ID G3TI48_LOXAF Unreviewed; 134 AA.
AC G3TI48;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
GN Name=PFDN4 {ECO:0000313|Ensembl:ENSLAFP00000014302.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000014302.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000014302.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014302.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000014302.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000014302.3};
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|PIRNR:PIRNR016477}.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits. {ECO:0000256|PIRNR:PIRNR016477}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045, ECO:0000256|PIRNR:PIRNR016477}.
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DR RefSeq; XP_003419949.1; XM_003419901.2.
DR AlphaFoldDB; G3TI48; -.
DR STRING; 9785.ENSLAFP00000014302; -.
DR Ensembl; ENSLAFT00000017062.3; ENSLAFP00000014302.3; ENSLAFG00000017064.3.
DR GeneID; 100663744; -.
DR KEGG; lav:100663744; -.
DR CTD; 5203; -.
DR eggNOG; KOG1760; Eukaryota.
DR GeneTree; ENSGT00390000006696; -.
DR HOGENOM; CLU_130032_0_1_1; -.
DR InParanoid; G3TI48; -.
DR OMA; NARMDEF; -.
DR OrthoDB; 5476468at2759; -.
DR TreeFam; TF106491; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0001540; F:amyloid-beta binding; 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:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR016661; PFDN4.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR21100; PREFOLDIN SUBUNIT 4; 1.
DR PANTHER; PTHR21100:SF9; PREFOLDIN SUBUNIT 4; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR016477};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT COILED 33..118
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 134 AA; 15300 MW; CEBB3F0499352CDD CRC64;
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI DVKKKQLQNL EDACDDIMLA
DDDCLMIPYQ VGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKIQLY
AKFGSNINLE ADES
//
