CRYAB_PIG
ID CRYAB_PIG Reviewed; 175 AA.
AC Q7M2W6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=9514893; DOI=10.1006/bbrc.1998.8226;
RA Liao J.H., Hung C.C., Lee J.S., Wu S.H., Chiou S.H.;
RT "Characterization, cloning, and expression of porcine alpha B crystallin.";
RL Biochem. Biophys. Res. Commun. 244:131-137(1998).
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 -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR PIR; JC5971; JC5971.
DR RefSeq; XP_005667376.1; XM_005667319.2.
DR RefSeq; XP_005667377.1; XM_005667320.2.
DR AlphaFoldDB; Q7M2W6; -.
DR SMR; Q7M2W6; -.
DR STRING; 9823.ENSSSCP00000015948; -.
DR iPTMnet; Q7M2W6; -.
DR PaxDb; Q7M2W6; -.
DR PeptideAtlas; Q7M2W6; -.
DR PRIDE; Q7M2W6; -.
DR Ensembl; ENSSSCT00000059078; ENSSSCP00000035382; ENSSSCG00000036724.
DR Ensembl; ENSSSCT00025057887; ENSSSCP00025024495; ENSSSCG00025042507.
DR Ensembl; ENSSSCT00030099319; ENSSSCP00030045709; ENSSSCG00030070976.
DR Ensembl; ENSSSCT00035087364; ENSSSCP00035036474; ENSSSCG00035064861.
DR Ensembl; ENSSSCT00040083229; ENSSSCP00040036260; ENSSSCG00040060499.
DR Ensembl; ENSSSCT00050030881; ENSSSCP00050012877; ENSSSCG00050022877.
DR Ensembl; ENSSSCT00055027724; ENSSSCP00055022074; ENSSSCG00055014007.
DR Ensembl; ENSSSCT00060086556; ENSSSCP00060037435; ENSSSCG00060063075.
DR Ensembl; ENSSSCT00070016677; ENSSSCP00070013824; ENSSSCG00070008603.
DR GeneID; 100519789; -.
DR KEGG; ssc:100519789; -.
DR CTD; 1410; -.
DR VGNC; VGNC:87013; CRYAB.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000157434; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; Q7M2W6; -.
DR OrthoDB; 1187096at2759; -.
DR TreeFam; TF105049; -.
DR Reactome; R-SSC-3371571; HSF1-dependent transactivation.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Chromosome 9.
DR Bgee; ENSSSCG00000036724; Expressed in psoas major muscle and 45 other tissues.
DR ExpressionAtlas; Q7M2W6; baseline and differential.
DR Genevisible; Q7M2W6; SS.
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:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 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_0000252666"
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: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; 20129 MW; EE372A30D83E9752 CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYFR PPSFLRAPSW
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRR QASGPERTIP ITREEKPAVT AAPKK
