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PFD5_CAEEL
ID   PFD5_CAEEL              Reviewed;         152 AA.
AC   Q21993;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Probable prefoldin subunit 5;
GN   Name=pfd-5; ORFNames=R151.9;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=18062952; DOI=10.1016/j.ydbio.2007.10.022;
RA   Lundin V.F., Srayko M., Hyman A.A., Leroux M.R.;
RT   "Efficient chaperone-mediated tubulin biogenesis is essential for cell
RT   division and cell migration in C. elegans.";
RL   Dev. Biol. 313:320-334(2008).
CC   -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC       transfers target proteins to it. Binds to nascent polypeptide chain and
CC       promotes folding in an environment in which there are many competing
CC       pathways for nonnative proteins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC       {ECO:0000305}.
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DR   EMBL; FO081317; CCD70764.1; -; Genomic_DNA.
DR   EMBL; AF303258; AAG50216.1; -; mRNA.
DR   PIR; T16760; T16760.
DR   RefSeq; NP_498582.1; NM_066181.5.
DR   AlphaFoldDB; Q21993; -.
DR   SMR; Q21993; -.
DR   BioGRID; 41225; 13.
DR   DIP; DIP-25712N; -.
DR   IntAct; Q21993; 4.
DR   STRING; 6239.R151.9; -.
DR   EPD; Q21993; -.
DR   PaxDb; Q21993; -.
DR   PeptideAtlas; Q21993; -.
DR   EnsemblMetazoa; R151.9.1; R151.9.1; WBGene00020112.
DR   GeneID; 176013; -.
DR   KEGG; cel:CELE_R151.9; -.
DR   CTD; 176013; -.
DR   WormBase; R151.9; CE00827; WBGene00020112; pfd-5.
DR   eggNOG; KOG3048; Eukaryota.
DR   GeneTree; ENSGT00390000008783; -.
DR   HOGENOM; CLU_091867_0_1_1; -.
DR   InParanoid; Q21993; -.
DR   OMA; QAKFKAC; -.
DR   OrthoDB; 1449403at2759; -.
DR   PhylomeDB; Q21993; -.
DR   PRO; PR:Q21993; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00020112; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016272; C:prefoldin complex; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR011599; PFD_alpha_archaea.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR004127; Prefoldin_subunit_alpha.
DR   PANTHER; PTHR12674; PTHR12674; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   TIGRFAMs; TIGR00293; TIGR00293; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Reference proteome.
FT   CHAIN           1..152
FT                   /note="Probable prefoldin subunit 5"
FT                   /id="PRO_0000153664"
SQ   SEQUENCE   152 AA;  17152 MW;  9D2D9B6DC3BDF5A2 CRC64;
     MAEEPKGVPL SELSLQQLGE LQKNCEQELN FFQESFNALK GLLTRNEKSI SALDDVKIAT
     AGHTALIPLS ESLYIRAELS DPSKHLVEIG TGYFVELDRE KAKAIFDRKK EHITKQVETV
     EGILKEKRRT RAYISDAFQT KVQSQLATMN TQ
 
 
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