ID   CRBA4_RAT               Reviewed;         196 AA.
AC   P56374;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Beta-crystallin A4;
DE   AltName: Full=Beta-A4 crystallin;
GN   Name=Cryba4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-196, ACETYLATION AT
RP   THR-2, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Lens;
RX   PubMed=11773034;
RA   Lampi K.J., Shih M., Ueda Y., Shearer T.R., David L.L.;
RT   "Lens proteomics: analysis of rat crystallin sequences and two-dimensional
RT   electrophoresis map.";
RL   Invest. Ophthalmol. Vis. Sci. 43:216-224(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 5-10.
RX   PubMed=8405363; DOI=10.1016/0014-5793(93)80131-d;
RA   David L.L., Shearer T.R.;
RT   "Beta-crystallins insolubilized by calpain II in vitro contain cleavage
RT   sites similar to beta-crystallins insolubilized during cataract.";
RL   FEBS Lett. 324:265-270(1993).
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   -!- MASS SPECTROMETRY: Mass=23922.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11773034};
CC   -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR   EMBL; AF013247; AAB67117.1; -; mRNA.
DR   RefSeq; NP_113877.1; NM_031689.1.
DR   RefSeq; XP_017453936.1; XM_017598447.1.
DR   AlphaFoldDB; P56374; -.
DR   SMR; P56374; -.
DR   STRING; 10116.ENSRNOP00000066572; -.
DR   iPTMnet; P56374; -.
DR   PhosphoSitePlus; P56374; -.
DR   PaxDb; P56374; -.
DR   Ensembl; ENSRNOT00000073763; ENSRNOP00000066572; ENSRNOG00000049770.
DR   GeneID; 64348; -.
DR   KEGG; rno:64348; -.
DR   CTD; 1413; -.
DR   RGD; 61962; Cryba4.
DR   eggNOG; ENOG502QTF8; Eukaryota.
DR   GeneTree; ENSGT00940000160372; -.
DR   HOGENOM; CLU_081883_0_0_1; -.
DR   InParanoid; P56374; -.
DR   OMA; GEYPSWE; -.
DR   OrthoDB; 1142622at2759; -.
DR   PhylomeDB; P56374; -.
DR   PRO; PR:P56374; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000049770; Expressed in ovary and 14 other tissues.
DR   Genevisible; P56374; RN.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005212; F:structural constituent of eye lens; IDA:RGD.
DR   GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; ISO:RGD.
DR   InterPro; IPR001064; Beta/gamma_crystallin.
DR   InterPro; IPR033342; CRYBA4.
DR   InterPro; IPR011024; G_crystallin-like.
DR   PANTHER; PTHR11818:SF19; PTHR11818:SF19; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11773034"
FT   CHAIN           2..196
FT                   /note="Beta-crystallin A4"
FT                   /id="PRO_0000057547"
FT   DOMAIN          12..51
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          52..98
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          105..146
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          147..195
FT                   /note="Beta/gamma crystallin 'Greek key' 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   REGION          2..11
FT                   /note="N-terminal arm"
FT   REGION          99..104
FT                   /note="Connecting peptide"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:11773034"
SQ   SEQUENCE   196 AA;  22382 MW;  58527F2E0F5E1D20 CRC64;
     MTLQCTKSAG HWRVVVWDEE GFQGRRHEFT AECPSVLDLG FETVRSLKVL SGAWVGFEHA
     GFQGQQYVLE RGDYPGWDAW GGNTAYPAER LTSFRPVACA NHRDSRLTIF EQENFLGRKG
     ELSDDYPSLQ AMGWDGTEVG SFHVQSGAWV CSQFPGYRGF QYVLESDHHS GDYKHFREWG
     SHAHTFQVQS VRRIQQ