CRBB3_MOUSE
ID CRBB3_MOUSE Reviewed; 211 AA.
AC Q9JJU9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-crystallin B3;
DE AltName: Full=Beta-B3 crystallin;
DE Contains:
DE RecName: Full=Beta-crystallin B3, N-terminally processed;
GN Name=Crybb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Graw J.;
RT "Sequence analysis of beta-A2-, beta-A4- and beta-B3-crystallin cDNA
RT completes the identification of the members of this gene family in the
RT mouse.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; AJ272229; CAB75587.1; -; mRNA.
DR EMBL; BC031442; AAH31442.1; -; mRNA.
DR EMBL; BC058522; AAH58522.1; -; mRNA.
DR CCDS; CCDS19547.1; -.
DR RefSeq; NP_001153122.1; NM_001159650.1.
DR RefSeq; NP_067327.1; NM_021352.3.
DR RefSeq; XP_006534825.1; XM_006534762.2.
DR AlphaFoldDB; Q9JJU9; -.
DR SMR; Q9JJU9; -.
DR STRING; 10090.ENSMUSP00000113572; -.
DR iPTMnet; Q9JJU9; -.
DR PhosphoSitePlus; Q9JJU9; -.
DR MaxQB; Q9JJU9; -.
DR PaxDb; Q9JJU9; -.
DR PRIDE; Q9JJU9; -.
DR ProteomicsDB; 284118; -.
DR Antibodypedia; 24112; 124 antibodies from 21 providers.
DR DNASU; 12962; -.
DR Ensembl; ENSMUST00000076069; ENSMUSP00000075440; ENSMUSG00000029352.
DR Ensembl; ENSMUST00000117143; ENSMUSP00000113347; ENSMUSG00000029352.
DR Ensembl; ENSMUST00000118226; ENSMUSP00000112618; ENSMUSG00000029352.
DR Ensembl; ENSMUST00000119627; ENSMUSP00000113572; ENSMUSG00000029352.
DR Ensembl; ENSMUST00000120506; ENSMUSP00000112718; ENSMUSG00000029352.
DR GeneID; 12962; -.
DR KEGG; mmu:12962; -.
DR UCSC; uc012ebl.1; mouse.
DR CTD; 1417; -.
DR MGI; MGI:102717; Crybb3.
DR VEuPathDB; HostDB:ENSMUSG00000029352; -.
DR eggNOG; ENOG502QTNZ; Eukaryota.
DR GeneTree; ENSGT00940000158425; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; Q9JJU9; -.
DR OMA; NEWNASQ; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; Q9JJU9; -.
DR TreeFam; TF331401; -.
DR BioGRID-ORCS; 12962; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Crybb3; mouse.
DR PRO; PR:Q9JJU9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JJU9; protein.
DR Bgee; ENSMUSG00000029352; Expressed in lens of camera-type eye and 66 other tissues.
DR ExpressionAtlas; Q9JJU9; baseline and differential.
DR Genevisible; Q9JJU9; MM.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:MGI.
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; IPR033115; CRYBB3.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF13; PTHR11818:SF13; 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 2: Evidence at transcript level;
KW Acetylation; Eye lens protein; Reference proteome; Repeat.
FT CHAIN 1..211
FT /note="Beta-crystallin B3"
FT /id="PRO_0000421775"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02524"
FT CHAIN 2..211
FT /note="Beta-crystallin B3, N-terminally processed"
FT /id="PRO_0000057561"
FT DOMAIN 24..63
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 64..108
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 114..155
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 156..198
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..23
FT /note="N-terminal arm"
FT REGION 109..113
FT /note="Connecting peptide"
FT REGION 200..211
FT /note="C-terminal arm"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P26998"
FT MOD_RES 2
FT /note="N-acetylalanine; in Beta-crystallin B3, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P02524"
SQ SEQUENCE 211 AA; 24291 MW; 2F23F47987102196 CRC64;
MAEQHGAPEQ AAAGKSHGGL GGSYKVTVYE LENFQGKRCE LSAECPNLTD SLLEKVGSIQ
VESGPWLAFE RRAFRGEQFV LEKGDYPRWD AWSSSRRSDI LLSLRPLHID GPDHKLHLFE
NPAFSGRKME IVDDDVPSLW AHGFQDRVAS IRVINGTWVG YEFPGYRGRQ YVFERGEFRH
WNEWDANQPQ LQSVRRIRDQ KWHKRGCFLS S
