CRBB3_BOVIN
ID CRBB3_BOVIN Reviewed; 211 AA.
AC P19141; O18790;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shih M., Lampi K.J., Shearer T.R., David L.L.;
RT "Confirmation of bovine beta-B3 crystallin sequence.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-211.
RC TISSUE=Lens cortex;
RX PubMed=6698025; DOI=10.1111/j.1432-1033.1984.tb08029.x;
RA Berbers G.A.M., Hoekman W.A., Bloemendal H., de Jong W.W., Kleinschmidt T.,
RA Braunitzer G.;
RT "Homology between the primary structures of the major bovine beta-
RT crystallin chains.";
RL Eur. J. Biochem. 139:467-479(1984).
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; AF013259; AAB67120.1; -; mRNA.
DR PIR; B27898; B27898.
DR RefSeq; NP_776952.1; NM_174527.3.
DR RefSeq; XP_005218081.1; XM_005218024.3.
DR AlphaFoldDB; P19141; -.
DR SMR; P19141; -.
DR IntAct; P19141; 1.
DR MINT; P19141; -.
DR STRING; 9913.ENSBTAP00000001656; -.
DR PaxDb; P19141; -.
DR Ensembl; ENSBTAT00000001656; ENSBTAP00000001656; ENSBTAG00000001255.
DR GeneID; 282206; -.
DR KEGG; bta:282206; -.
DR CTD; 1417; -.
DR VEuPathDB; HostDB:ENSBTAG00000001255; -.
DR VGNC; VGNC:27738; CRYBB3.
DR eggNOG; ENOG502QTNZ; Eukaryota.
DR GeneTree; ENSGT00940000158425; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P19141; -.
DR OMA; NEWNASQ; -.
DR OrthoDB; 1237607at2759; -.
DR TreeFam; TF331401; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000001255; Expressed in anterior segment of eyeball and 19 other tissues.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Eye lens protein;
KW Reference proteome; Repeat.
FT CHAIN 1..211
FT /note="Beta-crystallin B3"
FT /id="PRO_0000423200"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:6698025"
FT CHAIN 2..211
FT /note="Beta-crystallin B3, N-terminally processed"
FT /id="PRO_0000057559"
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, ECO:0000305"
FT CONFLICT 22
FT /note="G -> GG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="VI -> IV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="C -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="R -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="SN -> NG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..102
FT /note="SDSLL -> QDNLS (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="LH -> IK (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> GH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="H -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 121..125
FT /note="NPAFG -> HPNFA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..183
FT /note="NE -> DD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="N -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="L -> LG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24328 MW; 8D388B3F1785286A CRC64;
MAEQHSTPEQ AAAGKSHGGL GGSYKVIVYE MENFQGKRCE LTAECPNLTE SLLEKVGSIQ
VESGPWLAFE RRAFRGEQYV LEKGDYPRWD AWSNSHHSDS LLSLRPLHID GPDHKLHLFE
NPAFGGRKME IVDDDVPSLW AHGFQDRVAS VRAINGTWVG YEFPGYRGRQ YVFERGEYRH
WNEWDANQPQ LQSVRRIRDQ KWHKRGVFLS S
