CRBA1_RAT
ID CRBA1_RAT Reviewed; 215 AA.
AC P14881; O35237;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Beta-crystallin A3;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta4 form;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta7 form;
DE Contains:
DE RecName: Full=Beta-crystallin A3, isoform A1, Delta8 form;
GN Name=Cryba1;
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] OF 1-52, PROTEIN SEQUENCE, ACETYLATION, AND MASS
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-215.
RC TISSUE=Lens;
RX PubMed=2499686; DOI=10.1007/bf02103427;
RA Aarts H.J.M., Jacobs E.H.M., van Willigen G., Lubsen N.H.,
RA Schoenmakers J.G.G.;
RT "Different evolution rates within the lens-specific beta-crystallin gene
RT family.";
RL J. Mol. Evol. 28:313-321(1989).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=A3;
CC IsoId=P14881-1; Sequence=Displayed;
CC Name=A1;
CC IsoId=P14881-2; Sequence=VSP_018711;
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 several truncated forms. {ECO:0000250}.
CC -!- PTM: The initiator methionine for isoform A1 is removed. The new N-
CC terminal amino acid is then N-acetylated (By similarity).
CC {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Beta-crystallin A3]: Mass=25308.9;
CC Method=Electrospray; Note=Isoform A3.;
CC Evidence={ECO:0000269|PubMed:11773034};
CC -!- MASS SPECTROMETRY: [Isoform A1]: Mass=23191.3; Method=Electrospray;
CC Note=Isoform A1. The measured range is 2-198.;
CC Evidence={ECO:0000269|PubMed:11773034};
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
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DR EMBL; AF013248; AAB67118.1; -; mRNA.
DR EMBL; X15143; CAA33241.1; -; mRNA.
DR RefSeq; NP_037188.1; NM_013056.1. [P14881-1]
DR AlphaFoldDB; P14881; -.
DR SMR; P14881; -.
DR STRING; 10116.ENSRNOP00000011608; -.
DR PhosphoSitePlus; P14881; -.
DR PaxDb; P14881; -.
DR DNASU; 25583; -.
DR Ensembl; ENSRNOT00000011608; ENSRNOP00000011608; ENSRNOG00000008700. [P14881-1]
DR GeneID; 25583; -.
DR KEGG; rno:25583; -.
DR CTD; 1411; -.
DR RGD; 2415; Cryba1.
DR eggNOG; ENOG502QSM0; Eukaryota.
DR GeneTree; ENSGT00940000159685; -.
DR HOGENOM; CLU_081883_0_0_1; -.
DR InParanoid; P14881; -.
DR OMA; IGRQWEM; -.
DR OrthoDB; 1142622at2759; -.
DR PhylomeDB; P14881; -.
DR TreeFam; TF331401; -.
DR PRO; PR:P14881; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000008700; Expressed in cerebellum and 3 other tissues.
DR Genevisible; P14881; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; IEP:RGD.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:RGD.
DR GO; GO:0032007; P:negative regulation of TOR signaling; IMP:RGD.
DR GO; GO:0006909; P:phagocytosis; IMP:RGD.
DR GO; GO:2000210; P:positive regulation of anoikis; IMP:RGD.
DR GO; GO:0010506; P:regulation of autophagy; IMP:RGD.
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 Acetylation; Alternative initiation; Direct protein sequencing;
KW Eye lens protein; Glutathionylation; Methylation; Reference proteome;
KW Repeat.
FT CHAIN 1..215
FT /note="Beta-crystallin A3"
FT /id="PRO_0000006333"
FT CHAIN 23..215
FT /note="Beta-crystallin A3, isoform A1, Delta4 form"
FT /id="PRO_0000226695"
FT CHAIN 26..215
FT /note="Beta-crystallin A3, isoform A1, Delta7 form"
FT /id="PRO_0000226696"
FT CHAIN 27..215
FT /note="Beta-crystallin A3, isoform A1, Delta8 form"
FT /id="PRO_0000226697"
FT DOMAIN 31..70
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 71..117
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 124..165
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 166..214
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..30
FT /note="N-terminal arm"
FT REGION 118..123
FT /note="Connecting peptide"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P05813"
FT MOD_RES 82
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 82
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform A1)"
FT /evidence="ECO:0000305"
FT /id="VSP_018711"
FT INIT_MET P14881-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P14881-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 215 AA; 25270 MW; 3842A801352A96C3 CRC64;
METQTVQREL ETLPTTKMAQ TNPMPGSMGP WKITIYDQEN FQGKRMEFTS SCPNVSERSF
DNVRSLKVEC GAWIGYEHTS FCGQQFILER GEYPRWDAWS GSNAYHIERL MSFRPICSAN
HKESKITIFE KENFIGRQWE ICDDYPSLQA MGWFNNEVGS MKIQCGAWVC YQYPGYRGYQ
YILECDHHGG DYKHWREWGT HAQTSQIQSI RRIQQ
