CRB12_LITCT
ID CRB12_LITCT Reviewed; 198 AA.
AC Q91314;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Beta-crystallin A1-2;
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=8619837; DOI=10.1006/bbrc.1996.0577;
RA Lu S.-F., Pan F.-M., Chiou S.-H.;
RT "Sequence analysis of four acidic beta-crystallin subunits of amphibian
RT lenses: phylogenetic comparison between beta- and gamma-crystallins.";
RL Biochem. Biophys. Res. Commun. 221:219-228(1996).
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}.
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; X87760; CAA61034.1; -; mRNA.
DR PIR; JC4705; S55512.
DR AlphaFoldDB; Q91314; -.
DR SMR; Q91314; -.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
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 Eye lens protein; Repeat.
FT CHAIN 1..198
FT /note="Beta-crystallin A1-2"
FT /id="PRO_0000057536"
FT DOMAIN 14..53
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 54..100
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..197
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..13
FT /note="N-terminal arm"
FT REGION 101..106
FT /note="Connecting peptide"
SQ SEQUENCE 198 AA; 23096 MW; 52A09C6422C0C775 CRC64;
MAQINPLPVP LGPWKITVYD QENFQGKRME FTSSCANIME CGFDNIRSLK VECGAWIGYE
HTSFCGQQFV LERGEYPRWD AWSGSNAYHI ERLMSFRPIC SANHIESKLV IFEKENFVGP
QWELCDDYPS LQAMGWGNNE VGSMKVQCGA WVCYQYPGYR GYQYILESDH HGGEYKHWRE
WGSHAQTFQI QSIRRIQQ