CRYAB_RABIT
ID CRYAB_RABIT Reviewed; 175 AA.
AC P41316;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lens;
RX PubMed=8427639; DOI=10.1007/bf01024920;
RA Parveen R., Smith J.B., Sun Y., Smith D.L.;
RT "Primary structure of rabbit lens alpha-crystallins.";
RL J. Protein Chem. 12:93-101(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=8814151;
RA Krausz E., Augusteyn R.C., Quinlan R.A., Reddan J.R., Russell P., Sax C.M.,
RA Graw J.;
RT "Expression of crystallins, Pax6, filensin, CP49, MIP, and MP20 in lens-
RT derived cell lines.";
RL Invest. Ophthalmol. Vis. Sci. 37:2120-2128(1996).
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. Interacts with HSPBAP1 and TTN/titin.
CC Interacts with TMEM109. Interacts with DES; binds rapidly during early
CC stages of DES filament assembly and a reduced binding seen in the later
CC stages. Interacts with TMED10; the interaction mediates the
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) and thereby secretion. Interacts with
CC ATP6V1A and with MTOR, forming a ternary complex (By similarity).
CC {ECO:0000250|UniProtKB:P02511, ECO:0000250|UniProtKB:P23927}.
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 -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X95383; CAA64669.1; -; mRNA.
DR PIR; A53871; A53871.
DR RefSeq; NP_001075876.1; NM_001082407.1.
DR AlphaFoldDB; P41316; -.
DR BMRB; P41316; -.
DR SMR; P41316; -.
DR STRING; 9986.ENSOCUP00000011163; -.
DR iPTMnet; P41316; -.
DR Ensembl; ENSOCUT00000012969; ENSOCUP00000011163; ENSOCUG00000012972.
DR GeneID; 100009295; -.
DR KEGG; ocu:100009295; -.
DR CTD; 1410; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR InParanoid; P41316; -.
DR OMA; RPSFMRW; -.
DR OrthoDB; 1187096at2759; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000012972; Expressed in heart and 15 other tissues.
DR ExpressionAtlas; P41316; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl.
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_0000125912"
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"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8427639"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8427639"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8427639"
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:0000250"
SQ SEQUENCE 175 AA; 20107 MW; 636FBAB9D6CE90D3 CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QAPGPERTIP ITREEKPAVT AAPKK
