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Protein

Beta-crystallin B1

Gene

Crybb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • structural constituent of eye lens Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B1
Alternative name(s):
Beta-B1 crystallin
Cleaved into the following chain:
Gene namesi
Name:Crybb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi2416. Crybb1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 250249Beta-crystallin B1PRO_0000006339Add
BLAST
Chaini12 – 250239Beta-crystallin B1BPRO_0000006340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei228 – 2281Omega-N-methylated arginineBy similarity
Modified residuei229 – 2291Omega-N-methylated arginineBy similarity

Post-translational modificationi

Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II.

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

PaxDbiP02523.

PTM databases

PhosphoSiteiP02523.

Expressioni

Gene expression databases

ExpressionAtlasiP02523. baseline.
GenevisibleiP02523. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064741.

Structurei

3D structure databases

ProteinModelPortaliP02523.
SMRiP02523. Positions 53-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 9640Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 14145Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18842Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini189 – 23143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5655N-terminal armAdd
BLAST
Regioni142 – 1465Connecting peptide
Regioni233 – 25018C-terminal armAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the beta/gamma-crystallin family.Curated
Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiP02523.
OMAiMSFRPIK.
PhylomeDBiP02523.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 1 hit.
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVAKAAAT TAVNPGPDGK GKGTPSTGTA PAPGPTPVPA SVPRPAAKVG
60 70 80 90 100
ELPPGSYRLV VFEQENFQGR RVEFSGECLN LGDRGFDRVR SLIVLSGPWV
110 120 130 140 150
AFEQSAFRGE MFVLEKGEYP RWDTWTSSYR SDRLMSFRPI RMDSQEHKIC
160 170 180 190 200
LFEGANFKGN TMEIQEDDVP SLWVYGFCDR VGSITVSSGT WVGYQYPGYR
210 220 230 240 250
GYQYLLEPGD FRHWNEWGAF QPQMQAVRRL RDRQWHQEGC FPVLTAEPPK
Length:250
Mass (Da):28,093
Last modified:January 23, 2007 - v4
Checksum:i81B7F7D1D92A8AD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 182PD → Y in CAA29679 (PubMed:3879970).Curated
Sequence conflicti17 – 182PD → Y in AAA40979 (PubMed:3458246).Curated

Mass spectrometryi

Molecular mass is 28002.0 Da from positions 2 - 250. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06377 Genomic DNA. Translation: CAA29679.1.
X05900 mRNA. Translation: CAA29329.1.
M13534
, M13527, M13528, M13530, M13532 Genomic DNA. Translation: AAA40979.1.
BC126096 mRNA. Translation: AAI26097.1.
AF286652 mRNA. Translation: AAF97950.1.
PIRiA02925. CYRTB1.
RefSeqiNP_037068.2. NM_012936.2.
UniGeneiRn.10602.

Genome annotation databases

EnsembliENSRNOT00000073072; ENSRNOP00000064741; ENSRNOG00000047653.
GeneIDi25421.
KEGGirno:25421.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06377 Genomic DNA. Translation: CAA29679.1.
X05900 mRNA. Translation: CAA29329.1.
M13534
, M13527, M13528, M13530, M13532 Genomic DNA. Translation: AAA40979.1.
BC126096 mRNA. Translation: AAI26097.1.
AF286652 mRNA. Translation: AAF97950.1.
PIRiA02925. CYRTB1.
RefSeqiNP_037068.2. NM_012936.2.
UniGeneiRn.10602.

3D structure databases

ProteinModelPortaliP02523.
SMRiP02523. Positions 53-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000064741.

PTM databases

PhosphoSiteiP02523.

Proteomic databases

PaxDbiP02523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000073072; ENSRNOP00000064741; ENSRNOG00000047653.
GeneIDi25421.
KEGGirno:25421.

Organism-specific databases

CTDi1414.
RGDi2416. Crybb1.

Phylogenomic databases

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOVERGENiHBG003364.
InParanoidiP02523.
OMAiMSFRPIK.
PhylomeDBiP02523.

Miscellaneous databases

PROiP02523.

Gene expression databases

ExpressionAtlasiP02523. baseline.
GenevisibleiP02523. RN.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 1 hit.
PfamiPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSiPR01367. BGCRYSTALLIN.
SMARTiSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMiSSF49695. SSF49695. 1 hit.
PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat lens beta-crystallins are internally duplicated and homologous to gamma-crystallins."
    den Dunnen J.T., Moormann R.J.M., Schoenmakers J.G.G.
    Biochim. Biophys. Acta 824:295-303(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, NUCLEOTIDE SEQUENCE [MRNA] OF 51-250.
  2. "Intron insertions and deletions in the beta/gamma-crystallin gene family: the rat beta B1 gene."
    den Dunnen J.T., Moormann R.J.M., Lubsen N.H., Schoenmakers J.G.G.
    Proc. Natl. Acad. Sci. U.S.A. 83:2855-2859(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
    Tissue: Brain.
  4. "Lens proteomics: analysis of rat crystallin sequences and two-dimensional electrophoresis map."
    Lampi K.J., Shih M., Ueda Y., Shearer T.R., David L.L.
    Invest. Ophthalmol. Vis. Sci. 43:216-224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-250, PROTEIN SEQUENCE OF 2-250, ACETYLATION AT SER-2, MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Lens.
  5. "Beta-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to beta-crystallins insolubilized during cataract."
    David L.L., Shearer T.R.
    FEBS Lett. 324:265-270(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 51-56.

Entry informationi

Entry nameiCRBB1_RAT
AccessioniPrimary (citable) accession number: P02523
Secondary accession number(s): A0JN26, Q9JHV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.