ID G1P2M1_MYOLU Unreviewed; 128 AA.
AC G1P2M1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Prefoldin subunit 2 {ECO:0000313|Ensembl:ENSMLUP00000004115.2};
GN Name=PFDN2 {ECO:0000313|Ensembl:ENSMLUP00000004115.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000004115.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000004115.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000004115.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00024667}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045}.
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DR EMBL; AAPE02047223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02047229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P2M1; -.
DR STRING; 59463.ENSMLUP00000004115; -.
DR Ensembl; ENSMLUT00000004524.2; ENSMLUP00000004115.2; ENSMLUG00000004526.2.
DR eggNOG; KOG4098; Eukaryota.
DR GeneTree; ENSGT00390000009272; -.
DR HOGENOM; CLU_113004_0_0_1; -.
DR InParanoid; G1P2M1; -.
DR OMA; CFKMIGG; -.
DR TreeFam; TF313252; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016272; C:prefoldin complex; IEA:Ensembl.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IEA:Ensembl.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR027235; PFD2.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR13303; PREFOLDIN SUBUNIT 2; 1.
DR PANTHER; PTHR13303:SF0; PREFOLDIN SUBUNIT 2; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT REGION 98..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..96
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 98..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 128 AA; 14284 MW; 0618C5EB601CF5DD CRC64;
VIAGFNRLRQ EQRGLASKAA ELEMELNEHS LVIDTLKEVD ETRKCFRMVG GVLVERTVKE
VLPALENNKE QIQKIIETLT QQLQAKGKEL NEFREKHNIR LMGEDEKPAK ENSEGAGAKA
SSAGVLVS
//
