PFD5_PONAB
ID PFD5_PONAB Reviewed; 154 AA.
AC Q5RAY0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Prefoldin subunit 5;
GN Name=PFDN5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Represses the transcriptional activity
CC of MYC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; CR858881; CAH91080.1; -; mRNA.
DR RefSeq; NP_001125627.1; NM_001132155.1.
DR AlphaFoldDB; Q5RAY0; -.
DR SMR; Q5RAY0; -.
DR STRING; 9601.ENSPPYP00000005219; -.
DR GeneID; 100172545; -.
DR KEGG; pon:100172545; -.
DR CTD; 5204; -.
DR eggNOG; KOG3048; Eukaryota.
DR InParanoid; Q5RAY0; -.
DR OrthoDB; 1449403at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.10.287.370; -; 1.
DR HAMAP; MF_00308; PfdA; 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 Acetylation; Chaperone; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99471"
FT CHAIN 2..154
FT /note="Prefoldin subunit 5"
FT /id="PRO_0000153663"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99471"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99471"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99471"
SQ SEQUENCE 154 AA; 17356 MW; 0DA1F3644548C8DB CRC64;
MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
LQEKHAMKQA VMEMMSQKIR QLTALGAAQA TAKA