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CRBA4_MOUSE
ID   CRBA4_MOUSE             Reviewed;         196 AA.
AC   Q9JJV0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Beta-crystallin A4;
DE   AltName: Full=Beta-A4 crystallin;
GN   Name=Cryba4;
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 [MRNA].
RA   Graw J.;
RT   "Sequence analysis of beta-A2-, beta-A4- and beta-B3-crystallin cDNA
RT   completes the identification of the members of this gene family in the
RT   mouse.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; AJ272228; CAB75586.1; -; mRNA.
DR   EMBL; BC056444; AAH56444.1; -; mRNA.
DR   EMBL; BC058703; AAH58703.1; -; mRNA.
DR   CCDS; CCDS19536.1; -.
DR   RefSeq; NP_001299813.1; NM_001312884.1.
DR   RefSeq; NP_067326.1; NM_021351.2.
DR   AlphaFoldDB; Q9JJV0; -.
DR   SMR; Q9JJV0; -.
DR   BioGRID; 198912; 1.
DR   STRING; 10090.ENSMUSP00000108004; -.
DR   PhosphoSitePlus; Q9JJV0; -.
DR   MaxQB; Q9JJV0; -.
DR   PaxDb; Q9JJV0; -.
DR   PRIDE; Q9JJV0; -.
DR   ProteomicsDB; 284116; -.
DR   Antibodypedia; 24295; 141 antibodies from 22 providers.
DR   DNASU; 12959; -.
DR   Ensembl; ENSMUST00000086629; ENSMUSP00000083826; ENSMUSG00000066975.
DR   Ensembl; ENSMUST00000112385; ENSMUSP00000108004; ENSMUSG00000066975.
DR   GeneID; 12959; -.
DR   KEGG; mmu:12959; -.
DR   UCSC; uc008yst.1; mouse.
DR   CTD; 1413; -.
DR   MGI; MGI:102716; Cryba4.
DR   VEuPathDB; HostDB:ENSMUSG00000066975; -.
DR   eggNOG; ENOG502QTF8; Eukaryota.
DR   GeneTree; ENSGT00940000160372; -.
DR   InParanoid; Q9JJV0; -.
DR   OMA; GEYPSWE; -.
DR   OrthoDB; 1142622at2759; -.
DR   PhylomeDB; Q9JJV0; -.
DR   TreeFam; TF331401; -.
DR   BioGRID-ORCS; 12959; 4 hits in 75 CRISPR screens.
DR   ChiTaRS; Cryba4; mouse.
DR   PRO; PR:Q9JJV0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9JJV0; protein.
DR   Bgee; ENSMUSG00000066975; Expressed in lens of camera-type eye and 48 other tissues.
DR   ExpressionAtlas; Q9JJV0; baseline and differential.
DR   Genevisible; Q9JJV0; MM.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0005212; F:structural constituent of eye lens; ISO:MGI.
DR   GO; GO:0043010; P:camera-type eye development; ISO:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; ISO:MGI.
DR   InterPro; IPR001064; Beta/gamma_crystallin.
DR   InterPro; IPR033342; CRYBA4.
DR   InterPro; IPR011024; G_crystallin-like.
DR   PANTHER; PTHR11818:SF19; PTHR11818:SF19; 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   2: Evidence at transcript level;
KW   Acetylation; Eye lens protein; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P53673"
FT   CHAIN           2..196
FT                   /note="Beta-crystallin A4"
FT                   /id="PRO_0000057546"
FT   DOMAIN          12..51
FT                   /note="Beta/gamma crystallin 'Greek key' 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          52..98
FT                   /note="Beta/gamma crystallin 'Greek key' 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          105..146
FT                   /note="Beta/gamma crystallin 'Greek key' 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   DOMAIN          147..195
FT                   /note="Beta/gamma crystallin 'Greek key' 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT   REGION          2..11
FT                   /note="N-terminal arm"
FT   REGION          99..104
FT                   /note="Connecting peptide"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P53673"
SQ   SEQUENCE   196 AA;  22469 MW;  5911B1C784DD253B CRC64;
     MTLQCTKSAG HWRMVVWDEE GFQGRRHEFT AECPSVLELG FETVRSLKVL SGAWVGFEHA
     GFQGQQYVLE RGDYPGWDAW GGNTAYPAER LTSFRPVACA NHRDSRLTIF EQENFLGRKG
     ELNDDYPSLQ AMGWDGTEVG SFHVQSGAWV CSQFPGYRGF QYILESDHHS GDYKHFREWG
     SHAHTFQVQS VRRIQQ
 
 
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