ID   DJB14_XENLA             Reviewed;         371 AA.
AC   Q7ZXQ8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DnaJ homolog subfamily B member 14;
GN   Name=dnajb14;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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}.
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DR   EMBL; BC044298; AAH44298.1; -; mRNA.
DR   RefSeq; NP_001080644.1; NM_001087175.1.
DR   AlphaFoldDB; Q7ZXQ8; -.
DR   SMR; Q7ZXQ8; -.
DR   DNASU; 380336; -.
DR   GeneID; 380336; -.
DR   KEGG; xla:380336; -.
DR   CTD; 380336; -.
DR   Xenbase; XB-GENE-952318; dnajb14.S.
DR   OMA; AYCRKPA; -.
DR   OrthoDB; 1173544at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 380336; Expressed in blastula and 19 other tissues.
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: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   InterPro; IPR019734; TPR_repeat.
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.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Endoplasmic reticulum; Membrane; Reference proteome; TPR repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..371
FT                   /note="DnaJ homolog subfamily B member 14"
FT                   /id="PRO_0000281481"
FT   TOPO_DOM        1..238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..371
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          8..41
FT                   /note="TPR"
FT   DOMAIN          102..166
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          48..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  42247 MW;  14DF2675EAF8EB4F CRC64;
     MESNRDEAER CVRIGKAAIE AGDKEKARRF FSKAERLYPS SEARVLLDAL EKNDTAGNGP
     QSEKMSKSTE QPKAEKDSSG DTGKGHTQDQ VDGVQRIKKC KTYYEVLGVS PDAGEEDLKK
     AYRKLALKFH PDKNHAPGAT EAFKKIGNAY AVLSNPEKRK QYDLTGSEDN VQNNHRNGGF
     DYHRGFEADI TPEDLFNMFF GGGFPSGSVH TFSNGRTRYS HHQHHHHSGH DREEERADGG
     FSMFIQLMPI IVLILVSLLS QLMVSNPPYS LYPRSGQTIK RVTENLQISY YVSKDFKSEY
     NGMLLQKLEK NIEEDYVANV RNNCWRERQQ KQDLLHAAKV YRDERLRMKA ESISMENCKE
     LNRLTSLFRG G