CRYAB_MOUSE
ID CRYAB_MOUSE Reviewed; 175 AA.
AC P23927; Q64325;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
DE AltName: Full=P23;
GN Name=Cryab {ECO:0000312|MGI:MGI:88516}; Synonyms=Crya2;
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], AND PROTEIN SEQUENCE OF 1-10 AND 68-81.
RX PubMed=1846673; DOI=10.1128/mcb.11.2.803-812.1991;
RA Klemenz R., Froehli E., Aoyama A., Hoffmann S., Simpson R.J., Moritz R.L.,
RA Schaeffer R.;
RT "Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos
RT oncogene expression in mouse NIH 3T3 fibroblasts.";
RL Mol. Cell. Biol. 11:803-812(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=7838723; DOI=10.1093/nar/22.25.5686;
RA Frederikse P.H., Dubin R.A., Haynes J.I., Piatigorsky J.;
RT "Structure and alternate tissue-preferred transcription initiation of the
RT mouse alpha B-crystallin/small heat shock protein gene.";
RL Nucleic Acids Res. 22:5686-5694(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=2725488; DOI=10.1128/mcb.9.3.1083-1091.1989;
RA Dubin R.A., Wawrousek E.F., Piatigorsky J.;
RT "Expression of the murine alpha B-crystallin gene is not restricted to the
RT lens.";
RL Mol. Cell. Biol. 9:1083-1091(1989).
RN [5]
RP PROTEIN SEQUENCE OF 12-22 AND 124-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH HSPBAP1.
RX PubMed=10751411; DOI=10.1074/jbc.m001981200;
RA Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
RT "Identification and characterization of a novel protein from Sertoli cells,
RT PASS1, that associates with mammalian small stress protein hsp27.";
RL J. Biol. Chem. 275:18724-18731(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH ATP6V1A AND MTOR, SUBCELLULAR LOCATION, AND INDUCTION BY
RP HSF4.
RX PubMed=31786107; DOI=10.1016/j.bbagen.2019.129496;
RA Cui X., Feng R., Wang J., Du C., Pi X., Chen D., Li J., Li H., Zhang J.,
RA Zhang J., Mu H., Zhang F., Liu M., Hu Y.;
RT "Heat shock factor 4 regulates lysosome activity by modulating the alphaB-
RT crystallin-ATP6V1A-mTOR complex in ocular lens.";
RL Biochim. Biophys. Acta 1864:129496-129496(2020).
CC -!- FUNCTION: May contribute to the transparency and refractive index of
CC the lens. Has chaperone-like activity, preventing aggregation of
CC various proteins under a wide range of stress conditions. In lens
CC epithelial cells, stabilizes the ATP6V1A protein, preventing its
CC degradation by the proteasome (PubMed:31786107).
CC {ECO:0000269|PubMed:31786107}.
CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits.
CC Aggregates with homologous proteins, including the small heat shock
CC protein HSPB1, to form large heteromeric complexes. Inter-subunit
CC bridging via zinc ions enhances stability, which is crucial as there is
CC no protein turn over in the lens (By similarity). Interacts with
CC HSPBAP1 (PubMed:10751411). Interacts with TTN/titin. Interacts with
CC TMEM109. Interacts with DES; binds rapidly during early stages of DES
CC filament assembly and a reduced binding seen in the later stages.
CC Interacts with TMED10; the interaction mediates the translocation from
CC the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate
CC compartment) and thereby secretion (By similarity). Interacts with
CC ATP6V1A and with MTOR, forming a ternary complex (PubMed:31786107).
CC {ECO:0000250|UniProtKB:P02511, ECO:0000269|PubMed:10751411,
CC ECO:0000269|PubMed:31786107}.
CC -!- INTERACTION:
CC P23927; P42227: Stat3; NbExp=3; IntAct=EBI-299046, EBI-602878;
CC P23927; P07320: CRYGD; Xeno; NbExp=2; IntAct=EBI-299046, EBI-7673124;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}.
CC Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome
CC {ECO:0000305|PubMed:31786107}. Note=Translocates to the nucleus during
CC heat shock and resides in sub-nuclear structures known as SC35 speckles
CC or nuclear splicing speckles. Localizes at the Z-bands and the
CC intercalated disk in cardiomyocytes. Can be secreted; the secretion is
CC dependent on protein unfolding and facilitated by the cargo receptor
CC TMED10; it results in protein translocation from the cytoplasm into the
CC ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed
CC by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
CC -!- TISSUE SPECIFICITY: Lens as well as other tissues.
CC -!- INDUCTION: Up-regulated by HSF4. {ECO:0000269|PubMed:31786107}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; M63170; AAA37472.1; -; mRNA.
DR EMBL; M73741; AAA67045.1; -; Genomic_DNA.
DR EMBL; BC010768; AAH10768.1; -; mRNA.
DR EMBL; M25770; AAA37133.1; -; Genomic_DNA.
DR CCDS; CCDS23172.1; -.
DR PIR; A39608; A39608.
DR RefSeq; NP_001276711.1; NM_001289782.1.
DR RefSeq; NP_001276713.1; NM_001289784.1.
DR RefSeq; NP_001276714.1; NM_001289785.1.
DR RefSeq; NP_034094.1; NM_009964.3.
DR RefSeq; XP_006510033.1; XM_006509970.3.
DR AlphaFoldDB; P23927; -.
DR BMRB; P23927; -.
DR SMR; P23927; -.
DR BioGRID; 198909; 26.
DR DIP; DIP-31060N; -.
DR IntAct; P23927; 16.
DR MINT; P23927; -.
DR STRING; 10090.ENSMUSP00000034562; -.
DR iPTMnet; P23927; -.
DR PhosphoSitePlus; P23927; -.
DR SWISS-2DPAGE; P23927; -.
DR jPOST; P23927; -.
DR PaxDb; P23927; -.
DR PeptideAtlas; P23927; -.
DR PRIDE; P23927; -.
DR ProteomicsDB; 278038; -.
DR TopDownProteomics; P23927; -.
DR Antibodypedia; 3674; 1725 antibodies from 48 providers.
DR DNASU; 12955; -.
DR Ensembl; ENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
DR Ensembl; ENSMUST00000214962; ENSMUSP00000149759; ENSMUSG00000032060.
DR Ensembl; ENSMUST00000216755; ENSMUSP00000150669; ENSMUSG00000032060.
DR Ensembl; ENSMUST00000217475; ENSMUSP00000149803; ENSMUSG00000032060.
DR GeneID; 12955; -.
DR KEGG; mmu:12955; -.
DR UCSC; uc009pkl.2; mouse.
DR CTD; 1410; -.
DR MGI; MGI:88516; Cryab.
DR VEuPathDB; HostDB:ENSMUSG00000032060; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P23927; -.
DR OMA; RPSFMRW; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P23927; -.
DR TreeFam; TF105049; -.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR BioGRID-ORCS; 12955; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cryab; mouse.
DR PRO; PR:P23927; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P23927; protein.
DR Bgee; ENSMUSG00000032060; Expressed in epithelium of lens and 246 other tissues.
DR ExpressionAtlas; P23927; baseline and differential.
DR Genevisible; P23927; MM.
DR GO; GO:0032432; C:actin filament bundle; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031674; C:I band; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005212; F:structural constituent of eye lens; TAS:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IGI:MGI.
DR GO; GO:0043010; P:camera-type eye development; IGI:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IGI:MGI.
DR GO; GO:0031109; P:microtubule polymerization or depolymerization; ISO:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IGI:MGI.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0010941; P:regulation of cell death; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0007021; P:tubulin complex assembly; IMP:MGI.
DR CDD; cd06498; ACD_alphaB-crystallin_HspB5; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037882; ACD_alphaB-crystallin.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR003090; Alpha-crystallin_N.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR Pfam; PF00525; Crystallin; 1.
DR Pfam; PF00011; HSP20; 1.
DR PIRSF; PIRSF036514; Sm_HSP_B1; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Eye lens protein; Lysosome; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Secreted; Zinc.
FT CHAIN 1..175
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125910"
FT DOMAIN 56..164
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 145..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02510, ECO:0000305"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02510"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02511"
FT MOD_RES 166
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02511"
SQ SEQUENCE 175 AA; 20069 MW; 46702976C008EFD3 CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK
