CRBA1_BOVIN
ID CRBA1_BOVIN Reviewed; 215 AA.
AC P11843; P79425; Q6DTZ7; Q95113;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Beta-crystallin A3;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta4 form;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta7 form;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta8 form;
GN Name=CRYBA1;
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].
RX PubMed=6547897; DOI=10.3109/02713688409167211;
RA Gorin M.B., Horwitz J.;
RT "Cloning and characterization of a cow beta crystallin cDNA.";
RL Curr. Eye Res. 3:939-948(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA David L.L., Lampi K.J., Shih M., Shearer T.R., Sheil M.M., Stutchbury G.,
RA Truscott R.J.W.;
RT "Lens proteomics: identification of the major proteins in the bovine lens
RT and sequence analysis of beta A3, beta B3, and beta A4-crystallins.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-45 AND 111-245.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-131.
RX PubMed=6527379; DOI=10.1016/0022-2836(84)90022-6;
RA Quax-Jeuken Y., Janssen C., Quax W.J., van den Heuvel R., Bloemendal H.;
RT "Bovine beta-crystallin complementary DNA clones. Alternating
RT proline/alanine sequence of beta B1 subunit originates from a repetitive
RT DNA sequence.";
RL J. Mol. Biol. 180:457-472(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=A3;
CC IsoId=P11843-1; Sequence=Displayed;
CC Name=A1;
CC IsoId=P11843-2; Sequence=VSP_018709;
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- PTM: Specific cleavages in the N-terminal arm occur during lens
CC maturation and give rise to several truncated forms. {ECO:0000250}.
CC -!- PTM: Isoform A1 contains a N-acetylalanine at position 2.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; M33010; AAA30401.1; -; mRNA.
DR EMBL; AY645778; AAT72793.1; -; mRNA.
DR EMBL; M11850; AAA30473.1; -; mRNA.
DR EMBL; M11850; AAA30474.1; -; mRNA.
DR PIR; C27898; C27898.
DR PIR; I45857; I45857.
DR RefSeq; NP_776948.1; NM_174523.3.
DR AlphaFoldDB; P11843; -.
DR SMR; P11843; -.
DR STRING; 9913.ENSBTAP00000007037; -.
DR PaxDb; P11843; -.
DR GeneID; 282202; -.
DR KEGG; bta:282202; -.
DR CTD; 1411; -.
DR eggNOG; ENOG502QSM0; Eukaryota.
DR InParanoid; P11843; -.
DR OrthoDB; 1142622at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Direct protein sequencing;
KW Eye lens protein; Glutathionylation; Methylation; Reference proteome;
KW Repeat.
FT CHAIN 1..215
FT /note="Beta-crystallin A3"
FT /id="PRO_0000006329"
FT CHAIN 23..215
FT /note="Beta-crystallin A3, isoform A1, Delta4 form"
FT /id="PRO_0000226689"
FT CHAIN 26..215
FT /note="Beta-crystallin A3, isoform A1, Delta7 form"
FT /id="PRO_0000226690"
FT CHAIN 27..215
FT /note="Beta-crystallin A3, isoform A1, Delta8 form"
FT /id="PRO_0000226691"
FT DOMAIN 31..70
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 71..117
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 124..165
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 166..214
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..30
FT /note="N-terminal arm"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..123
FT /note="Connecting peptide"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P05813"
FT MOD_RES 82
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform A1)"
FT /evidence="ECO:0000305"
FT /id="VSP_018709"
FT CONFLICT 11
FT /note="E -> K (in Ref. 1; AAA30401)"
FT /evidence="ECO:0000305"
FT INIT_MET P11843-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P11843-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 215 AA; 25131 MW; 430785A7F1648ADC CRC64;
METQTVQQEL ESLPTTKMAQ TNPMPGSVGP WKITIYDQEN FQGKRMEFTS SCPNVSERNF
DNVRSLKVEC GAWVGYEHTS FCGQQFVLER GEYPRWDAWS GSNAYHIERL MSFRPICSAN
HKESKITIFE KENFIGRQWE ICDDYPSLQA MGWPNNEVGS MKIQCGAWVC YQYPGYRGYQ
YILECDHHGG DYKHWREWGS HAQTSQIQSI RRIQQ
