ID   DJB14_XENTR             Reviewed;         375 AA.
AC   Q28I38;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=DnaJ homolog subfamily B member 14;
GN   Name=dnajb14; ORFNames=TEgg043m09.1 {ECO:0000303|Ref.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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 by stabilizing
CC       nascent channel subunits and assembling them into tetramers. While
CC       stabilization of nascent channel proteins is dependent on hspa8/Hsc70,
CC       the process of oligomerization of channel subunits is independent of
CC       hspa8/Hsc70. {ECO:0000250|UniProtKB:Q8TBM8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR760610; CAJ81323.1; -; mRNA.
DR   RefSeq; NP_001016588.1; NM_001016588.2.
DR   AlphaFoldDB; Q28I38; -.
DR   SMR; Q28I38; -.
DR   STRING; 8364.ENSXETP00000018545; -.
DR   PaxDb; Q28I38; -.
DR   GeneID; 549342; -.
DR   KEGG; xtr:549342; -.
DR   CTD; 79982; -.
DR   Xenbase; XB-GENE-952313; dnajb14.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_043579_3_0_1; -.
DR   InParanoid; Q28I38; -.
DR   OMA; AYCRKPA; -.
DR   OrthoDB; 1173544at2759; -.
DR   PhylomeDB; Q28I38; -.
DR   TreeFam; TF105145; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000011168; Expressed in 2-cell stage embryo and 12 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="DnaJ homolog subfamily B member 14"
FT                   /id="PRO_0000281482"
FT   TOPO_DOM        1..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..375
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          106..170
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          48..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  42383 MW;  9D057839CCDF95CE CRC64;
     MESNRDEAER CVRIAKAAIE AGDKEKAKRF LSKAERLYPS SEARALLQAF EKNDTAGNGP
     QSAKMAKGTE QPKAEKDSNA SASSDTGKGH TQDQLDGVQR IKKCKTYYEV LGVSTDAGEE
     DLKKAYRKLA LKFHPDKNHA PGATEAFKKI GNAYAVLSNP EKRKQYDLTG SEDQMQNNHR
     NGGFDYHRGF EADITPEDLF NMFFGGGFPS GSVHTFSNGR ARYSHHQHHH HSGHDREDER
     ADGGFSMFIQ LMPIIVLILV SLLSQFMVSN PPYSLYPRSG QATKRVTENL QIAYYVSKDF
     QSEYSGILLQ KLEKNIEEDY VANVRNNCWR ERQQRSDLMH AAKVYRDERL KVKAESISME
     NCKELNRLTS LFRGG