CRBA1_MOUSE
ID CRBA1_MOUSE Reviewed; 198 AA.
AC P02525;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Beta-crystallin A1;
DE AltName: Full=Beta-A1-crystallin;
GN Name=Cryba1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX PubMed=6835368; DOI=10.1038/302310a0;
RA Inana G., Piatigorsky J., Norman B., Slingsby C., Blundell T.L.;
RT "Gene and protein structure of a beta-crystallin polypeptide in murine
RT lens: relationship of exons and structural motifs.";
RL Nature 302:310-315(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-198.
RX PubMed=6896514; DOI=10.1016/s0021-9258(18)34243-1;
RA Inana G., Shinohara T., Maizel J.V. Jr., Piatigorsky J.;
RT "Evolution and diversity of the crystallins. Nucleotide sequence of a beta-
RT crystallin mRNA from the mouse lens.";
RL J. Biol. Chem. 257:9064-9071(1982).
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; AL591136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; V00729; CAA24107.1; -; Genomic_DNA.
DR EMBL; V00728; CAA24106.1; -; mRNA.
DR EMBL; J00378; AAA51629.1; -; mRNA.
DR PIR; A02927; CYMSB.
DR AlphaFoldDB; P02525; -.
DR SMR; P02525; -.
DR STRING; 10090.ENSMUSP00000077693; -.
DR PhosphoSitePlus; P02525; -.
DR MaxQB; P02525; -.
DR PaxDb; P02525; -.
DR PRIDE; P02525; -.
DR ProteomicsDB; 284114; -.
DR MGI; MGI:88518; Cryba1.
DR eggNOG; ENOG502QSM0; Eukaryota.
DR InParanoid; P02525; -.
DR ChiTaRS; Cryba1; mouse.
DR PRO; PR:P02525; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P02525; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISO:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
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 2: Evidence at transcript level;
KW Eye lens protein; Glutathionylation; Methylation; Reference proteome;
KW Repeat.
FT CHAIN 1..198
FT /note="Beta-crystallin A1"
FT /id="PRO_0000057534"
FT DOMAIN 14..53
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 54..100
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..197
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 1..13
FT /note="N-terminal arm"
FT REGION 101..106
FT /note="Connecting peptide"
FT MOD_RES 65
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="S-methylcysteine; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 111
FT /note="I -> N (in Ref. 3; CAA24106/AAA51629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 23401 MW; F7EBDD750402FEC5 CRC64;
MLYLVLFLVP FNSIQITIYD QENFQGKRME FTSSCPNVSE RNFDNVRSLK VECGAWIGYE
HTSFCGQQFI LERGEYPRWD AWSGSNAYHI ERLMSFRPIC SANHKESKIT IFEKENFIGR
QWEICDDYPS LQAMGWFNNE VGSMKIQCGA WVCYQYPGYR GYQYILECDH HGGDYKHWPE
WGSHAQTSQI QSIRRIQQ
