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CRYAB_SHEEP
ID   CRYAB_SHEEP             Reviewed;         175 AA.
AC   Q5ENY9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Alpha-crystallin B chain;
DE   AltName: Full=Alpha(B)-crystallin;
GN   Name=CRYAB;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Robertson L.J.G.;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 ATP6V1A and with MTOR, forming a ternary complex
CC       (By similarity). {ECO:0000250|UniProtKB:P02511,
CC       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. {ECO:0000250|UniProtKB:P02511}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; AY819023; AAW79079.1; -; mRNA.
DR   RefSeq; NP_001012475.1; NM_001012457.2.
DR   AlphaFoldDB; Q5ENY9; -.
DR   SMR; Q5ENY9; -.
DR   STRING; 9940.ENSOARP00000016300; -.
DR   GeneID; 497274; -.
DR   KEGG; oas:497274; -.
DR   CTD; 1410; -.
DR   eggNOG; KOG3591; Eukaryota.
DR   OrthoDB; 1187096at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
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   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Eye lens protein; Glycoprotein;
KW   Lysosome; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Secreted; Zinc.
FT   CHAIN           1..175
FT                   /note="Alpha-crystallin B chain"
FT                   /id="PRO_0000125914"
FT   DOMAIN          56..164
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          139..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: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:0000250|UniProtKB:P02510"
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;  20067 MW;  A18FBBB5A705E4B5 CRC64;
     MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR PPSFLRAPSW
     IDTGLSEVRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
     KYRIPADVDP LTITSSLSSD GVLTMNGPRK QASGPERTIP ITREEKPAVT AAPKK
 
 
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