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HSP12_CAEEL
ID   HSP12_CAEEL             Reviewed;         145 AA.
AC   P06582;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Heat shock protein hsp-16.2 {ECO:0000305};
GN   Name=hsp-16.2 {ECO:0000312|WormBase:Y46H3A.3a};
GN   Synonyms=hsp-16 {ECO:0000312|WormBase:Y46H3A.3a},
GN   hsp16-2 {ECO:0000312|WormBase:Y46H3A.3a};
GN   ORFNames=Y46H3A.3 {ECO:0000312|WormBase:Y46H3A.3a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3017958; DOI=10.1016/s0021-9258(18)67194-7;
RA   Jones D., Russnak R.H., Kay R.J., Candido E.P.M.;
RT   "Structure, expression, and evolution of a heat shock gene locus in
RT   Caenorhabditis elegans that is flanked by repetitive elements.";
RL   J. Biol. Chem. 261:12006-12015(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   INDUCTION.
RX   PubMed=29500338; DOI=10.1038/s41467-018-02934-5;
RA   De Magalhaes Filho C.D., Henriquez B., Seah N.E., Evans R.M.,
RA   Lapierre L.R., Dillin A.;
RT   "Visible light reduces C. elegans longevity.";
RL   Nat. Commun. 9:927-927(2018).
CC   -!- INDUCTION: Induced by white light exposure.
CC       {ECO:0000269|PubMed:29500338}.
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR   EMBL; M14334; AAA28071.1; -; Genomic_DNA.
DR   EMBL; BX284605; CCD70651.1; -; Genomic_DNA.
DR   PIR; B25199; B25199.
DR   RefSeq; NP_503507.1; NM_071106.7.
DR   AlphaFoldDB; P06582; -.
DR   SMR; P06582; -.
DR   BioGRID; 43724; 2.
DR   IntAct; P06582; 1.
DR   STRING; 6239.Y46H3A.3; -.
DR   BindingDB; P06582; -.
DR   ChEMBL; CHEMBL2146313; -.
DR   EPD; P06582; -.
DR   PaxDb; P06582; -.
DR   PeptideAtlas; P06582; -.
DR   EnsemblMetazoa; Y46H3A.3a.1; Y46H3A.3a.1; WBGene00002016.
DR   GeneID; 178659; -.
DR   KEGG; cel:CELE_Y46H3A.3; -.
DR   UCSC; Y46H3A.3; c. elegans.
DR   CTD; 178659; -.
DR   WormBase; Y46H3A.3a; CE22002; WBGene00002016; hsp-16.2.
DR   eggNOG; KOG3591; Eukaryota.
DR   InParanoid; P06582; -.
DR   OMA; NTEGHER; -.
DR   OrthoDB; 1187096at2759; -.
DR   PhylomeDB; P06582; -.
DR   Reactome; R-CEL-3371571; HSF1-dependent transactivation.
DR   PRO; PR:P06582; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00002016; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; P06582; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:WormBase.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR   Gene3D; 2.60.40.790; -; 1.
DR   InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR   InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   PANTHER; PTHR45640; PTHR45640; 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   2: Evidence at transcript level;
KW   Reference proteome; Stress response.
FT   CHAIN           1..145
FT                   /note="Heat shock protein hsp-16.2"
FT                   /id="PRO_0000125959"
FT   DOMAIN          32..137
FT                   /note="sHSP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
SQ   SEQUENCE   145 AA;  16242 MW;  8A73449F99161889 CRC64;
     MSLYHYFRPA QRSVFGDLMR DMALMERQFA PVCRISPSES SEIVNNDQKF AINLNVSQFK
     PEDLKINLDG RTLSIQGEQE LKTDHGYSKK SFSRVILLPE DVDVGAVASN LSEDGKLSIE
     APKKEAVQGR SIPIQQAIVE EKSAE
 
 
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