ID   TIM14_BOVIN             Reviewed;         116 AA.
AC   Q3ZBN8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14;
DE   AltName: Full=DnaJ homolog subfamily C member 19;
GN   Name=DNAJC19; Synonyms=TIM14, TIMM14;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Rumen;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial co-chaperone which forms a complex with
CC       prohibitins to regulate cardiolipin remodeling (By similarity). May be
CC       a component of the PAM complex, a complex required for the
CC       translocation of transit peptide-containing proteins from the inner
CC       membrane into the mitochondrial matrix in an ATP-dependent manner. May
CC       act as a co-chaperone that stimulate the ATP-dependent activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q07914,
CC       ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- SUBUNIT: Interacts with PHB2; the interaction associates DNAJC19 with
CC       the prohibitin complex. Interacts with TIMM16/PAM16 (By similarity).
CC       May be a component of the PAM complex at least composed of a
CC       mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and
CC       TIMM14/DNAJC19 (By similarity). {ECO:0000250|UniProtKB:Q07914,
CC       ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9CQV7}; Single-pass membrane protein
CC       {ECO:0000255}; Matrix side {ECO:0000250|UniProtKB:Q9CQV7}.
CC   -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR   EMBL; BC103193; AAI03194.1; -; mRNA.
DR   RefSeq; NP_001029630.1; NM_001034458.1.
DR   AlphaFoldDB; Q3ZBN8; -.
DR   SMR; Q3ZBN8; -.
DR   STRING; 9913.ENSBTAP00000032039; -.
DR   PaxDb; Q3ZBN8; -.
DR   PRIDE; Q3ZBN8; -.
DR   Ensembl; ENSBTAT00000032097; ENSBTAP00000032039; ENSBTAG00000023513.
DR   GeneID; 513918; -.
DR   KEGG; bta:513918; -.
DR   CTD; 131118; -.
DR   VEuPathDB; HostDB:ENSBTAG00000023513; -.
DR   eggNOG; KOG0723; Eukaryota.
DR   GeneTree; ENSGT00940000154384; -.
DR   InParanoid; Q3ZBN8; -.
DR   OMA; GFQQTMT; -.
DR   OrthoDB; 1600166at2759; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000023513; Expressed in tongue muscle and 105 other tissues.
DR   GO; GO:0098800; C:inner mitochondrial membrane protein complex; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0099617; C:matrix side of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:1900208; P:regulation of cardiolipin metabolic process; ISS:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DA6"
FT   CHAIN           2..116
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM14"
FT                   /id="PRO_0000071099"
FT   TOPO_DOM        2..3
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..116
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          62..116
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DA6"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DA6"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96DA6"
SQ   SEQUENCE   116 AA;  12499 MW;  E7EE78795690D895 CRC64;
     MASTVVAVGL TIAAAGFAGR YALQAMKHME PQVKQVFQSL PKTAFSGGYY RGGFEPKMTK
     REAALILGVS PTANKAKIRD AHRRIMLLNH PDKGGSPYIA AKINEAKDLL EGQAKK