ID   DJB14_PONAB             Reviewed;         379 AA.
AC   Q5R6H3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=DnaJ homolog subfamily B member 14;
GN   Name=DNAJB14;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC       protein folding and trafficking, prevent aggregation of client
CC       proteins, and promote unfolded proteins to endoplasmic reticulum-
CC       associated degradation (ERAD) pathway. Acts by determining
CC       HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act
CC       independently of HSPA8/Hsc70: together with DNAJB12, acts as a
CC       chaperone that promotes maturation of potassium channels KCND2 and
CC       KCNH2 by stabilizing nascent channel subunits and assembling them into
CC       tetramers. While stabilization of nascent channel proteins is dependent
CC       on HSPA8/Hsc70, the process of oligomerization of channel subunits is
CC       independent of HSPA8/Hsc70. When overexpressed, forms membranous
CC       structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus;
CC       the role of these structures, named DJANGOs, is still unclear.
CC       {ECO:0000250|UniProtKB:Q8TBM8}.
CC   -!- SUBUNIT: Interacts (via J domain) with HSPA8/Hsc70. Forms a
CC       multiprotein complex, at least composed of DNAJB12, DNAJB14,
CC       HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is
CC       direct. {ECO:0000250|UniProtKB:Q8TBM8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein
CC       {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-
CC       pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic
CC       reticulum membrane. When overexpressed, forms membranous structures in
CC       the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR860516; CAH92643.1; -; mRNA.
DR   RefSeq; NP_001126547.1; NM_001133075.1.
DR   AlphaFoldDB; Q5R6H3; -.
DR   SMR; Q5R6H3; -.
DR   STRING; 9601.ENSPPYP00000016700; -.
DR   GeneID; 100173537; -.
DR   KEGG; pon:100173537; -.
DR   CTD; 79982; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q5R6H3; -.
DR   OrthoDB; 1173544at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR015399; DUF1977_DnaJ-like.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF09320; DUF1977; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..379
FT                   /note="DnaJ homolog subfamily B member 14"
FT                   /id="PRO_0000281480"
FT   TOPO_DOM        1..244
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..379
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..172
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          55..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  42456 MW;  F91B66EFD7ECA623 CRC64;
     MEGNRDEAEK CVEIAREALN AGNREKAQRF LQKAEKLYPL PSARALLEII MKNGSTAGNS
     PHCRKPSGSG DQSKPNCTKD STSGSGEGGK GYTKDQVDGV LSINKCKNCY EVLGVTKDAG
     DEDLKKAYRK LALKFHPDKN HAPGATDAFK KIGNAYAVLS NPEKRKQYDL TGNEEQACNH
     QNNGRFNFHR GCEADITPED LFNIFFGGGF PSGSVHSFSN GRAGYSQQHQ HRHSGHEREE
     ERGDGGFSVF IQLMPIIVLI LVSLLSQLMV SNPPYSLYPR SGTGQTIKMQ TENLGVVYYV
     NKDFKNEYKG MLLQKVEKSV EEDYVTNIRN NCWKERQQKT DMQYAAKVYR DDRLRRKADA
     LSMDNCKELE RLTSLYKGG