PFD6_MOUSE
ID PFD6_MOUSE Reviewed; 127 AA.
AC Q03958;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Prefoldin subunit 6;
DE AltName: Full=Protein Ke2;
GN Name=Pfdn6; Synonyms=H2-Ke2, Pfd6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=1748305; DOI=10.1016/0378-1119(91)90339-d;
RA Ha H., Abe K., Artzt K.;
RT "Primary structure of the embryo-expressed gene KE2 from the mouse H-2K
RT region.";
RL Gene 107:345-346(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; M65255; AAA39368.1; -; mRNA.
DR EMBL; M65256; AAA39369.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69895.1; -; Genomic_DNA.
DR EMBL; AK076015; BAC36121.1; -; mRNA.
DR EMBL; BC022974; AAH22974.1; -; mRNA.
DR CCDS; CCDS28636.1; -.
DR PIR; I53651; I53651.
DR RefSeq; NP_001172111.1; NM_001185182.1.
DR RefSeq; NP_034515.1; NM_010385.2.
DR AlphaFoldDB; Q03958; -.
DR SMR; Q03958; -.
DR BioGRID; 200157; 12.
DR IntAct; Q03958; 2.
DR MINT; Q03958; -.
DR STRING; 10090.ENSMUSP00000025163; -.
DR iPTMnet; Q03958; -.
DR PhosphoSitePlus; Q03958; -.
DR EPD; Q03958; -.
DR jPOST; Q03958; -.
DR PaxDb; Q03958; -.
DR PeptideAtlas; Q03958; -.
DR PRIDE; Q03958; -.
DR ProteomicsDB; 287919; -.
DR TopDownProteomics; Q03958; -.
DR Antibodypedia; 29059; 126 antibodies from 24 providers.
DR DNASU; 14976; -.
DR Ensembl; ENSMUST00000025163; ENSMUSP00000025163; ENSMUSG00000024309.
DR Ensembl; ENSMUST00000174048; ENSMUSP00000133656; ENSMUSG00000024309.
DR Ensembl; ENSMUST00000179418; ENSMUSP00000137072; ENSMUSG00000024309.
DR GeneID; 14976; -.
DR KEGG; mmu:14976; -.
DR UCSC; uc008cah.1; mouse.
DR CTD; 10471; -.
DR MGI; MGI:95908; Pfdn6.
DR VEuPathDB; HostDB:ENSMUSG00000024309; -.
DR eggNOG; KOG3478; Eukaryota.
DR GeneTree; ENSGT00390000010512; -.
DR HOGENOM; CLU_125172_0_1_1; -.
DR InParanoid; Q03958; -.
DR OMA; VQTEFAQ; -.
DR OrthoDB; 1559044at2759; -.
DR PhylomeDB; Q03958; -.
DR TreeFam; TF315166; -.
DR BioGRID-ORCS; 14976; 19 hits in 71 CRISPR screens.
DR ChiTaRS; Pfdn6; mouse.
DR PRO; PR:Q03958; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q03958; protein.
DR Bgee; ENSMUSG00000024309; Expressed in floor plate of midbrain and 271 other tissues.
DR ExpressionAtlas; Q03958; baseline and differential.
DR Genevisible; Q03958; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016272; C:prefoldin complex; ISO:MGI.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:MGI.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:MGI.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
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..127
FT /note="Prefoldin subunit 6"
FT /id="PRO_0000124851"
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 127 AA; 14455 MW; 7B1EB0ADB312A9B6 CRC64;
MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL
GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA
AKAPGKA
