CRYAB_RAT
ID CRYAB_RAT Reviewed; 175 AA.
AC P23928; Q6LDR2;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=Cryab {ECO:0000312|RGD:2414};
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=2176207; DOI=10.1016/s0021-9258(18)45689-x;
RA Iwaki A., Iwaki T., Goldman J.E., Liem R.K.;
RT "Multiple mRNAs of rat brain alpha-crystallin B chain result from
RT alternative transcriptional initiation.";
RL J. Biol. Chem. 265:22197-22203(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart, and Lens;
RX PubMed=1765091; DOI=10.1111/j.1432-1033.1991.tb16432.x;
RA Bhat S.P., Horwitz J., Srinivasan A.N., Ding L.;
RT "Alpha B-crystallin exists as an independent protein in the heart and in
RT the lens.";
RL Eur. J. Biochem. 202:775-781(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=1764082; DOI=10.1016/0006-291x(91)92083-v;
RA Atomi Y., Yamada S., Nishida T.;
RT "Early changes of alpha B-crystallin mRNA in rat skeletal muscle to
RT mechanical tension and denervation.";
RL Biochem. Biophys. Res. Commun. 181:1323-1330(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Spleen;
RA Srinivasan A.N., Bhat S.P.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=1783614; DOI=10.1093/oxfordjournals.jbchem.a123665;
RA Atomi Y., Yamada S., Strohman R., Nonomura Y.;
RT "Alpha B-crystallin in skeletal muscle: purification and localization.";
RL J. Biochem. 110:812-822(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-175.
RC TISSUE=Heart;
RX PubMed=2912453; DOI=10.1016/s0006-291x(89)80215-3;
RA Bhat S.P., Nagineni C.N.;
RT "Alpha-B subunit of lens-specific protein alpha-crystallin is present in
RT other ocular and non-ocular tissues.";
RL Biochem. Biophys. Res. Commun. 158:319-325(1989).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=8282729; DOI=10.1093/oxfordjournals.jbchem.a124184;
RA Inaguma Y., Goto S., Shinohara H., Hasegawa K., Ohshima K., Kato K.;
RT "Physiological and pathological changes in levels of the two small stress
RT proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles.";
RL J. Biochem. 114:378-384(1993).
RN [8]
RP GLYCOSYLATION AT THR-170.
RX PubMed=8639509; DOI=10.1021/bi951918j;
RA Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W.;
RT "Dynamic O-GlcNAcylation of the small heat shock protein alpha B-
RT crystallin.";
RL Biochemistry 35:3578-3586(1996).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P23927}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P02511, ECO:0000250|UniProtKB:P23927,
CC ECO:0000269|PubMed:10751411}.
CC -!- INTERACTION:
CC P23928; Q9WVJ5: Crybb1; Xeno; NbExp=2; IntAct=EBI-916888, EBI-8520354;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus
CC {ECO:0000250|UniProtKB:P02511}. Secreted
CC {ECO:0000250|UniProtKB:P02511}. Lysosome
CC {ECO:0000250|UniProtKB:P23927}. 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 -!- DEVELOPMENTAL STAGE: Levels are low in both the slow-twitch soleus and
CC fast-twitch rectus femoris muscles at prenatal day 2, then increase
CC slowly until postnatal day 3. At 2 weeks, levels in the rectus femoris
CC muscle then decrease while those in the soleus muscle increase sharply,
CC reaching adult levels by 4 weeks. {ECO:0000269|PubMed:8282729}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42911.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S74229; AAB20759.1; -; mRNA.
DR EMBL; S77138; AAP31995.1; -; mRNA.
DR EMBL; M55534; AAA40977.1; -; mRNA.
DR EMBL; X60352; CAA42911.1; ALT_INIT; mRNA.
DR EMBL; X60351; CAA42910.1; -; mRNA.
DR EMBL; S77142; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U04320; AAA03655.1; -; Unassigned_DNA.
DR EMBL; M24092; AAA40978.1; -; mRNA.
DR PIR; A23681; A23681.
DR RefSeq; NP_037067.1; NM_012935.4.
DR AlphaFoldDB; P23928; -.
DR BMRB; P23928; -.
DR SMR; P23928; -.
DR BioGRID; 247455; 3.
DR IntAct; P23928; 4.
DR MINT; P23928; -.
DR STRING; 10116.ENSRNOP00000055901; -.
DR GlyConnect; 34; 1 O-Linked glycan.
DR GlyGen; P23928; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P23928; -.
DR PhosphoSitePlus; P23928; -.
DR jPOST; P23928; -.
DR PaxDb; P23928; -.
DR PRIDE; P23928; -.
DR Ensembl; ENSRNOT00000059127; ENSRNOP00000055901; ENSRNOG00000010524.
DR GeneID; 25420; -.
DR KEGG; rno:25420; -.
DR UCSC; RGD:2414; rat.
DR CTD; 1410; -.
DR RGD; 2414; Cryab.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; P23928; -.
DR OMA; RPSFMRW; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P23928; -.
DR TreeFam; TF105049; -.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR PRO; PR:P23928; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010524; Expressed in heart and 20 other tissues.
DR Genevisible; P23928; RN.
DR GO; GO:0032432; C:actin filament bundle; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0097512; C:cardiac myofibril; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0031674; C:I band; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IDA:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0005212; F:structural constituent of eye lens; TAS:RGD.
DR GO; GO:0005198; F:structural molecule activity; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0031109; P:microtubule polymerization or depolymerization; IMP:RGD.
DR GO; GO:0010259; P:multicellular organism aging; IEP:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0032387; P:negative regulation of intracellular transport; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:RGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0010941; P:regulation of cell death; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IMP:RGD.
DR GO; GO:0007021; P:tubulin complex assembly; ISO:RGD.
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; Glycoprotein; Lysosome; Metal-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Secreted; Zinc.
FT CHAIN 1..175
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125913"
FT DOMAIN 56..164
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 142..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:0000250|UniProtKB:P02510"
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:16641100,
FT ECO:0007744|PubMed:22673903"
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"
FT CARBOHYD 170
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:8639509"
FT /id="CAR_000058"
SQ SEQUENCE 175 AA; 20089 MW; AB66796291518B9B CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW
IDTGLSEMRM EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK
