MTFR1_MOUSE
ID MTFR1_MOUSE Reviewed; 328 AA.
AC Q99MB2; Q9CQZ4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Mitochondrial fission regulator 1;
DE AltName: Full=Chondrocyte protein with a poly-proline region;
DE Flags: Precursor;
GN Name=Mtfr1; Synonyms=Chppr, Kiaa0009;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15389597; DOI=10.1002/jcp.20126;
RA Tonachini L., Monticone M., Puri C., Tacchetti C., Pinton P., Rizzuto R.,
RA Cancedda R., Tavella S., Castagnola P.;
RT "Chondrocyte protein with a poly-proline region (CHPPR) is a novel
RT mitochondrial protein and promotes mitochondrial fission.";
RL J. Cell. Physiol. 201:470-482(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, Small intestine, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17709566; DOI=10.1530/rep-07-0199;
RA Monticone M., Tonachini L., Tavella S., Degan P., Biticchi R., Palombi F.,
RA Puglisi R., Boitani C., Cancedda R., Castagnola P.;
RT "Impaired expression of genes coding for reactive oxygen species scavenging
RT enzymes in testes of Mtfr1/Chppr-deficient mice.";
RL Reproduction 134:483-492(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION IN AEROBIC RESPIRATION.
RX PubMed=20568109; DOI=10.1002/jcp.22279;
RA Monticone M., Panfoli I., Ravera S., Puglisi R., Jiang M.M., Morello R.,
RA Candiani S., Tonachini L., Biticchi R., Fabiano A., Cancedda R.,
RA Boitani C., Castagnola P.;
RT "The nuclear genes Mtfr1 and Dufd1 regulate mitochondrial dynamic and
RT cellular respiration.";
RL J. Cell. Physiol. 225:767-776(2010).
CC -!- FUNCTION: May play a role in mitochondrial aerobic respiration. May
CC also regulate mitochondrial organization and fission.
CC {ECO:0000269|PubMed:20568109}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=May be
CC associated with the inner and the outer mitochondrial membrane.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC testis. {ECO:0000269|PubMed:17709566}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. However, oxidative
CC DNA damages appear in the testis, associated with a reduced expression
CC of genes encoding enzymes with oxidoreductase activity.
CC {ECO:0000269|PubMed:17709566}.
CC -!- SIMILARITY: Belongs to the MTFR1 family. {ECO:0000305}.
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DR EMBL; AF354708; AAK26434.1; -; mRNA.
DR EMBL; AK004846; BAB23612.2; -; mRNA.
DR EMBL; AK006952; BAB24802.2; -; mRNA.
DR EMBL; AK075822; BAC35988.1; -; mRNA.
DR EMBL; AK075992; BAC36103.1; -; mRNA.
DR EMBL; BC019971; AAH19971.1; -; mRNA.
DR CCDS; CCDS17256.1; -.
DR RefSeq; NP_001240319.1; NM_001253390.1.
DR RefSeq; NP_001240320.1; NM_001253391.1.
DR RefSeq; NP_080458.1; NM_026182.5.
DR RefSeq; XP_006535589.1; XM_006535526.2.
DR RefSeq; XP_011248010.1; XM_011249708.2.
DR AlphaFoldDB; Q99MB2; -.
DR SMR; Q99MB2; -.
DR IntAct; Q99MB2; 1.
DR MINT; Q99MB2; -.
DR STRING; 10090.ENSMUSP00000119724; -.
DR iPTMnet; Q99MB2; -.
DR PhosphoSitePlus; Q99MB2; -.
DR MaxQB; Q99MB2; -.
DR PaxDb; Q99MB2; -.
DR PRIDE; Q99MB2; -.
DR ProteomicsDB; 287633; -.
DR Antibodypedia; 11925; 120 antibodies from 23 providers.
DR DNASU; 67472; -.
DR Ensembl; ENSMUST00000117529; ENSMUSP00000112824; ENSMUSG00000027601.
DR Ensembl; ENSMUST00000119865; ENSMUSP00000112752; ENSMUSG00000027601.
DR Ensembl; ENSMUST00000130645; ENSMUSP00000119724; ENSMUSG00000027601.
DR GeneID; 67472; -.
DR KEGG; mmu:67472; -.
DR UCSC; uc008orp.2; mouse.
DR CTD; 9650; -.
DR MGI; MGI:1914722; Mtfr1.
DR VEuPathDB; HostDB:ENSMUSG00000027601; -.
DR eggNOG; ENOG502QSSN; Eukaryota.
DR GeneTree; ENSGT00950000183215; -.
DR HOGENOM; CLU_059135_0_0_1; -.
DR InParanoid; Q99MB2; -.
DR OMA; KKPEIPN; -.
DR OrthoDB; 1485791at2759; -.
DR PhylomeDB; Q99MB2; -.
DR TreeFam; TF331404; -.
DR BioGRID-ORCS; 67472; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Mtfr1; mouse.
DR PRO; PR:Q99MB2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q99MB2; protein.
DR Bgee; ENSMUSG00000027601; Expressed in spermatid and 247 other tissues.
DR ExpressionAtlas; Q99MB2; baseline and differential.
DR Genevisible; Q99MB2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IMP: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 Coiled coil; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..328
FT /note="Mitochondrial fission regulator 1"
FT /id="PRO_0000096623"
FT REGION 95..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..299
FT /note="Necessary and sufficient to promote mitochondrial
FT fission"
FT /evidence="ECO:0000250"
FT REGION 283..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..167
FT /evidence="ECO:0000255"
FT COMPBIAS 95..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 328 AA; 35905 MW; 69C9352E2654B653 CRC64;
MLGWIKCLMR MWFQRVGVSM QSVLWSGKPY GSSRSIVRKI GTNLSLIQCP RVQFQLTSHA
TEWSPAHSGE DAVASFADVG LVATEEGECS IRLRAEVSSK PPHEDDPPCF EKPPSRHTSF
PSLSQDKPSP ERTLASEEAL QKISALENEL AALRAQIAKI VTLQEQQSPS AGCLDSSTSV
TVAPPPPPPP PPPPLPLVLH QSTSALDLIK ERREQRLSAG KTLATGHPKK PDMPNMLEIL
KDMNSVKLRS VKRSEKDVKP RPADTDHAAF IAEALKKKFA YRHNSQGETE RGIPKPESEA
TSEPALFGPH ILKSTGKMKA LIENVPDS
