CRBB2_BOVIN
ID CRBB2_BOVIN Reviewed; 205 AA.
AC P02522;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Beta-crystallin B2;
DE AltName: Full=Beta-B2 crystallin;
DE AltName: Full=Beta-crystallin Bp;
GN Name=CRYBB2;
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 PROTEIN SEQUENCE OF 2-205, AND ACETYLATION AT ALA-2.
RX PubMed=7035168; DOI=10.1111/j.1432-1033.1981.tb06433.x;
RA Driessen H.P.C., Herbrink P., Bloemendal H., de Jong W.W.;
RT "Primary structure of the bovine beta-crystallin Bp chain. Internal
RT duplication and homology with gamma-crystallin.";
RL Eur. J. Biochem. 121:83-91(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3427982; DOI=10.3109/02713688708997559;
RA Hogg D., Gorin M.B., Heinzmann C., Zollmann S., Mohandas T., Klisak I.,
RA Sparkes R.S., Breitman M., Tsui L.-C., Horwitz J.;
RT "Nucleotide sequence for the cDNA of the bovine beta B2 crystallin and
RT assignment of the orthologous human locus to chromosome 22.";
RL Curr. Eye Res. 6:1335-1342(1987).
RN [3]
RP GLYCATION AT LYS-11; LYS-48; LYS-68; LYS-76; LYS-101; LYS-108; LYS-120;
RP LYS-121; LYS-140; LYS-168 AND LYS-172, LACK OF GLYCATION AT LYS-18 AND
RP LYS-42, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8954094; DOI=10.1006/bbrc.1996.1768;
RA Zhao H.R., Smith J.B., Jiang X.Y., Abraham E.C.;
RT "Sites of glycation of beta B2-crystallin by glucose and fructose.";
RL Biochem. Biophys. Res. Commun. 229:128-133(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=2234050; DOI=10.1038/347776a0;
RA Bax B., Lapatto R., Nalini V., Driessen H.P.C., Lindley P.F., Mahadevan D.,
RA Blundell T.L., Slingsby C.;
RT "X-ray analysis of beta B2-crystallin and evolution of oligomeric lens
RT proteins.";
RL Nature 347:776-780(1990).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8477703; DOI=10.1111/j.1432-1033.1993.tb17764.x;
RA Carver J.A., Cooper P.G., Truscott R.J.;
RT "1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens.
RT Conformation of the N- and C-terminal extensions.";
RL Eur. J. Biochem. 213:313-320(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 -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; M22466; AAA30472.1; -; mRNA.
DR PIR; A54730; CYBOB.
DR RefSeq; NP_777232.1; NM_174807.1.
DR PDB; 1BLB; X-ray; 3.30 A; A/B/C/D=2-205.
DR PDB; 2BB2; X-ray; 2.10 A; A=15-195.
DR PDBsum; 1BLB; -.
DR PDBsum; 2BB2; -.
DR AlphaFoldDB; P02522; -.
DR PCDDB; P02522; -.
DR SMR; P02522; -.
DR IntAct; P02522; 1.
DR MINT; P02522; -.
DR STRING; 9913.ENSBTAP00000005341; -.
DR iPTMnet; P02522; -.
DR PaxDb; P02522; -.
DR Ensembl; ENSBTAT00000005341; ENSBTAP00000005341; ENSBTAG00000004088.
DR Ensembl; ENSBTAT00000081467; ENSBTAP00000068239; ENSBTAG00000004088.
DR GeneID; 287011; -.
DR KEGG; bta:287011; -.
DR CTD; 1415; -.
DR VEuPathDB; HostDB:ENSBTAG00000004088; -.
DR VGNC; VGNC:27737; CRYBB2.
DR eggNOG; ENOG502QVM6; Eukaryota.
DR GeneTree; ENSGT00940000160048; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P02522; -.
DR OMA; TWVAYQY; -.
DR OrthoDB; 1237607at2759; -.
DR TreeFam; TF331401; -.
DR EvolutionaryTrace; P02522; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000004088; Expressed in anterior segment of eyeball and 40 other tissues.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IPR033058; CRYBB2.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF11; PTHR11818:SF11; 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 3D-structure; Acetylation; Direct protein sequencing; Eye lens protein;
KW Glycation; Glycoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7035168"
FT CHAIN 2..205
FT /note="Beta-crystallin B2"
FT /id="PRO_0000057552"
FT DOMAIN 17..56
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 57..101
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..191
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..16
FT /note="N-terminal arm"
FT REGION 102..106
FT /note="Connecting peptide"
FT REGION 193..205
FT /note="C-terminal arm"
FT SITE 18
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:8954094"
FT SITE 42
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:8954094"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7035168"
FT CARBOHYD 11
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 48
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 68
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 76
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 101
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 108
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 120
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 121
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 140
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 168
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CARBOHYD 172
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954094"
FT CONFLICT 4
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="Q -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="Q -> H (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="H -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 36..37
FT /note="GP -> PG (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="N -> C (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:2BB2"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:2BB2"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2BB2"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2BB2"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2BB2"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:2BB2"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2BB2"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:2BB2"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2BB2"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2BB2"
SQ SEQUENCE 205 AA; 23298 MW; 9613C228491E3C8C CRC64;
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKIT LYENPNFTGK
KMEVIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSGDFGAP
QPQVQSVRRI RDMQWHQRGA FHPSS
