CRYAB_LITCT
ID CRYAB_LITCT Reviewed; 173 AA.
AC Q91312;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Alpha-crystallin B chain;
DE AltName: Full=Alpha(B)-crystallin;
GN Name=CRYAB;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=7488208; DOI=10.1006/bbrc.1995.2704;
RA Lu S.F., Pan F.M., Chiou S.H.;
RT "Sequence analysis of frog alpha B-crystallin cDNA: sequence homology and
RT evolutionary comparison of alpha A, alpha B and heat shock proteins.";
RL Biochem. Biophys. Res. Commun. 216:881-891(1995).
CC -!- FUNCTION: May contribute to the transparency and refractive index of
CC the lens.
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). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X87114; CAA60594.1; -; mRNA.
DR PIR; S54824; S54824.
DR AlphaFoldDB; Q91312; -.
DR SMR; Q91312; -.
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 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 PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Eye lens protein; Metal-binding; Zinc.
FT CHAIN 1..173
FT /note="Alpha-crystallin B chain"
FT /id="PRO_0000125920"
FT DOMAIN 54..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 109
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"
SQ SEQUENCE 173 AA; 20079 MW; 52A775FDA592ADB5 CRC64;
MDITIQHPWF RRQFYSFFGP NKMFEQCFGE HIQEADLFPS SVLSPFYFKY PFLRLPSWIE
SGLSEMRLEK DKFSINLDVK HFSPEELKVK VSGDFIEIHG KHEERQDEHG YVSRDFQRRY
KIPVDVDPLS ITSSLSPDGV LTVCGPRKQG DVPERSIPIT REEKAALGAA PKK
