CRBB2_RAT
ID CRBB2_RAT Reviewed; 205 AA.
AC P62697; P19942; P26775;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Beta-crystallin B2;
DE AltName: Full=Beta-B2 crystallin;
DE AltName: Full=Beta-crystallin Bp;
GN Name=Crybb2;
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].
RX PubMed=2753045; DOI=10.1111/j.1432-1033.1989.tb14892.x;
RA Aarts H.J.M., Lubsen N.H., Schoenmakers J.G.G.;
RT "Crystallin gene expression during rat lens development.";
RL Eur. J. Biochem. 183:31-36(1989).
RN [2]
RP SEQUENCE REVISION.
RA Lubsen N.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 9-14.
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).
RN [4]
RP 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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS).
RX PubMed=9655330; DOI=10.1002/pro.5560070602;
RA Wright G., Basak A.K., Wieligmann K., Mayr E.M., Slingsby C.;
RT "Circular permutation of betaB2-crystallin changes the hierarchy of domain
RT assembly.";
RL Protein Sci. 7:1280-1285(1998).
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=23292.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11773034};
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X16072; CAA34204.1; -; mRNA.
DR PIR; S05015; S05015.
DR RefSeq; NP_037069.1; NM_012937.1.
DR RefSeq; XP_017453762.1; XM_017598273.1.
DR PDB; 1BD7; X-ray; 2.78 A; A/B=15-192.
DR PDBsum; 1BD7; -.
DR AlphaFoldDB; P62697; -.
DR PCDDB; P62697; -.
DR SMR; P62697; -.
DR STRING; 10116.ENSRNOP00000067708; -.
DR PhosphoSitePlus; P62697; -.
DR PaxDb; P62697; -.
DR Ensembl; ENSRNOT00000072683; ENSRNOP00000067708; ENSRNOG00000050023.
DR GeneID; 25422; -.
DR KEGG; rno:25422; -.
DR CTD; 1415; -.
DR RGD; 2417; Crybb2.
DR eggNOG; ENOG502QVM6; Eukaryota.
DR GeneTree; ENSGT00940000160048; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P62697; -.
DR OMA; TWVAYQY; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P62697; -.
DR EvolutionaryTrace; P62697; -.
DR PRO; PR:P62697; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000050023; Expressed in colon and 2 other tissues.
DR Genevisible; P62697; RN.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; IEP: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; 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 Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02522"
FT CHAIN 2..205
FT /note="Beta-crystallin B2"
FT /id="PRO_0000057556"
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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02522"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1BD7"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1BD7"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1BD7"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1BD7"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1BD7"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1BD7"
SQ SEQUENCE 205 AA; 23381 MW; 73B4C4789D79B9FA CRC64;
MASDHQTQAG KPQPLNPKII IFEQENFQGH SHELSGPCPN LKETGMEKAG SVLVQAGPWV
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK
KMEIVDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDNSDFGAP
HPQVQSVRRI RDMQWHQRGA FHPSS
