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 03-AUG-2022, entry version 137.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; Q8VDV8; -.
DR PeptideAtlas; Q8VDV8; -.
DR PRIDE; Q8VDV8; -.
DR ProteomicsDB; 295619; -.
DR Antibodypedia; 47520; 85 antibodies from 21 providers.
DR Ensembl; ENSMUST00000027257; ENSMUSP00000027257; ENSMUSG00000026088.
DR Ensembl; ENSMUST00000139725; ENSMUSP00000123009; ENSMUSG00000026088.
DR GeneID; 69028; -.
DR KEGG; mmu:69028; -.
DR UCSC; uc007asi.1; mouse.
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; 1494805at2759; -.
DR PhylomeDB; Q8VDV8; -.
DR TreeFam; TF313066; -.
DR BioGRID-ORCS; 69028; 2 hits in 71 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 249 other tissues.
DR Genevisible; Q8VDV8; MM.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
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: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 GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR CDD; cd02683; MIT_1; 1.
DR CDD; cd02685; MIT_C; 1.
DR Gene3D; 3.30.870.30; -; 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 Pfam; PF04212; MIT; 1.
DR Pfam; PF16565; MIT_C; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 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
