MSTO1_MOUSE
ID MSTO1_MOUSE Reviewed; 556 AA.
AC Q2YDW2; Q3TJ50; Q3TLZ1; Q3TQV9; Q922H6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Protein misato homolog 1;
GN Name=Msto1;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, Mammary gland, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
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).
CC -!- FUNCTION: Involved in the regulation of mitochondrial distribution and
CC morphology. Required for mitochondrial fusion and mitochondrial network
CC formation. {ECO:0000250|UniProtKB:Q9BUK6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9BUK6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BUK6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2YDW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2YDW2-2; Sequence=VSP_028057;
CC -!- SIMILARITY: Belongs to the misato family. {ECO:0000305}.
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DR EMBL; AK163280; BAE37273.1; -; mRNA.
DR EMBL; AK166236; BAE38651.1; -; mRNA.
DR EMBL; AK167586; BAE39645.1; -; mRNA.
DR EMBL; BC008103; AAH08103.1; -; mRNA.
DR EMBL; BC108354; AAI08355.1; -; mRNA.
DR CCDS; CCDS17485.1; -. [Q2YDW2-1]
DR RefSeq; NP_659147.2; NM_144898.2.
DR AlphaFoldDB; Q2YDW2; -.
DR BioGRID; 230855; 1.
DR IntAct; Q2YDW2; 2.
DR MINT; Q2YDW2; -.
DR STRING; 10090.ENSMUSP00000115645; -.
DR iPTMnet; Q2YDW2; -.
DR PhosphoSitePlus; Q2YDW2; -.
DR EPD; Q2YDW2; -.
DR MaxQB; Q2YDW2; -.
DR PaxDb; Q2YDW2; -.
DR PeptideAtlas; Q2YDW2; -.
DR PRIDE; Q2YDW2; -.
DR ProteomicsDB; 287508; -. [Q2YDW2-1]
DR ProteomicsDB; 287509; -. [Q2YDW2-2]
DR GeneID; 229524; -.
DR KEGG; mmu:229524; -.
DR CTD; 55154; -.
DR MGI; MGI:2385175; Msto1.
DR eggNOG; KOG2530; Eukaryota.
DR InParanoid; Q2YDW2; -.
DR OrthoDB; 1321917at2759; -.
DR BioGRID-ORCS; 229524; 23 hits in 77 CRISPR screens.
DR ChiTaRS; Msto1; mouse.
DR PRO; PR:Q2YDW2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q2YDW2; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR029209; DML1/Misato_tubulin.
DR InterPro; IPR019605; Misato_II_tubulin-like.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR Pfam; PF10644; Misat_Tub_SegII; 1.
DR Pfam; PF14881; Tubulin_3; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="Protein misato homolog 1"
FT /id="PRO_0000304628"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 364..475
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028057"
FT CONFLICT 23
FT /note="H -> D (in Ref. 1; BAE37273)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> D (in Ref. 1; BAE37273/BAE39645)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="H -> Q (in Ref. 1; BAE37273/BAE39645 and 2;
FT AAH08103)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="G -> S (in Ref. 1; BAE38651)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="V -> A (in Ref. 1; BAE38651)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="S -> T (in Ref. 1; BAE38651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 61230 MW; F7611F673290C3CC CRC64;
MAGGAREVLT LQLGHFAGFV GAHWWNQQDA ALGRMAEDEE SPGELCPDVL YRTGRTLHGQ
ETYTPRLILM DLKGSLNTLK EEGNLYRDRQ LEAAVAWQGK LSTHREDAHP KNPNLQGLLS
AEGVRSSDGA WRAKLIQNIQ NGKENSIKVW SDFLRVHLHP RSICVIHKYH HDGETGRLEA
FGQGESVLKE PRYLEELEDR LHFYVEECDY LQGFQLLCDL HDGFSGVGAK TAELLQDEYA
GRGVLTWGLL PGPYSLGEPQ KNIYRLLNTA FGLVHLTGYS SFVCPLSLGG NLGLRPKPPV
NFPSLHYDAT LPFHCSAILA TALDTVTVPY RLRSSMVTMA HLADVLSFSG KKVVTAEAII
PFPLVRGQSL PDILTQLGEA TPWTSLSACG DSAGHRCFAQ SVVLRGIDRA SHTSKLNPGT
PLPSALHACA SGEEVLAQYL QQQHPRVLSS SHLLLTPCKV APPYPHFFSS FSQKGLAMDS
TPKGAAVQSI PVFGALRSTS SLHRTLGDLA EELSRLDLRR WASFMDAGVE QDDMEEMLHE
LHRLAQCYQE GDSLSN
