ID   CRBB2_LITCT             Reviewed;         205 AA.
AC   Q91318;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Beta-crystallin B2;
DE   AltName: Full=Beta-B2 crystallin;
DE   AltName: Full=Beta-crystallin Bp;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=8554619; DOI=10.1006/bbrc.1995.2861;
RA   Pan F.-M., Chang W.-C., Lu S.-F., Hsu A.-L., Chiou S.-H.;
RT   "Sequence analysis of one major basic beta-crystallin (beta Bp) of
RT   amphibian lenses: evolutionary comparison and phylogenetic relatedness
RT   between beta- and gamma-crystallins.";
RL   Biochem. Biophys. Res. Commun. 217:940-949(1995).
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   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; X91989; CAA63044.1; -; mRNA.
DR   PIR; JC4528; JC4528.
DR   AlphaFoldDB; Q91318; -.
DR   SMR; Q91318; -.
DR   GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   InterPro; IPR001064; Beta/gamma_crystallin.
DR   InterPro; IPR033058; CRYBB2.
DR   InterPro; IPR011024; G_crystallin-like.
DR   PANTHER; PTHR11818:SF11; PTHR11818:SF11; 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; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02522"
FT   CHAIN           2..205
FT                   /note="Beta-crystallin B2"
FT                   /id="PRO_0000057558"
FT   DOMAIN          17..56
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          57..101
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          107..148
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          149..191
FT                   /note="Beta/gamma crystallin 'Greek key' 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   REGION          2..16
FT                   /note="N-terminal arm"
FT   REGION          102..106
FT                   /note="Connecting peptide"
FT   REGION          193..205
FT                   /note="C-terminal arm"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P02522"
SQ   SEQUENCE   205 AA;  23649 MW;  49B6DFC7B5B2C959 CRC64;
     MASDHQSPAT KQQQPSSKIV LFEQENFQGR CHELSGPCTS LKEAGMEKIG SILVHSGPWV
     GYEQQNCKGE QFVFEKGEYP RWDSWTNSRK SESISSLRPI KVDSQEHKIV LYENPNFTGK
     KIEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GYQYLFEKGD YKDSSDFGAQ
     HPQIQSVRRI RDMQWHQRGT FHPTN