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Database: UniProt
Entry: MITD1_MOUSE
LinkDB: MITD1_MOUSE
Original site: MITD1_MOUSE 
ID   MITD1_MOUSE             Reviewed;         249 AA.
AC   Q8VDV8; Q9DB13;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=MIT domain-containing protein 1;
GN   Name=Mitd1;
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].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Spleen;
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].
RC   STRAIN=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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
RN   [4]
RP   STRUCTURE BY NMR OF 7-87.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of mouse MIT domain.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Required for efficient abscission at the end of cytokinesis,
CC       together with components of the ESCRT-III complex. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts (via MIT domain) with CHMP1A, CHMP1B,
CC       CHMP2A and IST1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Midbody
CC       {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=During cytokinesis,
CC       recruited to the midbody via interaction with CHMP1A. Interacts with
CC       membranes enriched in phosphoinositides (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain interacts with lipid membranes containing
CC       acidic phosphoinositides and is required for location at the midbody.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The MIT domain interacts with the MIT-interacting motifs of
CC       several components of the ESCRT-III complex. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB23964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK005342; BAB23964.1; ALT_FRAME; mRNA.
DR   EMBL; AK171903; BAE42727.1; -; mRNA.
DR   EMBL; BC020137; AAH20137.1; -; mRNA.
DR   CCDS; CCDS35542.1; -.
DR   RefSeq; NP_081189.1; NM_026913.2.
DR   PDB; 1WFD; NMR; -; A=8-87.
DR   PDBsum; 1WFD; -.
DR   AlphaFoldDB; Q8VDV8; -.
DR   SMR; Q8VDV8; -.
DR   BioGRID; 213179; 5.
DR   IntAct; Q8VDV8; 1.
DR   STRING; 10090.ENSMUSP00000027257; -.
DR   iPTMnet; Q8VDV8; -.
DR   PhosphoSitePlus; Q8VDV8; -.
DR   EPD; Q8VDV8; -.
DR   MaxQB; Q8VDV8; -.
DR   PaxDb; 10090-ENSMUSP00000027257; -.
DR   PeptideAtlas; Q8VDV8; -.
DR   ProteomicsDB; 295619; -.
DR   Pumba; Q8VDV8; -.
DR   Antibodypedia; 47520; 103 antibodies from 22 providers.
DR   Ensembl; ENSMUST00000027257.10; ENSMUSP00000027257.9; ENSMUSG00000026088.16.
DR   Ensembl; ENSMUST00000139725.8; ENSMUSP00000123009.2; ENSMUSG00000026088.16.
DR   GeneID; 69028; -.
DR   KEGG; mmu:69028; -.
DR   UCSC; uc007asi.1; mouse.
DR   AGR; MGI:1916278; -.
DR   CTD; 129531; -.
DR   MGI; MGI:1916278; Mitd1.
DR   VEuPathDB; HostDB:ENSMUSG00000026088; -.
DR   eggNOG; KOG4509; Eukaryota.
DR   GeneTree; ENSGT00390000010868; -.
DR   HOGENOM; CLU_088713_1_0_1; -.
DR   InParanoid; Q8VDV8; -.
DR   OMA; FYKASNP; -.
DR   OrthoDB; 168805at2759; -.
DR   PhylomeDB; Q8VDV8; -.
DR   TreeFam; TF313066; -.
DR   BioGRID-ORCS; 69028; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Mitd1; mouse.
DR   EvolutionaryTrace; Q8VDV8; -.
DR   PRO; PR:Q8VDV8; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8VDV8; Protein.
DR   Bgee; ENSMUSG00000026088; Expressed in ectoplacental cone and 252 other cell types or tissues.
DR   Genevisible; Q8VDV8; MM.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR   CDD; cd02683; MIT_1; 1.
DR   CDD; cd02685; MIT_C; 1.
DR   Gene3D; 3.30.870.30; MITD, C-terminal phospholipase D-like domain; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR032341; MITD1_C.
DR   InterPro; IPR038113; MITD1_C_sf.
DR   InterPro; IPR045331; MITD1_N.
DR   PANTHER; PTHR21222:SF1; MIT DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR21222; UNCHARACTERIZED; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF16565; MIT_C; 1.
DR   SMART; SM00745; MIT; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Endosome; Membrane;
KW   Reference proteome; Transport.
FT   CHAIN           1..249
FT                   /note="MIT domain-containing protein 1"
FT                   /id="PRO_0000260496"
FT   DOMAIN          8..86
FT                   /note="MIT"
FT   REGION          168..231
FT                   /note="Important for association with membranes"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        210
FT                   /note="G -> A (in Ref. 1; BAB23964)"
FT                   /evidence="ECO:0000305"
FT   HELIX           11..27
FT                   /evidence="ECO:0007829|PDB:1WFD"
FT   HELIX           31..50
FT                   /evidence="ECO:0007829|PDB:1WFD"
FT   HELIX           55..85
FT                   /evidence="ECO:0007829|PDB:1WFD"
SQ   SEQUENCE   249 AA;  28847 MW;  90E909D461728B61 CRC64;
     MAKSSLGQDS DSTAAVAVLK RAVELDAESR YQQALVCYQE GIDMLLQVLK GTKESSKRCV
     LRTKISGYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG FSYESLFREY LHETVTEVWI
     EDPYIRQTHQ LYNFLRFCEM LIKKPCKVRT IHLLTSGYEG LGNTQQSSGL EEIKQSLGSH
     GVVLEINYSS SIHDREIRFN NGWMIKIGRG LDYFKKPQGR FSLGYYDLDL RPCHETTVDI
     FHNKHTKKI
//
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