ID   PFD5_MOUSE              Reviewed;         154 AA.
AC   Q9WU28; Q3UKS8; Q9JMJ8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Prefoldin subunit 5;
DE   AltName: Full=EIG-1;
DE   AltName: Full=Myc modulator 1;
DE   AltName: Full=c-Myc-binding protein Mm-1;
GN   Name=Pfdn5; Synonyms=Eig1, Mm1, Pfd5;
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 [MRNA].
RC   TISSUE=Brain;
RA   Inazu T., Myint Z., Noguchi T.;
RT   "Molecular cloning of murine MM-1 and its expression.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Oyamatsu T., Kotani S., Todokoro K.;
RT   "Eig1 gene.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
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=C57BL/6J; 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, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   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. 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92269.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF108357; AAD28373.1; -; mRNA.
DR   EMBL; AB011473; BAA92269.1; ALT_INIT; mRNA.
DR   EMBL; AK028206; BAC25814.1; -; mRNA.
DR   EMBL; AK145883; BAE26723.1; -; mRNA.
DR   EMBL; BC026920; AAH26920.1; -; mRNA.
DR   CCDS; CCDS37227.1; -.
DR   RefSeq; NP_081320.2; NM_027044.3.
DR   AlphaFoldDB; Q9WU28; -.
DR   SMR; Q9WU28; -.
DR   BioGRID; 208102; 28.
DR   STRING; 10090.ENSMUSP00000129178; -.
DR   iPTMnet; Q9WU28; -.
DR   PhosphoSitePlus; Q9WU28; -.
DR   EPD; Q9WU28; -.
DR   jPOST; Q9WU28; -.
DR   MaxQB; Q9WU28; -.
DR   PaxDb; 10090-ENSMUSP00000129178; -.
DR   PeptideAtlas; Q9WU28; -.
DR   ProteomicsDB; 301795; -.
DR   Pumba; Q9WU28; -.
DR   Antibodypedia; 1782; 291 antibodies from 28 providers.
DR   DNASU; 56612; -.
DR   Ensembl; ENSMUST00000166658.8; ENSMUSP00000129178.2; ENSMUSG00000001289.13.
DR   GeneID; 56612; -.
DR   KEGG; mmu:56612; -.
DR   UCSC; uc007xvh.1; mouse.
DR   AGR; MGI:1928753; -.
DR   CTD; 5204; -.
DR   MGI; MGI:1928753; Pfdn5.
DR   VEuPathDB; HostDB:ENSMUSG00000001289; -.
DR   eggNOG; KOG3048; Eukaryota.
DR   GeneTree; ENSGT00390000008783; -.
DR   HOGENOM; CLU_091867_0_1_1; -.
DR   InParanoid; Q9WU28; -.
DR   OMA; TGYYVEN; -.
DR   OrthoDB; 241387at2759; -.
DR   PhylomeDB; Q9WU28; -.
DR   TreeFam; TF106509; -.
DR   BioGRID-ORCS; 56612; 27 hits in 81 CRISPR screens.
DR   ChiTaRS; Pfdn5; mouse.
DR   PRO; PR:Q9WU28; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9WU28; Protein.
DR   Bgee; ENSMUSG00000001289; Expressed in floor plate of midbrain and 246 other cell types or tissues.
DR   ExpressionAtlas; Q9WU28; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016272; C:prefoldin complex; ISO:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR   GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISO:MGI.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0006457; P:protein folding; ISO:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:1990113; P:RNA polymerase I assembly; IBA:GO_Central.
DR   GO; GO:1990114; P:RNA polymerase II core complex assembly; IBA:GO_Central.
DR   GO; GO:1990115; P:RNA polymerase III assembly; IBA:GO_Central.
DR   CDD; cd00584; Prefoldin_alpha; 1.
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   NCBIfam; TIGR00293; prefoldin subunit alpha; 1.
DR   PANTHER; PTHR12674; PREFOLDIN SUBUNIT 5; 1.
DR   PANTHER; PTHR12674:SF2; PREFOLDIN SUBUNIT 5; 1.
DR   Pfam; PF02996; Prefoldin; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   UCD-2DPAGE; Q9WU28; -.
DR   Genevisible; Q9WU28; MM.
PE   1: Evidence at protein 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_0000153662"
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;  0DA1EC744548CB14 CRC64;
     MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK
     ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA
     LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TVKA
//