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Mitochondrial import inner membrane translocase subunit TIM16 (Mitochondria-associated granulocyte macrophage CSF-signaling molecule) (Presequence translocated-associated motor subunit PAM16)

 TIM16_MOUSE             Reviewed;         125 AA.
Q9CQV1; Q6EIX1;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 131.
RecName: Full=Mitochondrial import inner membrane translocase subunit TIM16;
AltName: Full=Mitochondria-associated granulocyte macrophage CSF-signaling molecule;
AltName: Full=Presequence translocated-associated motor subunit PAM16;
Name=Pam16; Synonyms=Magmas, Tim16, Timm16;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=11750097; DOI=10.1016/S0301-472X(01)00749-4;
Jubinsky P.T., Messer A., Bender J., Morris R.E., Ciraolo G.M.,
Witte D.P., Hawley R.G., Short M.K.;
"Identification and characterization of Magmas, a novel mitochondria-
associated protein involved in granulocyte-macrophage colony-
stimulating factor signal transduction.";
Exp. Hematol. 29:1392-1402(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15984936;
Peng J., Huang C.-H., Short M.K., Jubinsky P.T.;
"Magmas gene structure and evolution.";
In Silico Biol. 5:251-263(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR; TISSUE=Cerebellum;
Hoshino J., Aruga J., Mikoshiba K.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
TISSUE SPECIFICITY.
PubMed=24786642; DOI=10.1371/journal.pgen.1004311;
Mehawej C., Delahodde A., Legeai-Mallet L., Delague V., Kaci N.,
Desvignes J.P., Kibar Z., Capo-Chichi J.M., Chouery E., Munnich A.,
Cormier-Daire V., Megarbane A.;
"The impairment of MAGMAS function in human is responsible for a
severe skeletal dysplasia.";
PLoS Genet. 10:E1004311-E1004311(2014).
-!- FUNCTION: Regulates ATP-dependent protein translocation into the
mitochondrial matrix. Inhibits DNAJC19 stimulation of
HSPA9/Mortalin ATPase activity (By similarity). {ECO:0000250}.
-!- SUBUNIT: Probable component of the PAM complex at least composed
of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44,
TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity). Interacts with
DNAJC19. Directly interacts with DNAJC15; this interaction
counteracts DNAJC15-dependent stimulation of HSPA9 ATPase activity
(By similarity). Associates with the TIM23 complex (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Matrix side
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in trabecular bone and cartilage and
by differentiated chondrocytes localized in the hypertrophic zone
and by osteoblasts at early developmental stages.
{ECO:0000269|PubMed:24786642}.
-!- DOMAIN: The J-like region, although related to the J domain does
not have co-chaperone activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
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EMBL; AF349454; AAL57766.1; -; mRNA.
EMBL; AY320045; AAQ86806.1; -; Genomic_DNA.
EMBL; AB073618; BAB91135.1; -; mRNA.
EMBL; AK003227; BAB22656.1; -; mRNA.
EMBL; AK008380; BAB25635.1; -; mRNA.
EMBL; BC024346; AAH24346.1; -; mRNA.
EMBL; BC096419; AAH96419.1; -; mRNA.
CCDS; CCDS37241.1; -.
RefSeq; NP_079847.1; NM_025571.1.
UniGene; Mm.354760; -.
ProteinModelPortal; Q9CQV1; -.
SMR; Q9CQV1; -.
IntAct; Q9CQV1; 2.
MINT; Q9CQV1; -.
STRING; 10090.ENSMUSP00000137140; -.
iPTMnet; Q9CQV1; -.
PhosphoSitePlus; Q9CQV1; -.
EPD; Q9CQV1; -.
MaxQB; Q9CQV1; -.
PaxDb; Q9CQV1; -.
PeptideAtlas; Q9CQV1; -.
PRIDE; Q9CQV1; -.
TopDownProteomics; Q9CQV1; -.
Ensembl; ENSMUST00000014445; ENSMUSP00000014445; ENSMUSG00000014301.
Ensembl; ENSMUST00000057649; ENSMUSP00000137140; ENSMUSG00000045886.
GeneID; 66449; -.
KEGG; mmu:66449; -.
UCSC; uc007xzx.1; mouse.
CTD; 51025; -.
MGI; MGI:1913699; Pam16.
eggNOG; KOG3442; Eukaryota.
eggNOG; ENOG411286G; LUCA.
GeneTree; ENSGT00390000012037; -.
HOGENOM; HOG000180095; -.
HOVERGEN; HBG094040; -.
InParanoid; Q9CQV1; -.
KO; K17805; -.
OMA; YLMEAND; -.
OrthoDB; EOG091G0ZKM; -.
PhylomeDB; Q9CQV1; -.
TreeFam; TF315134; -.
PRO; PR:Q9CQV1; -.
Proteomes; UP000000589; Chromosome 10.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000014301; -.
ExpressionAtlas; Q9CQV1; baseline and differential.
Genevisible; Q9CQV1; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0005744; C:mitochondrial inner membrane presequence translocase complex; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0001405; C:presequence translocase-associated import motor; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0071897; P:DNA biosynthetic process; IMP:MGI.
GO; GO:1902511; P:negative regulation of apoptotic DNA fragmentation; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0032780; P:negative regulation of ATPase activity; ISO:MGI.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0001503; P:ossification; ISS:UniProtKB.
GO; GO:0030150; P:protein import into mitochondrial matrix; ISO:MGI.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR005341; Tim16.
PANTHER; PTHR12388; PTHR12388; 1.
1: Evidence at protein level;
Complete proteome; Membrane; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Protein transport;
Reference proteome; Translocation; Transport.
CHAIN 1 125 Mitochondrial import inner membrane
translocase subunit TIM16.
/FTId=PRO_0000214079.
REGION 58 110 J-like.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
SEQUENCE 125 AA; 13785 MW; 54A71AB4EEA452ED CRC64;
MAKYLAQIIV MGVQVVGRAF ARALRQEFAA SQAAADARGR AGHQSAAASN LSGLSLQEAQ
QILNVSKLSP EEVQKNYEHL FKVNDKSVGG SFYLQSKVVR AKERLDEELR IQAQEDREKG
QKPKT


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