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Mitochondrial fission process protein 1 (Mitochondrial 18 kDa protein) (MTP18)

 MTFP1_HUMAN             Reviewed;         166 AA.
Q9UDX5; A6NFQ5; Q9H3K1; Q9P0N6;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Mitochondrial fission process protein 1;
AltName: Full=Mitochondrial 18 kDa protein;
Short=MTP18;
Name=MTFP1; Synonyms=MTP18; ORFNames=HSPC242, My022;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
Mao Y.M., Xie Y., Lin Q., Mu Z.M., Yuan Y.Z.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell, Bone marrow, Brain, Liver, Lymph, and Uterus;
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]
SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION.
PubMed=15155745; DOI=10.1074/jbc.M404704200;
Tondera D., Santel A., Schwarzer R., Dames S., Giese K., Klippel A.,
Kaufmann J.;
"Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent
protein, affects mitochondrial morphology and induces apoptosis.";
J. Biol. Chem. 279:31544-31555(2004).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15985469; DOI=10.1242/jcs.02415;
Tondera D., Czauderna F., Paulick K., Schwarzer R., Kaufmann J.,
Santel A.;
"The mitochondrial protein MTP18 contributes to mitochondrial fission
in mammalian cells.";
J. Cell Sci. 118:3049-3059(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Involved in the mitochondrial division probably by
regulating membrane fission. Loss-of-function induces the release
of cytochrome c, which activates the caspase cascade and leads to
apoptosis. {ECO:0000269|PubMed:15155745,
ECO:0000269|PubMed:15985469}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000305|PubMed:15155745, ECO:0000305|PubMed:15985469}; Multi-
pass membrane protein {ECO:0000305|PubMed:15155745,
ECO:0000305|PubMed:15985469}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UDX5-1; Sequence=Displayed;
Name=2;
IsoId=Q9UDX5-2; Sequence=VSP_041425;
-!- INDUCTION: Expression is regulated by the phosphatidylinositol
(PI) 3-kinase pathway. {ECO:0000269|PubMed:15155745}.
-!- SIMILARITY: Belongs to the MTFP1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF36162.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
Sequence=AAG43136.1; Type=Frameshift; Positions=66, 84; Evidence={ECO:0000305};
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EMBL; AF151076; AAF36162.1; ALT_SEQ; mRNA.
EMBL; AF060924; AAG43136.1; ALT_FRAME; mRNA.
EMBL; CR456345; CAG30231.1; -; mRNA.
EMBL; AC004832; AAF19257.1; -; Genomic_DNA.
EMBL; BC001608; AAH01608.1; -; mRNA.
EMBL; BC009300; AAH09300.1; -; mRNA.
EMBL; BC014446; AAH14446.1; -; mRNA.
EMBL; BC030989; AAH30989.1; -; mRNA.
EMBL; BC038831; AAH38831.1; -; mRNA.
EMBL; BC046132; AAH46132.1; -; mRNA.
CCDS; CCDS33634.1; -. [Q9UDX5-2]
CCDS; CCDS33635.1; -. [Q9UDX5-1]
RefSeq; NP_001003704.1; NM_001003704.2. [Q9UDX5-2]
RefSeq; NP_057582.2; NM_016498.4. [Q9UDX5-1]
UniGene; Hs.713636; -.
ProteinModelPortal; Q9UDX5; -.
BioGrid; 119597; 13.
IntAct; Q9UDX5; 1.
STRING; 9606.ENSP00000266263; -.
iPTMnet; Q9UDX5; -.
PhosphoSitePlus; Q9UDX5; -.
BioMuta; MTFP1; -.
DMDM; 52783151; -.
EPD; Q9UDX5; -.
PaxDb; Q9UDX5; -.
PeptideAtlas; Q9UDX5; -.
PRIDE; Q9UDX5; -.
TopDownProteomics; Q9UDX5-1; -. [Q9UDX5-1]
DNASU; 51537; -.
Ensembl; ENST00000266263; ENSP00000266263; ENSG00000242114. [Q9UDX5-1]
Ensembl; ENST00000355143; ENSP00000347267; ENSG00000242114. [Q9UDX5-2]
GeneID; 51537; -.
KEGG; hsa:51537; -.
UCSC; uc003ahw.3; human. [Q9UDX5-1]
CTD; 51537; -.
DisGeNET; 51537; -.
EuPathDB; HostDB:ENSG00000242114.5; -.
GeneCards; MTFP1; -.
H-InvDB; HIX0213393; -.
HGNC; HGNC:26945; MTFP1.
HPA; HPA077396; -.
MIM; 610235; gene.
neXtProt; NX_Q9UDX5; -.
OpenTargets; ENSG00000242114; -.
eggNOG; KOG3945; Eukaryota.
eggNOG; ENOG4111JTM; LUCA.
GeneTree; ENSGT00390000004019; -.
HOGENOM; HOG000293217; -.
HOVERGEN; HBG052517; -.
InParanoid; Q9UDX5; -.
KO; K17981; -.
OMA; TINRICA; -.
OrthoDB; EOG091G0PGM; -.
PhylomeDB; Q9UDX5; -.
TreeFam; TF324605; -.
GeneWiki; MTP18; -.
GenomeRNAi; 51537; -.
PRO; PR:Q9UDX5; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000242114; -.
ExpressionAtlas; Q9UDX5; baseline and differential.
Genevisible; Q9UDX5; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
InterPro; IPR019560; Mitochondrial_18_kDa_protein_.
Pfam; PF10558; MTP18; 2.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Membrane;
Mitochondrion; Mitochondrion inner membrane; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 166 Mitochondrial fission process protein 1.
/FTId=PRO_0000212411.
TRANSMEM 34 54 Helical. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TRANSMEM 129 149 Helical. {ECO:0000255}.
MOD_RES 123 123 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9CRB8}.
VAR_SEQ 67 166 PSPEAGRSARVTVAVVDTFVWQALASVAIPGFTINRVCAAS
LYVLGTATRWPLAVRKWTTTALGLLTIPIIIHPIDRSVDFL
LDSSLRKLYPTVGKPSSS -> GGFPPGLQPAQALPNSGEA
QLLLIILWYLACASASCFMSTSYSCQGMWTPGSLVSKDPGT
WVGLSWTEA (in isoform 2). {ECO:0000305}.
/FTId=VSP_041425.
CONFLICT 92 92 S -> A (in Ref. 2; AAG43136).
{ECO:0000305}.
SEQUENCE 166 AA; 18010 MW; 447D3BA5CC1ACA2D CRC64;
MSEPQPRGAE RDLYRDTWVR YLGYANEVGE AFRSLVPAAV VWLSYGVASS YVLADAIDKG
KKAGEVPSPE AGRSARVTVA VVDTFVWQAL ASVAIPGFTI NRVCAASLYV LGTATRWPLA
VRKWTTTALG LLTIPIIIHP IDRSVDFLLD SSLRKLYPTV GKPSSS


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