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Database: UniProt
Entry: A0A182RJL6_ANOFN
LinkDB: A0A182RJL6_ANOFN
Original site: A0A182RJL6_ANOFN 
ID   A0A182RJL6_ANOFN        Unreviewed;       138 AA.
AC   A0A182RJL6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=Prefoldin subunit 4 {ECO:0000256|PIRNR:PIRNR016477};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN006434-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN006434-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN006434-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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|ARBA:ARBA00011695,
CC       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   AlphaFoldDB; A0A182RJL6; -.
DR   STRING; 62324.A0A182RJL6; -.
DR   EnsemblMetazoa; AFUN006434-RA; AFUN006434-PA; AFUN006434.
DR   VEuPathDB; VectorBase:AFUN006434; -.
DR   VEuPathDB; VectorBase:AFUN2_005643; -.
DR   OrthoDB; 5476468at2759; -.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
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}.
FT   COILED          32..116
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   138 AA;  16019 MW;  BDE2FB1046C86B68 CRC64;
     MSTKVETKSK GTFQPDSDVH ITFEDQMKIN KFANYNAKVE DLKEELRIKQ NELKNLEEAG
     DEIELLDDDV QIPFLMGDVF LSHDQAKTLE LLAEAKERKK KEINNIQQTN RDLQQKMGDL
     KGYLYGRFGS NIHLENDE
//
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