CRYAA_RHEAM
ID CRYAA_RHEAM Reviewed; 173 AA.
AC P02505;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Alpha-crystallin A chain;
GN Name=CRYAA;
OS Rhea americana (Greater rhea) (Common rhea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Rheiformes; Rheidae; Rhea.
OX NCBI_TaxID=8797;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=6482951; DOI=10.1038/311257a0;
RA Stapel S.O., Leunissen J.A.M., Versteeg M., Wattel J., de Jong W.W.;
RT "Ratites as oldest offshoot of avian stem -- evidence from alpha-crystallin
RT A sequences.";
RL Nature 311:257-259(1984).
RN [2]
RP GLYCOSYLATION AT SER-162, AND STRUCTURE OF CARBOHYDRATE.
RX PubMed=1730617; DOI=10.1016/s0021-9258(18)48530-4;
RA Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A.,
RA Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.;
RT "Vertebrate lens alpha-crystallins are modified by O-linked N-
RT acetylglucosamine.";
RL J. Biol. Chem. 267:555-563(1992).
CC -!- FUNCTION: Contributes to the transparency and refractive index of the
CC lens. May act as a chaperone, preventing aggregation of various
CC proteins under a wide range of stress conditions.
CC {ECO:0000250|UniProtKB:P02489}.
CC -!- SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB subunits
CC (By similarity). Inter-subunit bridging via zinc ions enhances
CC stability, which is crucial as there is no protein turn over in the
CC lens. Can also form homodimers and homotetramers (dimers of dimers)
CC which serve as the building blocks of homooligomers (By similarity).
CC Within homooligomers, the zinc-binding motif is created from residues
CC of 3 different molecules. His-100 and Glu-102 from one molecule are
CC ligands of the zinc ion, and His-107 and His-154 residues from
CC additional molecules complete the site with tetrahedral coordination
CC geometry (By similarity). {ECO:0000250|UniProtKB:P02470,
CC 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. {ECO:0000250|UniProtKB:P02489}.
CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains.
CC {ECO:0000269|PubMed:1730617}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A02908; CYEHAA.
DR AlphaFoldDB; P02505; -.
DR SMR; P02505; -.
DR GlyConnect; 30; 1 O-Linked glycan.
DR iPTMnet; P02505; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 PIRSF; PIRSF036514; Sm_HSP_B1; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Eye lens protein;
KW Glycoprotein; Metal-binding; Nucleus; Zinc.
FT CHAIN 1..173
FT /note="Alpha-crystallin A chain"
FT /id="PRO_0000125896"
FT DOMAIN 52..162
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 142..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02470"
FT BINDING 154
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:0000269|PubMed:6482951"
FT CARBOHYD 162
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:1730617"
SQ SEQUENCE 173 AA; 19832 MW; 33399BA6896DFC6C CRC64;
MDITIQHPWF KRALGPLIPS RLFDQFFGEG LLEYDLLPLF SSTISPYYRQ SLFRSVLESG
ISEVRSDREK FTIMLDVKHF SPEDLSVKII DDFVEIHGKH SERQDDHGYI SREFHRRYRL
PSNVDQSAIT CSLSSDGMLT FSGPKVQANM DPSHSERPIP VSREEKPTSA PSS
