MTFP1_HUMAN
ID MTFP1_HUMAN Reviewed; 166 AA.
AC Q9UDX5; A6NFQ5; Q9H3K1; Q9P0N6;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Mitochondrial fission process protein 1;
DE AltName: Full=Mitochondrial 18 kDa protein;
DE Short=MTP18;
GN Name=MTFP1; Synonyms=MTP18; ORFNames=HSPC242, My022;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Lin Q., Mu Z.M., Yuan Y.Z.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, Bone marrow, Brain, Liver, Lymph, and Uterus;
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 SUBCELLULAR LOCATION, FUNCTION, AND INDUCTION.
RX PubMed=15155745; DOI=10.1074/jbc.m404704200;
RA Tondera D., Santel A., Schwarzer R., Dames S., Giese K., Klippel A.,
RA Kaufmann J.;
RT "Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent
RT protein, affects mitochondrial morphology and induces apoptosis.";
RL J. Biol. Chem. 279:31544-31555(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15985469; DOI=10.1242/jcs.02415;
RA Tondera D., Czauderna F., Paulick K., Schwarzer R., Kaufmann J., Santel A.;
RT "The mitochondrial protein MTP18 contributes to mitochondrial fission in
RT mammalian cells.";
RL J. Cell Sci. 118:3049-3059(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in the mitochondrial division probably by regulating
CC membrane fission. Loss-of-function induces the release of cytochrome c,
CC which activates the caspase cascade and leads to apoptosis.
CC {ECO:0000269|PubMed:15155745, ECO:0000269|PubMed:15985469}.
CC -!- INTERACTION:
CC Q9UDX5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1042890, EBI-748974;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:15155745, ECO:0000305|PubMed:15985469}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:15155745,
CC ECO:0000305|PubMed:15985469}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UDX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UDX5-2; Sequence=VSP_041425;
CC -!- INDUCTION: Expression is regulated by the phosphatidylinositol (PI) 3-
CC kinase pathway. {ECO:0000269|PubMed:15155745}.
CC -!- SIMILARITY: Belongs to the MTFP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36162.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG43136.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF151076; AAF36162.1; ALT_SEQ; mRNA.
DR EMBL; AF060924; AAG43136.1; ALT_FRAME; mRNA.
DR EMBL; CR456345; CAG30231.1; -; mRNA.
DR EMBL; AC004832; AAF19257.1; -; Genomic_DNA.
DR EMBL; BC001608; AAH01608.1; -; mRNA.
DR EMBL; BC009300; AAH09300.1; -; mRNA.
DR EMBL; BC014446; AAH14446.1; -; mRNA.
DR EMBL; BC030989; AAH30989.1; -; mRNA.
DR EMBL; BC038831; AAH38831.1; -; mRNA.
DR EMBL; BC046132; AAH46132.1; -; mRNA.
DR CCDS; CCDS33634.1; -. [Q9UDX5-2]
DR CCDS; CCDS33635.1; -. [Q9UDX5-1]
DR RefSeq; NP_001003704.1; NM_001003704.2. [Q9UDX5-2]
DR RefSeq; NP_057582.2; NM_016498.4. [Q9UDX5-1]
DR AlphaFoldDB; Q9UDX5; -.
DR BioGRID; 119597; 34.
DR IntAct; Q9UDX5; 10.
DR STRING; 9606.ENSP00000266263; -.
DR iPTMnet; Q9UDX5; -.
DR PhosphoSitePlus; Q9UDX5; -.
DR SwissPalm; Q9UDX5; -.
DR BioMuta; MTFP1; -.
DR DMDM; 52783151; -.
DR EPD; Q9UDX5; -.
DR jPOST; Q9UDX5; -.
DR MassIVE; Q9UDX5; -.
DR MaxQB; Q9UDX5; -.
DR PaxDb; Q9UDX5; -.
DR PeptideAtlas; Q9UDX5; -.
DR PRIDE; Q9UDX5; -.
DR ProteomicsDB; 84125; -. [Q9UDX5-1]
DR ProteomicsDB; 84126; -. [Q9UDX5-2]
DR TopDownProteomics; Q9UDX5-1; -. [Q9UDX5-1]
DR Antibodypedia; 34826; 110 antibodies from 21 providers.
DR DNASU; 51537; -.
DR Ensembl; ENST00000266263.10; ENSP00000266263.5; ENSG00000242114.6. [Q9UDX5-1]
DR Ensembl; ENST00000355143.8; ENSP00000347267.4; ENSG00000242114.6. [Q9UDX5-2]
DR GeneID; 51537; -.
DR KEGG; hsa:51537; -.
DR MANE-Select; ENST00000266263.10; ENSP00000266263.5; NM_016498.5; NP_057582.2.
DR UCSC; uc003ahw.3; human. [Q9UDX5-1]
DR CTD; 51537; -.
DR DisGeNET; 51537; -.
DR GeneCards; MTFP1; -.
DR HGNC; HGNC:26945; MTFP1.
DR HPA; ENSG00000242114; Low tissue specificity.
DR MIM; 610235; gene.
DR neXtProt; NX_Q9UDX5; -.
DR OpenTargets; ENSG00000242114; -.
DR VEuPathDB; HostDB:ENSG00000242114; -.
DR eggNOG; KOG3945; Eukaryota.
DR GeneTree; ENSGT00390000004019; -.
DR HOGENOM; CLU_1885070_0_0_1; -.
DR InParanoid; Q9UDX5; -.
DR OMA; DVFTWQM; -.
DR PhylomeDB; Q9UDX5; -.
DR TreeFam; TF324605; -.
DR PathwayCommons; Q9UDX5; -.
DR SignaLink; Q9UDX5; -.
DR BioGRID-ORCS; 51537; 20 hits in 1075 CRISPR screens.
DR GeneWiki; MTP18; -.
DR GenomeRNAi; 51537; -.
DR Pharos; Q9UDX5; Tbio.
DR PRO; PR:Q9UDX5; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UDX5; protein.
DR Bgee; ENSG00000242114; Expressed in mucosa of transverse colon and 93 other tissues.
DR ExpressionAtlas; Q9UDX5; baseline and differential.
DR Genevisible; Q9UDX5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR InterPro; IPR019560; Mitochondrial_18_kDa_protein.
DR PANTHER; PTHR11001; PTHR11001; 1.
DR Pfam; PF10558; MTP18; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..166
FT /note="Mitochondrial fission process protein 1"
FT /id="PRO_0000212411"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 123
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRB8"
FT VAR_SEQ 67..166
FT /note="PSPEAGRSARVTVAVVDTFVWQALASVAIPGFTINRVCAASLYVLGTATRWP
FT LAVRKWTTTALGLLTIPIIIHPIDRSVDFLLDSSLRKLYPTVGKPSSS -> GGFPPGL
FT QPAQALPNSGEAQLLLIILWYLACASASCFMSTSYSCQGMWTPGSLVSKDPGTWVGLSW
FT TEA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041425"
FT CONFLICT 92
FT /note="S -> A (in Ref. 2; AAG43136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 18010 MW; 447D3BA5CC1ACA2D CRC64;
MSEPQPRGAE RDLYRDTWVR YLGYANEVGE AFRSLVPAAV VWLSYGVASS YVLADAIDKG
KKAGEVPSPE AGRSARVTVA VVDTFVWQAL ASVAIPGFTI NRVCAASLYV LGTATRWPLA
VRKWTTTALG LLTIPIIIHP IDRSVDFLLD SSLRKLYPTV GKPSSS
