ID A0A452SLE8_URSAM Unreviewed; 154 AA.
AC A0A452SLE8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Prefoldin subunit 2 {ECO:0000313|Ensembl:ENSUAMP00000033473.1};
GN Name=PFDN2 {ECO:0000313|Ensembl:ENSUAMP00000033473.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000033473.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000033473.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452SLE8; -.
DR STRING; 9643.ENSUAMP00000033473; -.
DR Ensembl; ENSUAMT00000037283.1; ENSUAMP00000033473.1; ENSUAMG00000025499.1.
DR GeneTree; ENSGT00390000009272; -.
DR OMA; CFKMIGG; -.
DR OrthoDB; 178677at2759; -.
DR Proteomes; UP000291022; 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:UP000291022}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..121
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 154 AA; 16621 MW; 183D791CC0D4F599 CRC64;
MADSSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT
LKEVDEARKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGRELNEFRE
KHNIRLMGED EKPAAKENSE GAGAKSSSAG VLVS
//
