ID   PFD6_CANLF              Reviewed;         129 AA.
AC   Q5TJE6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Prefoldin subunit 6;
DE   AltName: Full=Protein Ke2;
GN   Name=PFDN6; Synonyms=KE2;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Doberman pinscher;
RX   PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA   Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA   Ollier W.E.R., Binns M.M.;
RT   "Genomic sequence of the class II region of the canine MHC: comparison with
RT   the MHC of other mammalian species.";
RL   Genomics 85:48-59(2005).
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:0000250|UniProtKB:O15212}.
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC       subunits (By similarity). Component of the PAQosome complex which is
CC       responsible for the biogenesis of several protein complexes and which
CC       consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI
CC       complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF,
CC       POLR2E and DNAAF10/WDR92 (By similarity).
CC       {ECO:0000250|UniProtKB:O15212, ECO:0000250|UniProtKB:P52553}.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC       {ECO:0000305}.
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DR   EMBL; AJ630366; CAI11442.1; -; Genomic_DNA.
DR   RefSeq; NP_001041554.1; NM_001048089.2.
DR   RefSeq; XP_013971975.1; XM_014116500.1.
DR   AlphaFoldDB; Q5TJE6; -.
DR   SMR; Q5TJE6; -.
DR   STRING; 9612.ENSCAFP00000001363; -.
DR   PaxDb; Q5TJE6; -.
DR   Ensembl; ENSCAFT00030024194; ENSCAFP00030021099; ENSCAFG00030013071.
DR   Ensembl; ENSCAFT00040039083; ENSCAFP00040034080; ENSCAFG00040021078.
DR   Ensembl; ENSCAFT00845037435; ENSCAFP00845029325; ENSCAFG00845021180.
DR   GeneID; 474872; -.
DR   GeneID; 610181; -.
DR   KEGG; cfa:474872; -.
DR   KEGG; cfa:610181; -.
DR   CTD; 10471; -.
DR   VEuPathDB; HostDB:ENSCAFG00845021180; -.
DR   eggNOG; KOG3478; Eukaryota.
DR   GeneTree; ENSGT00390000010512; -.
DR   HOGENOM; CLU_125172_0_1_1; -.
DR   InParanoid; Q5TJE6; -.
DR   OMA; VQTEFAQ; -.
DR   OrthoDB; 1559044at2759; -.
DR   TreeFam; TF315166; -.
DR   Proteomes; UP000002254; Chromosome 12.
DR   Bgee; ENSCAFG00000000956; Expressed in renal medulla and 49 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016272; C:prefoldin complex; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   Gene3D; 1.10.287.370; -; 1.
DR   InterPro; IPR002777; PFD_beta-like.
DR   InterPro; IPR009053; Prefoldin.
DR   Pfam; PF01920; Prefoldin_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chaperone; Isopeptide bond; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
FT   CHAIN           2..129
FT                   /note="Prefoldin subunit 6"
FT                   /id="PRO_0000124849"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
FT   MOD_RES         66
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O15212"
SQ   SEQUENCE   129 AA;  14573 MW;  8F138EA83512A312 CRC64;
     MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL
     GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA
     AKAGASGKA