5769.
PROP05813.
SOURCESearch...

Entry information

Entry nameCRBA1_HUMAN
AccessionPrimary (citable) accession number: P05813
Secondary accession number(s): Q13633, Q14CM9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM