CRBB3_RAT
ID CRBB3_RAT Reviewed; 211 AA.
AC P02524; P70522; Q9ET12;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Beta-crystallin B3;
DE AltName: Full=Beta-B3 crystallin;
DE Contains:
DE RecName: Full=Beta-crystallin B3, N-terminally processed;
GN Name=Crybb3;
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=3879970; DOI=10.1016/0167-4781(85)90035-1;
RA den Dunnen J.T., Moormann R.J.M., Schoenmakers J.G.G.;
RT "Rat lens beta-crystallins are internally duplicated and homologous to
RT gamma-crystallins.";
RL Biochim. Biophys. Acta 824:295-303(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-211, ACETYLATION AT
RP ALA-2, MASS SPECTROMETRY, AND VARIANT LEU-42.
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 [3]
RP PROTEIN SEQUENCE OF 6-11 AND 18-23.
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).
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: [Beta-crystallin B3, N-terminally processed]:
CC Mass=24271.5; Method=Electrospray; Note=Variant Leu-42.;
CC Evidence={ECO:0000269|PubMed:11773034};
CC -!- MASS SPECTROMETRY: [Beta-crystallin B3, N-terminally processed]:
CC Mass=24245.7; Method=Electrospray; Note=Variant Ser-42.;
CC Evidence={ECO:0000269|PubMed:11773034};
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; X05899; CAA29328.1; -; mRNA.
DR EMBL; AF287304; AAF98363.1; -; mRNA.
DR PIR; A02926; CYRTB3.
DR RefSeq; NP_113878.1; NM_031690.1.
DR RefSeq; XP_006249634.1; XM_006249572.2.
DR RefSeq; XP_017453937.1; XM_017598448.1.
DR AlphaFoldDB; P02524; -.
DR SMR; P02524; -.
DR STRING; 10116.ENSRNOP00000067156; -.
DR iPTMnet; P02524; -.
DR PhosphoSitePlus; P02524; -.
DR PaxDb; P02524; -.
DR Ensembl; ENSRNOT00000071328; ENSRNOP00000067156; ENSRNOG00000047673.
DR GeneID; 64349; -.
DR KEGG; rno:64349; -.
DR CTD; 1417; -.
DR RGD; 61980; Crybb3.
DR eggNOG; ENOG502QTNZ; Eukaryota.
DR GeneTree; ENSGT00940000158425; -.
DR HOGENOM; CLU_081883_0_1_1; -.
DR InParanoid; P02524; -.
DR OMA; NEWNASQ; -.
DR OrthoDB; 1237607at2759; -.
DR PhylomeDB; P02524; -.
DR PRO; PR:P02524; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Genevisible; P02524; RN.
DR GO; GO:0005212; F:structural constituent of eye lens; IDA:RGD.
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; IPR033115; CRYBB3.
DR InterPro; IPR011024; G_crystallin-like.
DR PANTHER; PTHR11818:SF13; PTHR11818:SF13; 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;
KW Reference proteome; Repeat.
FT CHAIN 1..211
FT /note="Beta-crystallin B3"
FT /id="PRO_0000423201"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:11773034"
FT CHAIN 2..211
FT /note="Beta-crystallin B3, N-terminally processed"
FT /id="PRO_0000057562"
FT DOMAIN 24..63
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 64..108
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 114..155
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 156..198
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 2..23
FT /note="N-terminal arm"
FT REGION 109..113
FT /note="Connecting peptide"
FT REGION 200..211
FT /note="C-terminal arm"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P26998"
FT MOD_RES 2
FT /note="N-acetylalanine; in Beta-crystallin B3, N-terminally
FT processed"
FT /evidence="ECO:0000269|PubMed:11773034"
FT VARIANT 42
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:11773034"
FT CONFLICT 14
FT /note="S -> N (in Ref. 1; CAA29328)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="R -> A (in Ref. 1; CAA29328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24334 MW; D3B694BF858A94DB CRC64;
MAEQHGAPEQ AAASKSHGGL GGSYKVTVYE LENFQGKRCE LSAECPNLTE SLLQKVGSIQ
VESGPWLAFE RRAFRGEQFV LEKGDYPRWD AWSSSRRSDI LLSLRPLHID GPDHKLHLFE
NPAFSGRKME IVDDDVPSLW AHGFQDRVAS IRVINGTWVG YEFPGYRGRQ YVFERGEFRH
WNEWDANQPQ LQSVRRIRDQ KWHKRGCFLS S
