CRGB_BOVIN
ID CRGB_BOVIN Reviewed; 175 AA.
AC P02526; A2TJU8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Gamma-crystallin B;
DE AltName: Full=Gamma-B-crystallin;
DE AltName: Full=Gamma-crystallin II;
GN Name=CRYGB;
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=3606621; DOI=10.1016/0006-291x(87)90729-7;
RA Hay R.E., Woods W.D., Church R.L., Petrash J.M.;
RT "cDNA clones encoding bovine gamma-crystallins.";
RL Biochem. Biophys. Res. Commun. 146:332-338(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=6092016; DOI=10.1089/dna.1.1984.3.287;
RA Bhat S.P., Spector A.;
RT "Complete nucleotide sequence of a cDNA derived from calf lens gamma-
RT crystallin mRNA: presence of Alu I-like DNA sequences.";
RL DNA 3:287-295(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Wistow G.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=3255364; DOI=10.1007/bf01025415;
RA Chiou S.H., Azari P., Himmel M.E.;
RT "Physicochemical characterization of gamma-crystallins from bovine lens
RT -- hydrodynamic and biochemical properties.";
RL J. Protein Chem. 7:67-80(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-26, AND DISULFIDE BOND.
RX PubMed=3364984; DOI=10.1016/0003-9861(88)90413-4;
RA McDermott M.J., Gawinowicz-Kolks M.A., Chiesa R., Spector A.;
RT "The disulfide content of calf gamma-crystallin.";
RL Arch. Biochem. Biophys. 262:609-619(1988).
RN [6]
RP GLYCATION AT LYS-3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8954545; DOI=10.1006/abio.1996.0501;
RA Smith J.B., Hanson S.R., Cerny R.L., Zhao H.R., Abraham E.C.;
RT "Identification of the glycation site of lens gamma B-crystallin by fast
RT atom bombardment tandem mass spectrometry.";
RL Anal. Biochem. 243:186-189(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=7464942; DOI=10.1038/289771a0;
RA Blundell T.L., Lindley P., Miller L., Moss D., Slingsby C., Tickle I.,
RA Turnell B., Wistow G.;
RT "The molecular structure and stability of the eye lens: X-ray analysis of
RT gamma-crystallin II.";
RL Nature 289:771-777(1981).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=6631960; DOI=10.1016/s0022-2836(83)80232-0;
RA Wistow G., Turnell B., Summers L., Slingsby C., Moss D., Miller L.,
RA Lindley P., Blundell T.L.;
RT "X-ray analysis of the eye lens protein gamma-II crystallin at 1.9-A
RT resolution.";
RL J. Mol. Biol. 170:175-202(1983).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS).
RX PubMed=15299528; DOI=10.1107/s0907444992007601;
RA Najmudin S., Nalini V., Dreissen H.P.C., Slingsby C., Blundell T.L.,
RA Moss D.S., Lindley P.F.;
RT "Structure of the bovine eye lens protein gammaB (gammaII)-crystallin at
RT 1.47 A.";
RL Acta Crystallogr. D 49:223-233(1993).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=15299624; DOI=10.1107/s0907444995014302;
RA Kumaraswamy V.S., Lindley P.F., Slingsby C., Glover I.D.;
RT "An eye lens protein-water structure: 1.2-A resolution structure of gammaB-
RT crystallin at 150 K.";
RL Acta Crystallogr. D 52:611-622(1996).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=9541393; DOI=10.1002/pro.5560070310;
RA Palme S., Jaenicke R., Slingsby C.;
RT "X-ray structures of three interface mutants of gammaB-crystallin from
RT bovine eye lens.";
RL Protein Sci. 7:611-618(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ALA-57.
RX PubMed=9642083; DOI=10.1006/jmbi.1998.1850;
RA Palme S., Jaenicke R., Slingsby C.;
RT "Unusual domain pairing in a mutant of bovine lens gammaB-crystallin.";
RL J. Mol. Biol. 279:1053-1059(1998).
CC -!- FUNCTION: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
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; X01036; CAA25518.1; -; mRNA.
DR EMBL; M16894; AAA30476.1; -; mRNA.
DR EMBL; EF208024; ABM97504.1; -; mRNA.
DR PIR; A29655; CYBOG.
DR RefSeq; NP_001013612.1; NM_001013594.1.
DR PDB; 1AMM; X-ray; 1.20 A; A=2-175.
DR PDB; 1DSL; X-ray; 1.55 A; A=88-175.
DR PDB; 1GAM; X-ray; 2.60 A; A/B=88-173.
DR PDB; 1GCS; X-ray; 2.00 A; A=2-175.
DR PDB; 1I5I; X-ray; 2.40 A; A=2-175.
DR PDB; 4GCR; X-ray; 1.47 A; A=2-175.
DR PDB; 4W9A; X-ray; 1.38 A; A=1-175.
DR PDB; 4W9B; X-ray; 1.28 A; A=1-175.
DR PDB; 6QDW; EM; 2.83 A; z=1-38.
DR PDB; 6YS3; EM; 2.58 A; z=1-38.
DR PDBsum; 1AMM; -.
DR PDBsum; 1DSL; -.
DR PDBsum; 1GAM; -.
DR PDBsum; 1GCS; -.
DR PDBsum; 1I5I; -.
DR PDBsum; 4GCR; -.
DR PDBsum; 4W9A; -.
DR PDBsum; 4W9B; -.
DR PDBsum; 6QDW; -.
DR PDBsum; 6YS3; -.
DR AlphaFoldDB; P02526; -.
DR PCDDB; P02526; -.
DR SMR; P02526; -.
DR STRING; 9913.ENSBTAP00000009553; -.
DR PaxDb; P02526; -.
DR PRIDE; P02526; -.
DR Ensembl; ENSBTAT00000009553; ENSBTAP00000009553; ENSBTAG00000021770.
DR GeneID; 281720; -.
DR KEGG; bta:281720; -.
DR CTD; 1419; -.
DR VEuPathDB; HostDB:ENSBTAG00000021770; -.
DR VGNC; VGNC:55341; CRYGB.
DR eggNOG; ENOG502RXJY; Eukaryota.
DR GeneTree; ENSGT00940000156190; -.
DR HOGENOM; CLU_081883_1_1_1; -.
DR InParanoid; P02526; -.
DR OMA; AYRMKIY; -.
DR OrthoDB; 1220704at2759; -.
DR EvolutionaryTrace; P02526; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000021770; Expressed in floor plate of diencephalon and 9 other tissues.
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; 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 3D-structure; Direct protein sequencing; Disulfide bond; Eye lens protein;
KW Glycation; Glycoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3255364,
FT ECO:0000269|PubMed:3364984"
FT CHAIN 2..175
FT /note="Gamma-crystallin B"
FT /id="PRO_0000057581"
FT DOMAIN 2..40
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 41..83
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 89..129
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 130..172
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 84..88
FT /note="Connecting peptide"
FT CARBOHYD 3
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:8954545"
FT DISULFID 19..23
FT /evidence="ECO:0000269|PubMed:3364984"
FT CONFLICT 120
FT /note="T -> S (in Ref. 2; CAA25518)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:1AMM"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1AMM"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1AMM"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6YS3"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1AMM"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1AMM"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1AMM"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1AMM"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1AMM"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1AMM"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1AMM"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1AMM"
SQ SEQUENCE 175 AA; 21097 MW; 0CF283DA837CC593 CRC64;
MGKITFYEDR GFQGHCYECS SDCPNLQPYF SRCNSIRVDS GCWMLYERPN YQGHQYFLRR
GDYPDYQQWM GFNDSIRSCR LIPQHTGTFR MRIYERDDFR GQMSEITDDC PSLQDRFHLT
EVHSLNVLEG SWVLYEMPSY RGRQYLLRPG EYRRYLDWGA MNAKVGSLRR VMDFY
