CRBB1_RAT
ID CRBB1_RAT Reviewed; 250 AA.
AC P02523; A0JN26; Q9JHV9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-crystallin B1;
DE AltName: Full=Beta-B1 crystallin;
DE Contains:
DE RecName: Full=Beta-crystallin B1B;
GN Name=Crybb1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50, AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 51-250.
RX PubMed=3879970; DOI=10.1016/0167-4781(85)90035-1;
RA den Dunnen J.T., Moormann R.J.M., Schoenmakers J.G.G.;
RT "Rat lens beta-crystallins are internally duplicated and homologous to
RT gamma-crystallins.";
RL Biochim. Biophys. Acta 824:295-303(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3458246; DOI=10.1073/pnas.83.9.2855;
RA den Dunnen J.T., Moormann R.J.M., Lubsen N.H., Schoenmakers J.G.G.;
RT "Intron insertions and deletions in the beta/gamma-crystallin gene family:
RT the rat beta B1 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2855-2859(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-250, PROTEIN SEQUENCE OF 2-250, ACETYLATION
RP AT SER-2, AND MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Lens;
RX PubMed=11773034;
RA Lampi K.J., Shih M., Ueda Y., Shearer T.R., David L.L.;
RT "Lens proteomics: analysis of rat crystallin sequences and two-dimensional
RT electrophoresis map.";
RL Invest. Ophthalmol. Vis. Sci. 43:216-224(2002).
RN [5]
RP PROTEIN SEQUENCE OF 51-56.
RX PubMed=8405363; DOI=10.1016/0014-5793(93)80131-d;
RA David L.L., Shearer T.R.;
RT "Beta-crystallins insolubilized by calpain II in vitro contain cleavage
RT sites similar to beta-crystallins insolubilized during cataract.";
RL FEBS Lett. 324:265-270(1993).
CC -!- FUNCTION: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
CC -!- SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure
CC of beta-crystallin oligomers seems to be stabilized through
CC interactions between the N-terminal arms.
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- PTM: Specific cleavages in the N-terminal arm occur during lens
CC maturation and give rise to truncated forms, leading to impaired
CC oligomerization and protein insolubilization. The protease responsible
CC for this partial degradation could be calpain II.
CC -!- MASS SPECTROMETRY: [Beta-crystallin B1]: Mass=28002.0;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11773034};
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06377; CAA29679.1; -; Genomic_DNA.
DR EMBL; X05900; CAA29329.1; -; mRNA.
DR EMBL; M13534; AAA40979.1; -; Genomic_DNA.
DR EMBL; M13527; AAA40979.1; JOINED; Genomic_DNA.
DR EMBL; M13528; AAA40979.1; JOINED; Genomic_DNA.
DR EMBL; M13530; AAA40979.1; JOINED; Genomic_DNA.
DR EMBL; M13532; AAA40979.1; JOINED; Genomic_DNA.
DR EMBL; BC126096; AAI26097.1; -; mRNA.
DR EMBL; AF286652; AAF97950.1; -; mRNA.
DR PIR; A02925; CYRTB1.
DR RefSeq; NP_037068.2; NM_012936.2.
DR AlphaFoldDB; P02523; -.
DR SMR; P02523; -.
DR STRING; 10116.ENSRNOP00000064741; -.
DR iPTMnet; P02523; -.
DR PhosphoSitePlus; P02523; -.
DR PaxDb; P02523; -.
DR Ensembl; ENSRNOT00000073072; ENSRNOP00000064741; ENSRNOG00000047653.
DR GeneID; 25421; -.
DR KEGG; rno:25421; -.
DR CTD; 1414; -.
DR RGD; 2416; Crybb1.
DR eggNOG; ENOG502QTJT; Eukaryota.
DR GeneTree; ENSGT00940000160516; -.
DR InParanoid; P02523; -.
DR OMA; AQEHKIC; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P02523; -.
DR PRO; PR:P02523; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000047653; Expressed in heart and 13 other tissues.
DR ExpressionAtlas; P02523; baseline and differential.
DR Genevisible; P02523; RN.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033059; CRYBB1.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF12; PTHR11818:SF12; 1.
DR Pfam; PF00030; Crystall; 2.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49695; SSF49695; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Eye lens protein; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11773034"
FT CHAIN 2..250
FT /note="Beta-crystallin B1"
FT /id="PRO_0000006339"
FT CHAIN 12..250
FT /note="Beta-crystallin B1B"
FT /id="PRO_0000006340"
FT DOMAIN 57..96
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 97..141
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 147..188
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 189..231
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..56
FT /note="N-terminal arm"
FT REGION 142..146
FT /note="Connecting peptide"
FT REGION 233..250
FT /note="C-terminal arm"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:11773034"
FT CONFLICT 17..18
FT /note="PD -> Y (in Ref. 1; CAA29679 and 2; AAA40979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28093 MW; 81B7F7D1D92A8AD9 CRC64;
MSQVAKAAAT TAVNPGPDGK GKGTPSTGTA PAPGPTPVPA SVPRPAAKVG ELPPGSYRLV
VFEQENFQGR RVEFSGECLN LGDRGFDRVR SLIVLSGPWV AFEQSAFRGE MFVLEKGEYP
RWDTWTSSYR SDRLMSFRPI RMDSQEHKIC LFEGANFKGN TMEIQEDDVP SLWVYGFCDR
VGSITVSSGT WVGYQYPGYR GYQYLLEPGD FRHWNEWGAF QPQMQAVRRL RDRQWHQEGC
FPVLTAEPPK
