TIM16_MOUSE
ID TIM16_MOUSE Reviewed; 125 AA.
AC Q9CQV1; Q6EIX1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM16 {ECO:0000305};
DE AltName: Full=Mitochondria-associated granulocyte macrophage CSF-signaling molecule;
DE AltName: Full=Presequence translocated-associated motor subunit PAM16;
GN Name=Pam16 {ECO:0000312|MGI:MGI:1913699}; Synonyms=Magmas, Tim16, Timm16;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=11750097; DOI=10.1016/s0301-472x(01)00749-4;
RA Jubinsky P.T., Messer A., Bender J., Morris R.E., Ciraolo G.M., Witte D.P.,
RA Hawley R.G., Short M.K.;
RT "Identification and characterization of Magmas, a novel mitochondria-
RT associated protein involved in granulocyte-macrophage colony-stimulating
RT factor signal transduction.";
RL Exp. Hematol. 29:1392-1402(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15984936;
RA Peng J., Huang C.-H., Short M.K., Jubinsky P.T.;
RT "Magmas gene structure and evolution.";
RL In Silico Biol. 5:251-263(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Cerebellum;
RA Hoshino J., Aruga J., Mikoshiba K.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Mammary gland;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC and Testis;
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DNAJC19 AND TIMM44.
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).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=24786642; DOI=10.1371/journal.pgen.1004311;
RA Mehawej C., Delahodde A., Legeai-Mallet L., Delague V., Kaci N.,
RA Desvignes J.P., Kibar Z., Capo-Chichi J.M., Chouery E., Munnich A.,
RA Cormier-Daire V., Megarbane A.;
RT "The impairment of MAGMAS function in human is responsible for a severe
RT skeletal dysplasia.";
RL PLoS Genet. 10:E1004311-E1004311(2014).
CC -!- FUNCTION: Regulates ATP-dependent protein translocation into the
CC mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin
CC ATPase activity. {ECO:0000250|UniProtKB:Q9Y3D7}.
CC -!- SUBUNIT: Probable 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). Interacts with DNAJC19. Directly
CC interacts with DNAJC15; this interaction counteracts DNAJC15-dependent
CC stimulation of HSPA9 ATPase activity (By similarity). Associates with
CC the TIM23 complex (Probable). {ECO:0000250|UniProtKB:Q9Y3D7,
CC ECO:0000305|PubMed:24856930}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9Y3D7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y3D7}; Matrix side
CC {ECO:0000250|UniProtKB:Q9Y3D7}.
CC -!- TISSUE SPECIFICITY: Expressed in trabecular bone and cartilage and by
CC differentiated chondrocytes localized in the hypertrophic zone and by
CC osteoblasts at early developmental stages.
CC {ECO:0000269|PubMed:24786642}.
CC -!- DOMAIN: The J-like region, although related to the J domain does not
CC have co-chaperone activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
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DR EMBL; AF349454; AAL57766.1; -; mRNA.
DR EMBL; AY320045; AAQ86806.1; -; Genomic_DNA.
DR EMBL; AB073618; BAB91135.1; -; mRNA.
DR EMBL; AK003227; BAB22656.1; -; mRNA.
DR EMBL; AK008380; BAB25635.1; -; mRNA.
DR EMBL; BC024346; AAH24346.1; -; mRNA.
DR EMBL; BC096419; AAH96419.1; -; mRNA.
DR CCDS; CCDS37241.1; -.
DR RefSeq; NP_079847.1; NM_025571.1.
DR AlphaFoldDB; Q9CQV1; -.
DR SMR; Q9CQV1; -.
DR STRING; 10090.ENSMUSP00000014445; -.
DR iPTMnet; Q9CQV1; -.
DR PhosphoSitePlus; Q9CQV1; -.
DR EPD; Q9CQV1; -.
DR jPOST; Q9CQV1; -.
DR MaxQB; Q9CQV1; -.
DR PaxDb; Q9CQV1; -.
DR PeptideAtlas; Q9CQV1; -.
DR PRIDE; Q9CQV1; -.
DR ProteomicsDB; 262784; -.
DR TopDownProteomics; Q9CQV1; -.
DR DNASU; 66449; -.
DR Ensembl; ENSMUST00000014445; ENSMUSP00000014445; ENSMUSG00000014301.
DR Ensembl; ENSMUST00000057649; ENSMUSP00000137140; ENSMUSG00000045886.
DR GeneID; 66449; -.
DR KEGG; mmu:66449; -.
DR UCSC; uc007xzx.1; mouse.
DR CTD; 51025; -.
DR MGI; MGI:1913699; Pam16.
DR VEuPathDB; HostDB:ENSMUSG00000014301; -.
DR VEuPathDB; HostDB:ENSMUSG00000045886; -.
DR eggNOG; KOG3442; Eukaryota.
DR GeneTree; ENSGT00390000012037; -.
DR HOGENOM; CLU_101461_3_0_1; -.
DR InParanoid; Q9CQV1; -.
DR OMA; RMFKIND; -.
DR OrthoDB; 1640138at2759; -.
DR PhylomeDB; Q9CQV1; -.
DR TreeFam; TF315134; -.
DR BioGRID-ORCS; 66449; 27 hits in 71 CRISPR screens.
DR PRO; PR:Q9CQV1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9CQV1; protein.
DR Bgee; ENSMUSG00000014301; Expressed in primary oocyte and 66 other tissues.
DR ExpressionAtlas; Q9CQV1; baseline and differential.
DR Genevisible; Q9CQV1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR GO; GO:0071897; P:DNA biosynthetic process; IMP:MGI.
DR GO; GO:1902511; P:negative regulation of apoptotic DNA fragmentation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0001503; P:ossification; ISS:UniProtKB.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; ISO:MGI.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR005341; Tim16.
DR PANTHER; PTHR12388; PTHR12388; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport.
FT CHAIN 1..125
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM16"
FT /id="PRO_0000214079"
FT REGION 58..110
FT /note="J-like"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 125 AA; 13785 MW; 54A71AB4EEA452ED CRC64;
MAKYLAQIIV MGVQVVGRAF ARALRQEFAA SQAAADARGR AGHQSAAASN LSGLSLQEAQ
QILNVSKLSP EEVQKNYEHL FKVNDKSVGG SFYLQSKVVR AKERLDEELR IQAQEDREKG
QKPKT
