ID   TIM14_DICDI             Reviewed;         113 AA.
AC   Q54QN1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 97.
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; ORFNames=DDB_G0283735;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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; AAFI02000056; EAL65634.1; -; Genomic_DNA.
DR   RefSeq; XP_638992.1; XM_633900.1.
DR   AlphaFoldDB; Q54QN1; -.
DR   SMR; Q54QN1; -.
DR   STRING; 44689.DDB0237975; -.
DR   PaxDb; Q54QN1; -.
DR   EnsemblProtists; EAL65634; EAL65634; DDB_G0283735.
DR   GeneID; 8624238; -.
DR   KEGG; ddi:DDB_G0283735; -.
DR   dictyBase; DDB_G0283735; dnajc19.
DR   eggNOG; KOG0723; Eukaryota.
DR   HOGENOM; CLU_017633_13_3_1; -.
DR   InParanoid; Q54QN1; -.
DR   OMA; GFQQTMT; -.
DR   PhylomeDB; Q54QN1; -.
DR   PRO; PR:Q54QN1; -.
DR   Proteomes; UP000002195; Chromosome 4.
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   Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..113
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM14"
FT                   /id="PRO_0000331206"
FT   TOPO_DOM        1..4
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..113
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          59..113
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ   SEQUENCE   113 AA;  12436 MW;  FD2F901FD9A7CE1B CRC64;
     MATPIIVGAT IAGIAYSSRF LIRVIQRAKS KQLFEMVSTP GFTVETIEDG FENKMTPAEA
     ANILGLKEES TKEEIKIRHK LLMIKNHPDK GGSSYLATKI NEARNVLSSK NSN