ID   CRBA1_RANTE             Reviewed;         198 AA.
AC   P07317;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Beta-crystallin A1;
OS   Rana temporaria (European common frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=8407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens;
RX   PubMed=3499937; DOI=10.1016/0167-4838(87)90104-x;
RA   Luchin S.V., Zinovieva R.D., Tomarev S.I., Dolgilevich S.M.,
RA   Gause G.G. Jr., Bax J.B., Driessen H.P.C., Blundell T.L.;
RT   "Frog lens beta A1-crystallin: the nucleotide sequence of the cloned cDNA
RT   and computer graphics modelling of the three-dimensional structure.";
RL   Biochim. Biophys. Acta 916:163-171(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luchin S.V., Tomarev S.I., Dolgilevich S.M., Kraev A.S., Sryabin K.G.,
RA   Gause G.G. Jr.;
RT   "Isolation and structure of a clone of recombinant cDNA encoding beta-
RT   crystallin of the eye lens of the frog Rana temporaria.";
RL   Dokl. Biochem. 279:357-361(1985).
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}.
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; X02767; CAA26544.1; -; mRNA.
DR   EMBL; X06421; CAA29730.1; -; mRNA.
DR   PIR; S01608; S01608.
DR   AlphaFoldDB; P07317; -.
DR   SMR; P07317; -.
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"
FT                   /id="PRO_0000057537"
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"
FT   VARIANT         144
FT                   /note="M -> R"
SQ   SEQUENCE   198 AA;  23246 MW;  CA049CDA7D6AB999 CRC64;
     MAQINPLPVP LGPWKITVYD QENFQGKRME FTSSCANIME CGFDNIRSLK VECGGWIGYE
     HTSFCGQQFV LERGEYPRWD AWSGSNAYHI ERLMSFRPIC SANHKESKLV IFEKENFIGR
     QWEMCDDYPS LQAMGWVNNE VGSMKVQCGS WVCYQYPGYR GYQYILESDH HGGEYKHWRE
     WGSHAQTFQI QSIRRIQQ