MTFR2_HUMAN
ID MTFR2_HUMAN Reviewed; 385 AA.
AC Q6P444; A8K8D8; E1P585; Q5JWR7; Q6ZUE8; Q7L3U6; Q9BZ39;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mitochondrial fission regulator 2;
DE AltName: Full=DUF729 domain-containing protein 1;
GN Name=MTFR2; Synonyms=DUFD1, FAM54A;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Ovary;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-291 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: May play a role in mitochondrial aerobic respiration
CC essentially in the testis. Can also promote mitochondrial fission (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6P444; P13196: ALAS1; NbExp=5; IntAct=EBI-10252703, EBI-3905054;
CC Q6P444; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10252703, EBI-618309;
CC Q6P444; P43365: MAGEA12; NbExp=3; IntAct=EBI-10252703, EBI-749530;
CC Q6P444; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10252703, EBI-1105213;
CC Q6P444; P36406: TRIM23; NbExp=3; IntAct=EBI-10252703, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=Associated with
CC membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P444-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P444-2; Sequence=VSP_039795, VSP_039796;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MTFR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86277.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK125758; BAC86277.1; ALT_SEQ; mRNA.
DR EMBL; AK292303; BAF84992.1; -; mRNA.
DR EMBL; AL121713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47953.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47954.1; -; Genomic_DNA.
DR EMBL; BC011716; AAH11716.2; -; mRNA.
DR EMBL; BC063688; AAH63688.2; -; mRNA.
DR CCDS; CCDS5176.1; -. [Q6P444-1]
DR RefSeq; NP_001092756.1; NM_001099286.2. [Q6P444-1]
DR RefSeq; NP_001305667.1; NM_001318738.1.
DR RefSeq; NP_612428.2; NM_138419.4. [Q6P444-1]
DR RefSeq; XP_011533712.1; XM_011535410.2.
DR RefSeq; XP_011533714.1; XM_011535412.2.
DR RefSeq; XP_011533715.1; XM_011535413.2.
DR AlphaFoldDB; Q6P444; -.
DR SMR; Q6P444; -.
DR BioGRID; 125224; 56.
DR IntAct; Q6P444; 18.
DR MINT; Q6P444; -.
DR STRING; 9606.ENSP00000395232; -.
DR CarbonylDB; Q6P444; -.
DR iPTMnet; Q6P444; -.
DR PhosphoSitePlus; Q6P444; -.
DR BioMuta; MTFR2; -.
DR DMDM; 56404526; -.
DR EPD; Q6P444; -.
DR jPOST; Q6P444; -.
DR MassIVE; Q6P444; -.
DR MaxQB; Q6P444; -.
DR PaxDb; Q6P444; -.
DR PeptideAtlas; Q6P444; -.
DR PRIDE; Q6P444; -.
DR ProteomicsDB; 66942; -. [Q6P444-1]
DR ProteomicsDB; 66943; -. [Q6P444-2]
DR Antibodypedia; 33003; 79 antibodies from 16 providers.
DR DNASU; 113115; -.
DR Ensembl; ENST00000367784.6; ENSP00000356758.2; ENSG00000146410.12. [Q6P444-2]
DR Ensembl; ENST00000420702.6; ENSP00000395232.1; ENSG00000146410.12. [Q6P444-1]
DR Ensembl; ENST00000451457.6; ENSP00000407010.2; ENSG00000146410.12. [Q6P444-1]
DR GeneID; 113115; -.
DR KEGG; hsa:113115; -.
DR MANE-Select; ENST00000420702.6; ENSP00000395232.1; NM_001099286.3; NP_001092756.1.
DR UCSC; uc003qgt.2; human. [Q6P444-1]
DR CTD; 113115; -.
DR DisGeNET; 113115; -.
DR GeneCards; MTFR2; -.
DR HGNC; HGNC:21115; MTFR2.
DR HPA; ENSG00000146410; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR neXtProt; NX_Q6P444; -.
DR OpenTargets; ENSG00000146410; -.
DR PharmGKB; PA134871105; -.
DR VEuPathDB; HostDB:ENSG00000146410; -.
DR eggNOG; ENOG502QUU8; Eukaryota.
DR GeneTree; ENSGT00950000183215; -.
DR HOGENOM; CLU_059135_0_0_1; -.
DR InParanoid; Q6P444; -.
DR OMA; SHNHFVI; -.
DR OrthoDB; 1485791at2759; -.
DR PhylomeDB; Q6P444; -.
DR TreeFam; TF331404; -.
DR PathwayCommons; Q6P444; -.
DR SignaLink; Q6P444; -.
DR BioGRID-ORCS; 113115; 6 hits in 1069 CRISPR screens.
DR GenomeRNAi; 113115; -.
DR Pharos; Q6P444; Tbio.
DR PRO; PR:Q6P444; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6P444; protein.
DR Bgee; ENSG00000146410; Expressed in buccal mucosa cell and 123 other tissues.
DR ExpressionAtlas; Q6P444; baseline and differential.
DR Genevisible; Q6P444; HS.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR InterPro; IPR007972; Mtfr1.
DR PANTHER; PTHR14215; PTHR14215; 1.
DR Pfam; PF05308; Mito_fiss_reg; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Mitochondrion; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..385
FT /note="Mitochondrial fission regulator 2"
FT /id="PRO_0000087164"
FT REGION 195..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 22..44
FT /note="VLLIWENKDYGSTRSIVRIIGKM -> LEVTSAYLSSLWKKQTGRNLRST
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039795"
FT VAR_SEQ 45..385
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039796"
SQ SEQUENCE 385 AA; 43384 MW; 20A2970A9129CBB7 CRC64;
MSLILNILRE MLEYFGVPVE QVLLIWENKD YGSTRSIVRI IGKMLPLEPC RRPNFELIPL
LNSVDSDNCG SMVPSFADIL YVANDEEASY LRFRNSIWKN EEEKVEIFHP LRLVRDPLSP
AVRQKETVKN DLPVNEAAIR KIAALENELT FLRSQIAAIV EMQELKNSTN SSSFGLSDER
ISLGQLSSSR AAHLSVDPDQ LPGSVLSPPP PPPLPPQFSS LQPPCFPPVQ PGSNNICDSD
NPATEMSKQN PAANKTNYSH HSKSQRNKDI PNMLDVLKDM NKVKLRAIER SPGGRPIHKR
KRQNSHWDPV SLISHALKQK FAFQEDDSFE KENRSWESSP FSSPETSRFG HHISQSEGQR
TKEEMVNTKA VDQGISNTSL LNSRI
