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CRYAB_BOVIN
ID   CRYAB_BOVIN             Reviewed;         175 AA.
AC   P02510; O46508; Q3SZQ9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Alpha-crystallin B chain;
DE   AltName: Full=Alpha(B)-crystallin;
GN   Name=CRYAB; Synonyms=CRYA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX   PubMed=4477528; DOI=10.1111/j.1432-1033.1974.tb03821.x;
RA   van der Ouderaa F.J., de Jong W.W., Hilderink A., Bloemendal H.;
RT   "The amino-acids sequence of the alphaB2 chain of bovine alpha-
RT   crystallin.";
RL   Eur. J. Biochem. 49:157-168(1974).
RN   [2]
RP   SEQUENCE REVISION TO 80.
RA   de Jong W.W.;
RL   Submitted (NOV-1991) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kelley P.B., Abraham E.C., Zhao H.R., Shroff N.P., Cherian M., Thomas J.J.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 69-175.
RX   PubMed=8114688; DOI=10.1007/bf01674432;
RA   Merck K.B., Horwitz J., Kersten M., Overkamp P., Gaestel M., Bloemendal H.,
RA   de Jong W.W.;
RT   "Comparison of the homologous carboxy-terminal domain and tail of alpha-
RT   crystallin and small heat shock protein.";
RL   Mol. Biol. Rep. 18:209-215(1993).
RN   [6]
RP   PHOSPHORYLATION AT SER-45 AND SER-59.
RX   PubMed=3579961; DOI=10.1016/0006-291x(87)91457-4;
RA   Chiesa R., Gawinowicz-Kolks M.A., Kleiman N.J., Spector A.;
RT   "The phosphorylation sites of the B2 chain of bovine alpha-crystallin.";
RL   Biochem. Biophys. Res. Commun. 144:1340-1347(1987).
RN   [7]
RP   PHOSPHORYLATION AT SER-19 AND SER-45.
RX   PubMed=2599111; DOI=10.1016/0014-5793(89)81491-7;
RA   Voorter C.E.M., de Haard-Hoekman W.A., Roersma E.S., Meyer H.E.,
RA   Bloemendal H., de Jong W.W.;
RT   "The in vivo phosphorylation sites of bovine alpha B-crystallin.";
RL   FEBS Lett. 259:50-52(1989).
RN   [8]
RP   SEQUENCE REVISION TO 80, AND PHOSPHORYLATION AT SER-19; SER-45 AND SER-59.
RX   PubMed=1304359; DOI=10.1002/pro.5560010506;
RA   Smith J.B., Sun Y., Smith D.L., Green B.;
RT   "Identification of the posttranslational modifications of bovine lens alpha
RT   B-crystallins by mass spectrometry.";
RL   Protein Sci. 1:601-608(1992).
RN   [9]
RP   GLYCATION AT LYS-90 AND LYS-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=7912928; DOI=10.1006/bbrc.1994.1866;
RA   Abraham E.C., Cherian M., Smith J.B.;
RT   "Site selectivity in the glycation of alpha A- and alpha B-crystallins by
RT   glucose.";
RL   Biochem. Biophys. Res. Commun. 201:1451-1456(1994).
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. In lens
CC       epithelial cells, stabilizes the ATP6V1A protein, preventing its
CC       degradation by the proteasome (By similarity).
CC       {ECO:0000250|UniProtKB:P23927}.
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. Interacts with HSPBAP1 and TTN/titin.
CC       Interacts with TMEM109. Interacts with DES; binds rapidly during early
CC       stages of DES filament assembly and a reduced binding seen in the later
CC       stages. Interacts with TMED10; the interaction mediates the
CC       translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC       Golgi intermediate compartment) and thereby secretion. Interacts with
CC       ATP6V1A and with MTOR, forming a ternary complex (By similarity).
CC       {ECO:0000250|UniProtKB:P02511, ECO:0000250|UniProtKB:P23927}.
CC   -!- INTERACTION:
CC       P02510; P02470: CRYAA; NbExp=4; IntAct=EBI-7824601, EBI-15796552;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus
CC       {ECO:0000250|UniProtKB:P02511}. Secreted
CC       {ECO:0000250|UniProtKB:P02511}. Lysosome
CC       {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during
CC       heat shock and resides in sub-nuclear structures known as SC35 speckles
CC       or nuclear splicing speckles. Localizes at the Z-bands and the
CC       intercalated disk in cardiomyocytes. Can be secreted; the secretion is
CC       dependent on protein unfolding and facilitated by the cargo receptor
CC       TMED10; it results in protein translocation from the cytoplasm into the
CC       ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed
CC       by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
CC   -!- TISSUE SPECIFICITY: Lens as well as other tissues.
CC   -!- PTM: It is not known whether either Lys-90, or Lys-92, or both are
CC       glycated.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; AF029793; AAB95323.2; -; mRNA.
DR   EMBL; BC102745; AAI02746.1; -; mRNA.
DR   PIR; A42446; CYBOAB.
DR   RefSeq; NP_776715.1; NM_174290.2.
DR   AlphaFoldDB; P02510; -.
DR   BMRB; P02510; -.
DR   SMR; P02510; -.
DR   BioGRID; 159035; 1.
DR   DIP; DIP-43761N; -.
DR   IntAct; P02510; 1.
DR   MINT; P02510; -.
DR   STRING; 9913.ENSBTAP00000000556; -.
DR   CarbonylDB; P02510; -.
DR   GlyConnect; 32; 1 O-Linked glycan (1 site).
DR   GlyConnect; 37; 1 O-Linked glycan.
DR   GlyConnect; 38; 1 O-Linked glycan.
DR   iPTMnet; P02510; -.
DR   UCD-2DPAGE; P02510; -.
DR   PaxDb; P02510; -.
DR   PeptideAtlas; P02510; -.
DR   Ensembl; ENSBTAT00000087415; ENSBTAP00000068917; ENSBTAG00000000434.
DR   GeneID; 281719; -.
DR   KEGG; bta:281719; -.
DR   CTD; 1410; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000434; -.
DR   VGNC; VGNC:27732; CRYAB.
DR   eggNOG; KOG3591; Eukaryota.
DR   GeneTree; ENSGT00940000157434; -.
DR   HOGENOM; CLU_095001_2_0_1; -.
DR   InParanoid; P02510; -.
DR   OrthoDB; 1187096at2759; -.
DR   TreeFam; TF105049; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000000434; Expressed in gluteus medius and 102 other tissues.
DR   ExpressionAtlas; P02510; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
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   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR   GO; GO:0032387; P:negative regulation of intracellular transport; ISS:AgBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IBA:GO_Central.
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   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; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Eye lens protein; Glycation; Glycoprotein; Lysosome; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Secreted; Zinc.
FT   CHAIN           1..175
FT                   /note="Alpha-crystallin B chain"
FT                   /id="PRO_0000125906"
FT   DOMAIN          56..164
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT   REGION          144..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         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   SITE            72
FT                   /note="Not glycated"
FT   SITE            82
FT                   /note="Not glycated"
FT   SITE            103
FT                   /note="Not glycated"
FT   SITE            121
FT                   /note="Not glycated"
FT   SITE            150
FT                   /note="Not glycated"
FT   SITE            166
FT                   /note="Not glycated"
FT   SITE            174
FT                   /note="Not glycated"
FT   SITE            175
FT                   /note="Not glycated"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:4477528"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:1304359,
FT                   ECO:0000269|PubMed:2599111"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:1304359,
FT                   ECO:0000269|PubMed:2599111, ECO:0000269|PubMed:3579961"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:1304359,
FT                   ECO:0000269|PubMed:3579961"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P02511"
FT   MOD_RES         166
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02511"
FT   CARBOHYD        90
FT                   /note="N-linked (Glc) (glycation) lysine"
FT                   /evidence="ECO:0000269|PubMed:7912928"
FT   CARBOHYD        92
FT                   /note="N-linked (Glc) (glycation) lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:7912928"
SQ   SEQUENCE   175 AA;  20037 MW;  E0CFBBA8D6DE82B2 CRC64;
     MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR PPSFLRAPSW
     IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
     KYRIPADVDP LAITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK
 
 
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