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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_HUMAN             Reviewed;         125 AA.
Q9Y3D7; Q6I9Z3; Q9H5X3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
18-JUL-2018, entry version 152.
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; ORFNames=CGI-136;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND VARIANT LYS-114.
TISSUE=Peripheral blood;
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 [LARGE SCALE MRNA].
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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]
TISSUE SPECIFICITY.
PubMed=15704001; DOI=10.1007/s10735-004-3840-8;
Jubinsky P.T., Short M.K., Mutema G., Morris R.E., Ciraolo G.M.,
Li M.;
"Magmas expression in neoplastic human prostate.";
J. Mol. Histol. 36:69-75(2005).
[7]
FUNCTION, INTERACTION WITH DNAJC19, ASSOCIATION WITH THE TIM23
COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-62;
85-ASP--SER-87; PHE-92; TYR-93 AND LEU-94.
PubMed=20053669; DOI=10.1093/hmg/ddq002;
Sinha D., Joshi N., Chittoor B., Samji P., D'Silva P.;
"Role of Magmas in protein transport and human mitochondria
biogenesis.";
Hum. Mol. Genet. 19:1248-1262(2010).
[8]
INTERACTION WITH DNAJC15.
PubMed=23263864; DOI=10.1093/hmg/dds541;
Schusdziarra C., Blamowska M., Azem A., Hell K.;
"Methylation-controlled J-protein MCJ acts in the import of proteins
into human mitochondria.";
Hum. Mol. Genet. 22:1348-1357(2013).
[9]
INVOLVEMENT IN SMDMDM, AND VARIANT SMDMDM ASP-76.
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. {ECO:0000269|PubMed:20053669}.
-!- 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. Associates with the TIM23 complex. {ECO:0000250,
ECO:0000269|PubMed:20053669, ECO:0000269|PubMed:23263864}.
-!- INTERACTION:
Q15041:ARL6IP1; NbExp=3; IntAct=EBI-721147, EBI-714543;
Q9Y5T4:DNAJC15; NbExp=4; IntAct=EBI-721147, EBI-10329228;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669};
Peripheral membrane protein {ECO:0000269|PubMed:11750097,
ECO:0000269|PubMed:20053669}; Matrix side
{ECO:0000269|PubMed:11750097, ECO:0000269|PubMed:20053669}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:15704001}.
-!- INDUCTION: By CSF2/GM-CSF.
-!- DOMAIN: The J-like region, although related to the J domain does
not have co-chaperone activity. {ECO:0000250}.
-!- DISEASE: Spondylometaphyseal dysplasia, Megarbane-Dagher-Melike
type (SMDMDM) [MIM:613320]: An autosomal recessive disease
characterized by pre- and postnatal short stature, developmental
delay, dysmorphic facial appearance, narrow chest, prominent
abdomen, platyspondyly, and short limbs.
{ECO:0000269|PubMed:24786642}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TIM16/PAM16 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF349455; AAL57767.1; -; mRNA.
EMBL; AF151894; AAD34131.1; -; mRNA.
EMBL; AK026514; BAB15494.1; -; mRNA.
EMBL; CR457362; CAG33643.1; -; mRNA.
EMBL; BC005024; AAH05024.1; -; mRNA.
CCDS; CCDS10512.1; -.
RefSeq; NP_057153.8; NM_016069.9.
UniGene; Hs.730693; -.
ProteinModelPortal; Q9Y3D7; -.
SMR; Q9Y3D7; -.
BioGrid; 119231; 39.
IntAct; Q9Y3D7; 15.
MINT; Q9Y3D7; -.
STRING; 9606.ENSP00000315693; -.
iPTMnet; Q9Y3D7; -.
PhosphoSitePlus; Q9Y3D7; -.
BioMuta; PAM16; -.
DMDM; 23503082; -.
EPD; Q9Y3D7; -.
MaxQB; Q9Y3D7; -.
PaxDb; Q9Y3D7; -.
PeptideAtlas; Q9Y3D7; -.
PRIDE; Q9Y3D7; -.
ProteomicsDB; 86023; -.
TopDownProteomics; Q9Y3D7; -.
DNASU; 51025; -.
Ensembl; ENST00000318059; ENSP00000315693; ENSG00000217930.
Ensembl; ENST00000576217; ENSP00000461047; ENSG00000217930.
Ensembl; ENST00000616009; ENSP00000484240; ENSG00000282228.
Ensembl; ENST00000634045; ENSP00000487678; ENSG00000282228.
GeneID; 51025; -.
KEGG; hsa:51025; -.
UCSC; uc002cwd.4; human.
CTD; 51025; -.
DisGeNET; 51025; -.
EuPathDB; HostDB:ENSG00000217930.7; -.
GeneCards; PAM16; -.
HGNC; HGNC:29679; PAM16.
HPA; HPA062721; -.
MalaCards; PAM16; -.
MIM; 613320; phenotype.
MIM; 614336; gene.
neXtProt; NX_Q9Y3D7; -.
OpenTargets; ENSG00000217930; -.
Orphanet; 401979; Autosomal recessive spondylometaphyseal dysplasia, Megarbane type.
eggNOG; KOG3442; Eukaryota.
eggNOG; ENOG411286G; LUCA.
GeneTree; ENSGT00760000119195; -.
HOGENOM; HOG000180095; -.
HOVERGEN; HBG094040; -.
InParanoid; Q9Y3D7; -.
KO; K17805; -.
PhylomeDB; Q9Y3D7; -.
TreeFam; TF315134; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
ChiTaRS; PAM16; human.
GenomeRNAi; 51025; -.
PRO; PR:Q9Y3D7; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000217930; -.
ExpressionAtlas; Q9Y3D7; baseline and differential.
Genevisible; Q9Y3D7; HS.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; IDA:GO_Central.
GO; GO:0001405; C:presequence translocase-associated import motor; IGI:GO_Central.
GO; GO:0032991; C:protein-containing complex; IDA:GO_Central.
GO; GO:0032780; P:negative regulation of ATPase activity; IDA:GO_Central.
GO; GO:0001503; P:ossification; IMP:UniProtKB.
GO; GO:0030150; P:protein import into mitochondrial matrix; IGI:GO_Central.
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; Disease mutation; Dwarfism; Membrane;
Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Translocation;
Transport.
CHAIN 1 125 Mitochondrial import inner membrane
translocase subunit TIM16.
/FTId=PRO_0000214078.
REGION 58 110 J-like.
MOD_RES 69 69 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CQV1}.
VARIANT 76 76 N -> D (in SMDMDM; dbSNP:rs786203989).
{ECO:0000269|PubMed:24786642}.
/FTId=VAR_073419.
VARIANT 114 114 Q -> K (in dbSNP:rs11989).
{ECO:0000269|PubMed:11750097}.
/FTId=VAR_013764.
MUTAGEN 62 62 I->A,Q,W: Substantial loss of protein
translocation into mitochondria in a
heterologous system.
{ECO:0000269|PubMed:20053669}.
MUTAGEN 85 87 DKS->HPD: No effect on protein
translocation into mitochondria in a
heterologous system.
{ECO:0000269|PubMed:20053669}.
MUTAGEN 92 92 F->G: Partial loss of protein
translocation into mitochondria in a
heterologous system. Substantial loss of
protein translocation into mitochondria
in a heterologous system; when associated
with G-93. Partial loss of DNAJC19-
binding. Loss of DNAJC19-binding; when
associated with G-93. Partial loss of
inhibition of DNAJC19 stimulation of
HSPA9 ATPase activity. Complete loss of
inhibition of DNAJC19 stimulation of
HSPA9 ATPase activity; when associated
with G-93. {ECO:0000269|PubMed:20053669}.
MUTAGEN 93 93 Y->G: Partial loss of protein
translocation into mitochondria in a
heterologous system. Substantial loss of
protein translocation into mitochondria
in a heterologous system; when associated
with G-92. Loss of DNAJC19-binding; when
associated with G-92. Complete loss of
inhibition of DNAJC19 stimulation of
HSPA9 ATPase activity; when associated
with G-92. {ECO:0000269|PubMed:20053669}.
MUTAGEN 94 94 L->A: No effect on protein translocation
into mitochondria in a heterologous
system. {ECO:0000269|PubMed:20053669}.
MUTAGEN 94 94 L->Q: Substantial loss of protein
translocation into mitochondria in a
heterologous system. Substantial loss of
DNAJC19-binding. Partial loss of
inhibition of DNAJC19 stimulation of
HSPA9 ATPase activity.
{ECO:0000269|PubMed:20053669}.
CONFLICT 120 120 G -> W (in Ref. 2; AAD34131).
{ECO:0000305}.
SEQUENCE 125 AA; 13825 MW; 5E7877B30CC89C61 CRC64;
MAKYLAQIIV MGVQVVGRAF ARALRQEFAA SRAAADARGR AGHRSAAASN LSGLSLQEAQ
QILNVSKLSP EEVQKNYEHL FKVNDKSVGG SFYLQSKVVR AKERLDEELK IQAQEDREKG
QMPHT


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