CRBB1_BOVIN
ID CRBB1_BOVIN Reviewed; 253 AA.
AC P07318;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Beta-crystallin B1;
DE AltName: Full=Beta-B1 crystallin;
GN Name=CRYBB1;
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=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).
RN [2]
RP PROTEIN SEQUENCE OF 2-253.
RC TISSUE=Lens cortex;
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).
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.
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 truncated forms, leading to impaired
CC oligomerization and protein insolubilization.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; X01808; CAA25951.1; -; mRNA.
DR PIR; S07264; S07264.
DR RefSeq; NP_776951.1; NM_174526.2.
DR AlphaFoldDB; P07318; -.
DR SMR; P07318; -.
DR BioGRID; 159479; 1.
DR STRING; 9913.ENSBTAP00000025671; -.
DR PaxDb; P07318; -.
DR PRIDE; P07318; -.
DR Ensembl; ENSBTAT00000025671; ENSBTAP00000025671; ENSBTAG00000019280.
DR GeneID; 282205; -.
DR KEGG; bta:282205; -.
DR CTD; 1414; -.
DR VEuPathDB; HostDB:ENSBTAG00000019280; -.
DR VGNC; VGNC:27736; CRYBB1.
DR eggNOG; ENOG502QTJT; Eukaryota.
DR GeneTree; ENSGT00940000160516; -.
DR InParanoid; P07318; -.
DR OrthoDB; 1237607at2759; -.
DR TreeFam; TF331401; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000019280; Expressed in anterior segment of eyeball and 100 other tissues.
DR ExpressionAtlas; P07318; baseline and differential.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR033059; CRYBB1.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF12; PTHR11818:SF12; 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; Methylation;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6698025"
FT CHAIN 2..253
FT /note="Beta-crystallin B1"
FT /id="PRO_0000057549"
FT DOMAIN 60..99
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 100..144
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 150..191
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 192..234
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..59
FT /note="N-terminal arm"
FT REGION 145..149
FT /note="Connecting peptide"
FT REGION 236..253
FT /note="C-terminal arm"
FT COMPBIAS 21..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P53674, ECO:0000305"
FT CONFLICT 8..11
FT /note="ASAT -> TSAA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..102
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28144 MW; 47998660FC7E7D20 CRC64;
MSQPAAKASA TAAVNPGPDG KGKAGPPPGP APGSGPAPAP APAPAQPAPA AKAELPPGSY
KLVVFEQENF QGRRVEFSGE CLNLGDRGFE RVRSIIVTSG PWVAFEQSNF RGEMFVLEKG
EYPRWDTWSS SYRSDRLMSF RPIKMDAQEH KLCLFEGANF KGNTMEIQED DVPSLWVYGF
CDRVGSVRVS SGTWVGYQYP GYRGYQYLLE PGDFRHWNEW GAFQPQMQAV RRLRDRQWHR
EGCFPVLAAE PPK
