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CRYAA_ELERU
ID   CRYAA_ELERU             Reviewed;         161 AA.
AC   P82530;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Alpha-crystallin A chain;
DE   Flags: Fragment;
GN   Name=CRYAA;
OS   Elephantulus rufescens (East African long-eared elephant shrew) (Galegeeska
OS   rufescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Galegeeska.
OX   NCBI_TaxID=42151;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   de Jong W.W., Leunissen J.A.M., Wistow G.J.;
RT   "Eye lens crystallins and the phylogeny of placental orders: evidence for a
RT   macroscelid-paenungulate clade?";
RL   (In) Szalay F.S., Novacek M.J., McKenna M.C. (eds.);
RL   Mammal phylogeny: placentals, pp.5-12, Springer-Verlag, New York (1993).
CC   -!- FUNCTION: Contributes to the transparency and refractive index of the
CC       lens. In its oxidized form (absence of intramolecular disulfide bond),
CC       acts as a chaperone, preventing aggregation of various proteins under a
CC       wide range of stress conditions. Required for the correct formation of
CC       lens intermediate filaments as part of a complex composed of BFSP1,
CC       BFSP2 and CRYAA. {ECO:0000250|UniProtKB:P02489}.
CC   -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits.
CC       Inter-subunit bridging via zinc ions enhances stability, which is
CC       crucial as there is no protein turn over in the lens. Can also form
CC       homodimers and homotetramers (dimers of dimers) which serve as the
CC       building blocks of homooligomers (By similarity). Within homooligomers,
CC       the zinc-binding motif is created from residues of 3 different
CC       molecules. His-88 and Glu-90 from one molecule are ligands of the zinc
CC       ion, and His-95 and His-142 residues from additional molecules complete
CC       the site with tetrahedral coordination geometry (By similarity). Part
CC       of a complex required for lens intermediate filament formation composed
CC       of BFSP1, BFSP2 and CRYAA (By similarity).
CC       {ECO:0000250|UniProtKB:P02470, ECO:0000250|UniProtKB:P02489}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02489}. Nucleus
CC       {ECO:0000250|UniProtKB:P02489}. Note=Translocates to the nucleus during
CC       heat shock and resides in sub-nuclear structures known as SC35 speckles
CC       or nuclear splicing speckles. {ECO:0000250|UniProtKB:P02489}.
CC   -!- PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus.
CC       {ECO:0000250|UniProtKB:P02489}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR012274; Alpha-crystallin_A.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640; PTHR45640; 1.
DR   PANTHER; PTHR45640:SF14; PTHR45640:SF14; 1.
DR   Pfam; PF00011; HSP20; 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   Disulfide bond; Eye lens protein; Glycoprotein; Metal-binding; Methylation;
KW   Nucleus; Phosphoprotein; Zinc.
FT   CHAIN           <1..161
FT                   /note="Alpha-crystallin A chain"
FT                   /id="PRO_0000125856"
FT   DOMAIN          40..150
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          <1..51
FT                   /note="Required for complex formation with BFSP1 and BFSP2"
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   REGION          141..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   MOD_RES         38
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         87
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   MOD_RES         89
FT                   /note="Deamidated asparagine; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02470"
FT   MOD_RES         111
FT                   /note="Deamidated asparagine; partial"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         135
FT                   /note="Deamidated glutamine; partial"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        150
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..130
FT                   /evidence="ECO:0000250|UniProtKB:P02489"
FT   NON_TER         1
SQ   SEQUENCE   161 AA;  18049 MW;  6FBC446454C27578 CRC64;
     ALGPFYPSRX XXXXXXXXXX XXXXXXXXXX XXXXXXXQSL FRTVLDSGIS EVRSDRDQFL
     ILLDVKHFSP EDLTVKVLDD FVEIHGKHNE RQDDHGYISR EFHRRYRLPS NVDQSALSCS
     LSADGMLTFC GXXVQSGMDA SHSERAIPVS REEKPSSAPS S
 
 
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