ID L5L028_PTEAL Unreviewed; 136 AA.
AC L5L028;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Prefoldin subunit 2 {ECO:0000313|EMBL:ELK16378.1};
GN ORFNames=PAL_GLEAN10017952 {ECO:0000313|EMBL:ELK16378.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16378.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030474; ELK16378.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L028; -.
DR STRING; 9402.L5L028; -.
DR eggNOG; KOG4098; Eukaryota.
DR InParanoid; L5L028; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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 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:UP000010552}.
FT REGION 106..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 106..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 136 AA; 15302 MW; D9A859FFBA026D3C CRC64;
MMEPSLRKVI AGFNRLRQEQ RGLASKAAEL EMELNEHSLV IDTLKEVDET RRCYRMVGGV
LVERTVKEVL PALENNKEQI QKIIETLTQQ LQAKGKELNE FREKHNIRLM GEDEKPAKEN
SEGAGAKASS AGVLVS
//
