CRYAA_TRIIN
ID CRYAA_TRIIN Reviewed; 161 AA.
AC P02500;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alpha-crystallin A chain;
DE Flags: Fragments;
GN Name=CRYAA;
OS Trichechus inunguis (Amazon manatee) (Brazilian manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=9777;
RN [1]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7254349; DOI=10.1038/292538a0;
RA de Jong W.W., Zweers A., Goodman M.;
RT "Relationship of aardvark to elephants, hyraxes and sea cows from alpha-
RT crystallin sequences.";
RL Nature 292:538-540(1981).
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 AlphaFoldDB; P02500; -.
DR SMR; P02500; -.
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; IPR003090; Alpha-crystallin_N.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR PANTHER; PTHR45640:SF14; PTHR45640:SF14; 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 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_0000125888"
FT DOMAIN 41..150
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 1..53
FT /note="Required for complex formation with BFSP1 and BFSP2"
FT /evidence="ECO:0000250|UniProtKB:P02489"
FT REGION 135..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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02474, ECO:0000305"
FT MOD_RES 6
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 40
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_CONS 39..40
FT /evidence="ECO:0000305"
FT NON_CONS 66..67
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18495 MW; BE1EE25D24542D23 CRC64;
MDVTIQHPWF KRALGPFYHN RLFDQFFGEG LFEYDLLPFQ SLFRTVLDSG ISEVRSDRDQ
FLILLDHFSP EDLTVKVLDD FVEIHGKHNE RQDDHGYISR EFHRRYRLPS NVDKSALSCS
LSADGMLTFC GPKVQSGMDA SHSERAIPVS REEKASSAPN S
