TIM14_MOUSE
ID TIM14_MOUSE Reviewed; 116 AA.
AC Q9CQV7; Q8R1N1; Q9D896;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14 {ECO:0000305};
DE AltName: Full=DnaJ homolog subfamily C member 19;
GN Name=Dnajc19 {ECO:0000312|MGI:MGI:1914963}; Synonyms=Tim14, Timm14;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Small intestine, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AFG3L2; PAM16 AND PHB2,
RP AND MUTAGENESIS OF HIS-90.
RX PubMed=24856930; DOI=10.1016/j.cmet.2014.04.016;
RA Richter-Dennerlein R., Korwitz A., Haag M., Tatsuta T., Dargazanli S.,
RA Baker M., Decker T., Lamkemeyer T., Rugarli E.I., Langer T.;
RT "DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms
RT a complex with prohibitins to regulate cardiolipin remodeling.";
RL Cell Metab. 20:158-171(2014).
CC -!- FUNCTION: Mitochondrial co-chaperone which forms a complex with
CC prohibitins to regulate cardiolipin remodeling (PubMed:24856930). May
CC be 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:0000269|PubMed:24856930}.
CC -!- SUBUNIT: Interacts with PHB2; the interaction associates DNAJC19 with
CC the prohibitin complex (PubMed:24856930). Interacts with TIMM16/PAM16
CC (PubMed:24856930). May be a component of the PAM complex at least
CC composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44,
CC TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity).
CC {ECO:0000250|UniProtKB:Q07914, ECO:0000269|PubMed:24856930}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:24856930}; Single-pass membrane protein
CC {ECO:0000255}; Matrix side {ECO:0000269|PubMed:24856930}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CQV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CQV7-2; Sequence=VSP_016390;
CC Name=3;
CC IsoId=Q9CQV7-3; Sequence=VSP_016391;
CC -!- SIMILARITY: Belongs to the TIM14 family. {ECO:0000305}.
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DR EMBL; AK007866; BAB25317.1; -; mRNA.
DR EMBL; AK008267; BAB25565.1; -; mRNA.
DR EMBL; AK010204; BAB26767.1; -; mRNA.
DR EMBL; AK012051; BAB27993.1; -; mRNA.
DR EMBL; BC024335; AAH24335.1; -; mRNA.
DR CCDS; CCDS38411.1; -. [Q9CQV7-2]
DR CCDS; CCDS38412.1; -. [Q9CQV7-1]
DR CCDS; CCDS71233.1; -. [Q9CQV7-3]
DR RefSeq; NP_001021382.1; NM_001026211.2.
DR RefSeq; NP_001273901.1; NM_001286972.1. [Q9CQV7-3]
DR RefSeq; NP_001273902.1; NM_001286973.1.
DR RefSeq; NP_080608.3; NM_026332.4. [Q9CQV7-1]
DR RefSeq; XP_003084767.1; XM_003084719.3.
DR AlphaFoldDB; Q9CQV7; -.
DR SMR; Q9CQV7; -.
DR STRING; 10090.ENSMUSP00000011029; -.
DR iPTMnet; Q9CQV7; -.
DR PhosphoSitePlus; Q9CQV7; -.
DR jPOST; Q9CQV7; -.
DR MaxQB; Q9CQV7; -.
DR PaxDb; Q9CQV7; -.
DR PRIDE; Q9CQV7; -.
DR ProteomicsDB; 260656; -. [Q9CQV7-1]
DR ProteomicsDB; 260657; -. [Q9CQV7-2]
DR ProteomicsDB; 260658; -. [Q9CQV7-3]
DR Antibodypedia; 33761; 175 antibodies from 27 providers.
DR DNASU; 67713; -.
DR Ensembl; ENSMUST00000108195; ENSMUSP00000103830; ENSMUSG00000027679. [Q9CQV7-1]
DR Ensembl; ENSMUST00000117223; ENSMUSP00000113484; ENSMUSG00000027679. [Q9CQV7-3]
DR GeneID; 67713; -.
DR KEGG; mmu:67713; -.
DR UCSC; uc008oxo.2; mouse. [Q9CQV7-1]
DR UCSC; uc008oxp.2; mouse. [Q9CQV7-3]
DR CTD; 131118; -.
DR MGI; MGI:1914963; Dnajc19.
DR VEuPathDB; HostDB:ENSMUSG00000027679; -.
DR eggNOG; KOG0723; Eukaryota.
DR GeneTree; ENSGT00940000154384; -.
DR HOGENOM; CLU_017633_13_3_1; -.
DR InParanoid; Q9CQV7; -.
DR OMA; GFQQTMT; -.
DR OrthoDB; 1600166at2759; -.
DR PhylomeDB; Q9CQV7; -.
DR BioGRID-ORCS; 67713; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dnajc19; mouse.
DR PRO; PR:Q9CQV7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CQV7; protein.
DR Bgee; ENSMUSG00000027679; Expressed in right kidney and 189 other tissues.
DR ExpressionAtlas; Q9CQV7; baseline and differential.
DR Genevisible; Q9CQV7; MM.
DR GO; GO:0098800; C:inner mitochondrial membrane protein complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR GO; GO:0048806; P:genitalia development; ISO:MGI.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:1900208; P:regulation of cardiolipin metabolic process; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; 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_0000071101"
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"
FT VAR_SEQ 95..116
FT /note="GSPYIAAKINEAKDLLEGQAKK -> PLVEEGLKPIPICRSCSSICRRSILS
FT CSTSYDQNKNPFTVCVCVHSSAHTGIHTPVKPCETTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016390"
FT VAR_SEQ 95..116
FT /note="GSPYIAAKINEAKDLLEGQAKK -> KQLLLLYWTVNGIANSWCYECLCVSS
FT FPVVDHIVVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016391"
FT MUTAGEN 90
FT /note="H->Q: Inhibits cell growth. No effect on interaction
FT with PHB2."
FT /evidence="ECO:0000269|PubMed:24856930"
SQ SEQUENCE 116 AA; 12437 MW; 51E4313DB4F6083E CRC64;
MASTVVAVGL TIAAAGFAGR YVLQAMKHVE PQVKQVFQSL PKSAFGGGYY RGGFEPKMTK
REAALILGVS PTANKGKIRD AHRRIMLLNH PDKGGSPYIA AKINEAKDLL EGQAKK
