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Database: UniProt
Entry: A0A2R9CGA6_PANPA
LinkDB: A0A2R9CGA6_PANPA
Original site: A0A2R9CGA6_PANPA 
ID   A0A2R9CGA6_PANPA        Unreviewed;       175 AA.
AC   A0A2R9CGA6;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Alpha-crystallin B chain {ECO:0000256|ARBA:ARBA00018516};
DE   AltName: Full=Alpha(B)-crystallin {ECO:0000256|ARBA:ARBA00030175};
GN   Name=CRYAB {ECO:0000313|Ensembl:ENSPPAP00000040063.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000040063.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000040063.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000040063.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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.
CC       {ECO:0000256|PIRNR:PIRNR036514}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000256|PIRNR:PIRNR036514, ECO:0000256|PROSITE-ProRule:PRU00285,
CC       ECO:0000256|RuleBase:RU003616}.
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DR   EMBL; AJFE02014386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003805507.1; XM_003805459.3.
DR   RefSeq; XP_003805508.1; XM_003805460.3.
DR   RefSeq; XP_008969591.1; XM_008971343.2.
DR   AlphaFoldDB; A0A2R9CGA6; -.
DR   SMR; A0A2R9CGA6; -.
DR   STRING; 9597.ENSPPAP00000040063; -.
DR   Ensembl; ENSPPAT00000062976.1; ENSPPAP00000040063.1; ENSPPAG00000042685.1.
DR   GeneID; 100972736; -.
DR   KEGG; pps:100972736; -.
DR   CTD; 1410; -.
DR   GeneTree; ENSGT00940000157434; -.
DR   OMA; FRDWWED; -.
DR   OrthoDB; 3014506at2759; -.
DR   Proteomes; UP000240080; Chromosome 11.
DR   Bgee; ENSPPAG00000042685; Expressed in heart and 6 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR   GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR   GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0032387; P:negative regulation of intracellular transport; IEA:Ensembl.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl.
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:SF5; ALPHA-CRYSTALLIN B CHAIN; 1.
DR   PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 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; HSP20-like chaperones; 1.
DR   PROSITE; PS01031; SHSP; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|PIRNR:PIRNR036514};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Eye lens protein {ECO:0000256|PIRNR:PIRNR036514};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036514-1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   Zinc {ECO:0000256|PIRSR:PIRSR036514-1}.
FT   DOMAIN          56..164
FT                   /note="SHSP"
FT                   /evidence="ECO:0000259|PROSITE:PS01031"
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         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036514-1"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036514-1"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036514-1"
SQ   SEQUENCE   175 AA;  20145 MW;  AE08BEC36015E81B CRC64;
     MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW
     FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
     KYRVPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK
//
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