ID W7TPN2_9STRA Unreviewed; 145 AA.
AC W7TPN2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN ORFNames=Naga_100024g23 {ECO:0000313|EMBL:EWM29085.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM29085.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM29085.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM29085.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
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. {ECO:0000256|PIRNR:PIRNR016477}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000256|PIRNR:PIRNR016477}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|PIRNR:PIRNR016477}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWM29085.1}.
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DR EMBL; AZIL01000178; EWM29085.1; -; Genomic_DNA.
DR AlphaFoldDB; W7TPN2; -.
DR EnsemblProtists; EWM29085; EWM29085; Naga_100024g23.
DR OrthoDB; 5476468at2759; -.
DR Proteomes; UP000019335; Chromosome 3.
DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR016661; PFDN4.
DR PANTHER; PTHR21100; PREFOLDIN SUBUNIT 4; 1.
DR PANTHER; PTHR21100:SF9; PREFOLDIN SUBUNIT 4; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|PIRNR:PIRNR016477};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335}.
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 145 AA; 16427 MW; 44B2BDEC11286BB3 CRC64;
MSTTGVMREV NPSQDKGKAK TPDEAPDVEV RKEDQEMINE FGRLNNQYLE LDEDLAYLKE
QLEKLDDAVT ELMVGVGGPV RLSLGEAFMD VSEDYATEHC ERKQEQLQAK VEELGREKGK
IATRQMELKK VLYGRFGSSI NLENS
//