ID   MITD1_RAT               Reviewed;         249 AA.
AC   Q5I0J5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=MIT domain-containing protein 1;
GN   Name=Mitd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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).
CC   -!- FUNCTION: Required for efficient abscission at the end of cytokinesis,
CC       together with components of the ESCRT complexes. Seems not to be
CC       involved in endosomal transport (By similarity). {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}.
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DR   EMBL; BC088263; AAH88263.1; -; mRNA.
DR   RefSeq; NP_001009714.1; NM_001009714.1.
DR   AlphaFoldDB; Q5I0J5; -.
DR   SMR; Q5I0J5; -.
DR   STRING; 10116.ENSRNOP00000024959; -.
DR   PaxDb; Q5I0J5; -.
DR   Ensembl; ENSRNOT00000024959; ENSRNOP00000024959; ENSRNOG00000018467.
DR   GeneID; 363219; -.
DR   KEGG; rno:363219; -.
DR   UCSC; RGD:1307700; rat.
DR   CTD; 129531; -.
DR   RGD; 1307700; Mitd1.
DR   eggNOG; KOG4509; Eukaryota.
DR   GeneTree; ENSGT00390000010868; -.
DR   HOGENOM; CLU_088713_1_0_1; -.
DR   InParanoid; Q5I0J5; -.
DR   OMA; GNIQMNF; -.
DR   OrthoDB; 1494805at2759; -.
DR   PhylomeDB; Q5I0J5; -.
DR   PRO; PR:Q5I0J5; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000018467; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q5I0J5; RN.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR   GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
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   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Endosome; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..249
FT                   /note="MIT domain-containing protein 1"
FT                   /id="PRO_0000260497"
FT   DOMAIN          8..86
FT                   /note="MIT"
FT   REGION          168..231
FT                   /note="Important for association with membranes"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   249 AA;  28849 MW;  0A34DFBD391E99AE CRC64;
     MAKSSLGQDS DSTAAVAVLK RAVELDAESR YQQALVCYQE GIDMLLQVLK GTKESSKRST
     LRTKISGYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG FSYESLFREY LQETVTEVWI
     EDPYIRQTHQ LYNFLRFCEM LIKKPCKVRT IHLLTSGDEG FGNTQQSSGL EEIKQSLRSH
     GVVLEINYSS SIHDREIRFN NGWMIKIGRG LDYFKKPQGR FSLGYCDLDL RPCHETTVDI
     FHNKHTKKI