TIM14_YEAST
ID TIM14_YEAST Reviewed; 168 AA.
AC Q07914; D6VY10;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14;
DE AltName: Full=Presequence translocated-associated motor subunit PAM18;
GN Name=PAM18; Synonyms=TIM14; OrderedLocusNames=YLR008C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, IDENTIFICATION IN THE PAM
RP COMPLEX, INTERACTION WITH SSC1 AND TIM17, AND MUTAGENESIS OF HIS-141.
RX PubMed=14517234; DOI=10.1093/emboj/cdg485;
RA Mokranjac D., Sichting M., Neupert W., Hell K.;
RT "Tim14, a novel key component of the import motor of the TIM23 protein
RT translocase of mitochondria.";
RL EMBO J. 22:4945-4956(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PAM COMPLEX,
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=14638855; DOI=10.1083/jcb.200308004;
RA Truscott K.N., Voos W., Frazier A.E., Lind M., Li Y., Geissler A.,
RA Dudek J., Mueller H., Sickmann A., Meyer H.E., Meisinger C., Guiard B.,
RA Rehling P., Pfanner N.;
RT "A J-protein is an essential subunit of the presequence translocase-
RT associated protein import motor of mitochondria.";
RL J. Cell Biol. 163:707-713(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF
RP 141-HIS--ASP-143 AND HIS-141.
RX PubMed=14605210; DOI=10.1073/pnas.1936150100;
RA D'Silva P.D., Schilke B., Walter W., Andrew A., Craig E.A.;
RT "J protein cochaperone of the mitochondrial inner membrane required for
RT protein import into the mitochondrial matrix.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13839-13844(2003).
RN [7]
RP INTERACTION WITH PAM16.
RX PubMed=15218029; DOI=10.1074/jbc.m404319200;
RA Li Y., Dudek J., Guiard B., Pfanner N., Rehling P., Voos W.;
RT "The presequence translocase-associated protein import motor of
RT mitochondria. Pam16 functions in an antagonistic manner to Pam18.";
RL J. Biol. Chem. 279:38047-38054(2004).
RN [8]
RP INTERACTION WITH PAM16.
RX PubMed=14981507; DOI=10.1038/nsmb735;
RA Frazier A.E., Dudek J., Guiard B., Voos W., Li Y., Lind M., Meisinger C.,
RA Geissler A., Sickmann A., Meyer H.E., Bilanchone V., Cumsky M.G.,
RA Truscott K.N., Pfanner N., Rehling P.;
RT "Pam16 has an essential role in the mitochondrial protein import motor.";
RL Nat. Struct. Mol. Biol. 11:226-233(2004).
RN [9]
RP IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; TIM44; SSC1 AND MGE1.
RX PubMed=16107694; DOI=10.1128/mcb.25.17.7449-7458.2005;
RA van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A.,
RA Meyer H.E., Guiard B., Meisinger C., Pfanner N., Rehling P.;
RT "Pam17 is required for architecture and translocation activity of the
RT mitochondrial protein import motor.";
RL Mol. Cell. Biol. 25:7449-7458(2005).
RN [10]
RP SUBUNIT, INTERACTION WITH PAM16, DOMAIN, AND MUTAGENESIS OF PRO-142;
RP ASP-143; LYS-144 AND LEU-150.
RX PubMed=16105940; DOI=10.1073/pnas.0505969102;
RA D'Silva P.R., Schilke B., Walter W., Craig E.A.;
RT "Role of Pam16's degenerate J domain in protein import across the
RT mitochondrial inner membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12419-12424(2005).
CC -!- FUNCTION: Essential component of the PAM complex, a complex required
CC for the translocation of transit peptide-containing proteins from the
CC inner membrane into the mitochondrial matrix in an ATP-dependent
CC manner. In the complex, it is required to stimulate activity of mtHSP70
CC (SSC1). {ECO:0000269|PubMed:14517234, ECO:0000269|PubMed:14605210,
CC ECO:0000269|PubMed:14638855}.
CC -!- SUBUNIT: Homodimer and heterodimer with PAM16/TIM16. Homodimerization
CC may not be relevant in vivo, while heterodimerization is essential for
CC activity regulation of mtHSP70. Component of the PAM complex, at least
CC composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18/TIM14.
CC Interacts directly with mtHsp70. Interacts directly with TIM17 subunit
CC of the TIM23 complex. {ECO:0000269|PubMed:14517234,
CC ECO:0000269|PubMed:14638855, ECO:0000269|PubMed:14981507,
CC ECO:0000269|PubMed:15218029, ECO:0000269|PubMed:16105940,
CC ECO:0000269|PubMed:16107694}.
CC -!- INTERACTION:
CC Q07914; P42949: PAM16; NbExp=5; IntAct=EBI-31963, EBI-26019;
CC Q07914; P39515: TIM17; NbExp=3; IntAct=EBI-31963, EBI-9127;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14517234, ECO:0000269|PubMed:14605210,
CC ECO:0000269|PubMed:14638855}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14517234, ECO:0000269|PubMed:14605210,
CC ECO:0000269|PubMed:14638855}.
CC -!- DOMAIN: The J domain is essential for co-chaperone activity and
CC mediates the heterodimerization with the J-like domain of PAM16.
CC {ECO:0000269|PubMed:16105940}.
CC -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR EMBL; Z73180; CAA97530.1; -; Genomic_DNA.
DR EMBL; AY558196; AAS56522.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09326.1; -; Genomic_DNA.
DR PIR; S64830; S64830.
DR RefSeq; NP_013108.1; NM_001181895.1.
DR PDB; 2GUZ; X-ray; 2.00 A; A/C/E/G/I/K/M/O=99-168.
DR PDBsum; 2GUZ; -.
DR AlphaFoldDB; Q07914; -.
DR SMR; Q07914; -.
DR BioGRID; 31281; 206.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR DIP; DIP-2125N; -.
DR IntAct; Q07914; 24.
DR MINT; Q07914; -.
DR STRING; 4932.YLR008C; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR MaxQB; Q07914; -.
DR PaxDb; Q07914; -.
DR PRIDE; Q07914; -.
DR EnsemblFungi; YLR008C_mRNA; YLR008C; YLR008C.
DR GeneID; 850694; -.
DR KEGG; sce:YLR008C; -.
DR SGD; S000003998; PAM18.
DR VEuPathDB; FungiDB:YLR008C; -.
DR eggNOG; KOG0723; Eukaryota.
DR GeneTree; ENSGT00940000171836; -.
DR HOGENOM; CLU_017633_13_0_1; -.
DR InParanoid; Q07914; -.
DR OMA; EGSAEWY; -.
DR BioCyc; YEAST:G3O-32169-MON; -.
DR EvolutionaryTrace; Q07914; -.
DR PRO; PR:Q07914; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07914; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..168
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM14"
FT /id="PRO_0000071118"
FT TOPO_DOM 1..65
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..168
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 112..168
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 141..143
FT /note="HPD->AAA: Induces lethality."
FT /evidence="ECO:0000269|PubMed:14605210"
FT MUTAGEN 141
FT /note="H->Q: Induces lethality."
FT /evidence="ECO:0000269|PubMed:14517234,
FT ECO:0000269|PubMed:14605210"
FT MUTAGEN 142
FT /note="P->A: Induces a strong reduction in ability to
FT stimulate mtHSP70 activity but does not affect import of
FT proteins into mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:16105940"
FT MUTAGEN 143
FT /note="D->N: Induces lethality."
FT /evidence="ECO:0000269|PubMed:16105940"
FT MUTAGEN 144
FT /note="K->Q: Induces a strong reduction in ability to
FT stimulate mtHSP70 activity but does not affect import of
FT proteins into mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:16105940"
FT MUTAGEN 150
FT /note="L->W: Temperature-sensitive mutant that impairs
FT heterodimerization with PAM16 and import of proteins into
FT mitochondrial matrix when incubated at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16105940"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:2GUZ"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2GUZ"
FT HELIX 126..140
FT /evidence="ECO:0007829|PDB:2GUZ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2GUZ"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:2GUZ"
SQ SEQUENCE 168 AA; 17910 MW; 9CBF71CA50A0F341 CRC64;
MSSQSNTGNS IEAPQLPIPG QTNGSANVTV DGAGVNVGIQ NGSQGQKTGM DLYFDQALNY
MGEHPVITGF GAFLTLYFTA GAYKSISKGL NGGKSTTAFL KGGFDPKMNS KEALQILNLT
ENTLTKKKLK EVHRKIMLAN HPDKGGSPFL ATKINEAKDF LEKRGISK
