ID MITD1_HUMAN Reviewed; 249 AA.
AC Q8WV92; Q69YV0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 164.
DE RecName: Full=MIT domain-containing protein 1;
GN Name=MITD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-249.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP2A.
RX PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
RA Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
RA Sanderson C.M.;
RT "A systematic analysis of human CHMP protein interactions: additional MIT
RT domain-containing proteins bind to multiple components of the human ESCRT
RT III complex.";
RL Genomics 88:333-346(2006).
RN [5]
RP INTERACTION WITH CHMP1B.
RX PubMed=19129480; DOI=10.1091/mbc.e08-05-0474;
RA Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
RA Ameer-Beg S., Bowers K., Martin-Serrano J.;
RT "Essential role of hIST1 in cytokinesis.";
RL Mol. Biol. Cell 20:1374-1387(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, INTERACTION WITH CHMP1A AND IST1, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=23015756; DOI=10.1091/mbc.e12-04-0292;
RA Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.;
RT "MITD1 is recruited to midbodies by ESCRT-III and participates in
RT cytokinesis.";
RL Mol. Biol. Cell 23:4347-4361(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH CHMP1A, FUNCTION,
RP SUBUNIT, DOMAIN, INTERACTION WITH CHMP1A; CHMP1B; CHMP2A AND IST1,
RP MUTAGENESIS OF MET-69; GLU-73; TYR-132; ARG-168; ARG-220; PHE-221; TYR-225
RP AND ARG-231, AND SUBCELLULAR LOCATION.
RX PubMed=23045692; DOI=10.1073/pnas.1206839109;
RA Hadders M.A., Agromayor M., Obita T., Perisic O., Caballe A., Kloc M.,
RA Lamers M.H., Williams R.L., Martin-Serrano J.;
RT "ESCRT-III binding protein MITD1 is involved in cytokinesis and has an
RT unanticipated PLD fold that binds membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17424-17429(2012).
CC -!- FUNCTION: Required for efficient abscission at the end of cytokinesis,
CC together with components of the ESCRT-III complex.
CC {ECO:0000269|PubMed:23015756, ECO:0000269|PubMed:23045692}.
CC -!- SUBUNIT: Homodimer. Interacts (via MIT domain) with CHMP1A, CHMP1B,
CC CHMP2A and IST1. {ECO:0000269|PubMed:16730941,
CC ECO:0000269|PubMed:19129480, ECO:0000269|PubMed:23015756,
CC ECO:0000269|PubMed:23045692}.
CC -!- INTERACTION:
CC Q8WV92; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-2691489, EBI-3866279;
CC Q8WV92; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-2691489, EBI-1057156;
CC Q8WV92; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-2691489, EBI-2118090;
CC Q8WV92; O43633: CHMP2A; NbExp=8; IntAct=EBI-2691489, EBI-2692789;
CC Q8WV92; Q9NZZ3: CHMP5; NbExp=3; IntAct=EBI-2691489, EBI-751303;
CC Q8WV92; Q9NQX3-2: GPHN; NbExp=3; IntAct=EBI-2691489, EBI-11043087;
CC Q8WV92; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2691489, EBI-2556193;
CC Q8WV92; Q8WV92: MITD1; NbExp=3; IntAct=EBI-2691489, EBI-2691489;
CC Q8WV92; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2691489, EBI-741158;
CC Q8WV92; O95197-3: RTN3; NbExp=3; IntAct=EBI-2691489, EBI-11525735;
CC Q8WV92; Q6PID6: TTC33; NbExp=3; IntAct=EBI-2691489, EBI-2555404;
CC Q8WV92; Q96K21: ZFYVE19; NbExp=6; IntAct=EBI-2691489, EBI-6448240;
CC Q8WV92; Q96K21-3: ZFYVE19; NbExp=3; IntAct=EBI-2691489, EBI-10187928;
CC Q8WV92; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2691489, EBI-625509;
CC Q8WV92; P04618: rev; Xeno; NbExp=2; IntAct=EBI-2691489, EBI-6164309;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein; Cytoplasmic side. Midbody. Membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=During cytokinesis, recruited to the
CC midbody via interaction with CHMP1A. Interacts with membranes enriched
CC in phosphoinositides.
CC -!- DOMAIN: The C-terminal domain interacts with lipid membranes containing
CC acidic phosphoinositides and is required for location at the midbody.
CC {ECO:0000269|PubMed:23045692}.
CC -!- DOMAIN: The MIT domain interacts with the MIT-interacting motifs of
CC several components of the ESCRT-III complex.
CC {ECO:0000269|PubMed:23045692}.
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DR EMBL; AC092587; AAX88928.1; -; Genomic_DNA.
DR EMBL; BC018453; AAH18453.1; -; mRNA.
DR EMBL; AL161992; CAH10777.1; -; mRNA.
DR CCDS; CCDS2040.1; -.
DR RefSeq; NP_001307346.1; NM_001320417.1.
DR RefSeq; NP_001307347.1; NM_001320418.1.
DR RefSeq; NP_001307348.1; NM_001320419.1.
DR RefSeq; NP_620153.1; NM_138798.2.
DR PDB; 2YMB; X-ray; 3.40 A; A/B/C/D=1-249.
DR PDB; 4A5X; X-ray; 1.91 A; A/B=9-85.
DR PDB; 4A5Z; X-ray; 2.30 A; A/B/C/D=90-243.
DR PDBsum; 2YMB; -.
DR PDBsum; 4A5X; -.
DR PDBsum; 4A5Z; -.
DR AlphaFoldDB; Q8WV92; -.
DR SMR; Q8WV92; -.
DR BioGRID; 126197; 45.
DR IntAct; Q8WV92; 34.
DR STRING; 9606.ENSP00000289359; -.
DR GlyGen; Q8WV92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WV92; -.
DR PhosphoSitePlus; Q8WV92; -.
DR BioMuta; MITD1; -.
DR DMDM; 74730820; -.
DR EPD; Q8WV92; -.
DR jPOST; Q8WV92; -.
DR MassIVE; Q8WV92; -.
DR MaxQB; Q8WV92; -.
DR PaxDb; 9606-ENSP00000289359; -.
DR PeptideAtlas; Q8WV92; -.
DR ProteomicsDB; 74764; -.
DR Pumba; Q8WV92; -.
DR Antibodypedia; 47520; 103 antibodies from 22 providers.
DR DNASU; 129531; -.
DR Ensembl; ENST00000289359.6; ENSP00000289359.2; ENSG00000158411.11.
DR GeneID; 129531; -.
DR KEGG; hsa:129531; -.
DR MANE-Select; ENST00000289359.6; ENSP00000289359.2; NM_138798.3; NP_620153.1.
DR UCSC; uc002szs.2; human.
DR AGR; HGNC:25207; -.
DR CTD; 129531; -.
DR DisGeNET; 129531; -.
DR GeneCards; MITD1; -.
DR HGNC; HGNC:25207; MITD1.
DR HPA; ENSG00000158411; Low tissue specificity.
DR MalaCards; MITD1; -.
DR neXtProt; NX_Q8WV92; -.
DR OpenTargets; ENSG00000158411; -.
DR PharmGKB; PA147357601; -.
DR VEuPathDB; HostDB:ENSG00000158411; -.
DR eggNOG; KOG4509; Eukaryota.
DR GeneTree; ENSGT00390000010868; -.
DR InParanoid; Q8WV92; -.
DR OMA; FYKASNP; -.
DR OrthoDB; 2877779at2759; -.
DR PhylomeDB; Q8WV92; -.
DR TreeFam; TF313066; -.
DR PathwayCommons; Q8WV92; -.
DR SignaLink; Q8WV92; -.
DR BioGRID-ORCS; 129531; 23 hits in 1165 CRISPR screens.
DR GenomeRNAi; 129531; -.
DR Pharos; Q8WV92; Tbio.
DR PRO; PR:Q8WV92; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WV92; Protein.
DR Bgee; ENSG00000158411; Expressed in calcaneal tendon and 180 other cell types or tissues.
DR ExpressionAtlas; Q8WV92; baseline and differential.
DR Genevisible; Q8WV92; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:UniProtKB.
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 IDEAL; IID00575; -.
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_0000260495"
FT DOMAIN 8..86
FT /note="MIT"
FT REGION 168..231
FT /note="Important for association with membranes"
FT MUTAGEN 69
FT /note="M->D: Abolishes interaction with CHMP1A, CHMP1B and
FT CHMP2A."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 73
FT /note="E->A: Abolishes interaction with CHMP1A, CHMP1B and
FT CHMP2A. Abolishes location at the midbody."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 132
FT /note="Y->A: Abolishes homodimerization; when associated
FT with A-221 and A-225."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 168
FT /note="R->E: Strongly reduces binding to membranes; when
FT associated with E-221 and E-231."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 220
FT /note="R->E: Strongly reduces binding to membranes; when
FT associated with E-168 and E-231."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 221
FT /note="F->A: Abolishes homodimerization; when associated
FT with A-132 and A-225."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 225
FT /note="Y->A: Abolishes homodimerization; when associated
FT with A-132 and A-221."
FT /evidence="ECO:0000269|PubMed:23045692"
FT MUTAGEN 231
FT /note="R->E: Strongly reduces binding to membranes; when
FT associated with E-221 and E-220."
FT /evidence="ECO:0000269|PubMed:23045692"
FT CONFLICT 84
FT /note="E -> EGK (in Ref. 3; CAH10777)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Q -> QV (in Ref. 3; CAH10777)"
FT /evidence="ECO:0000305"
FT HELIX 11..27
FT /evidence="ECO:0007829|PDB:4A5X"
FT HELIX 31..50
FT /evidence="ECO:0007829|PDB:4A5X"
FT HELIX 55..81
FT /evidence="ECO:0007829|PDB:4A5X"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4A5Z"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:4A5Z"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:4A5Z"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:4A5Z"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4A5Z"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:4A5Z"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4A5Z"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4A5Z"
SQ SEQUENCE 249 AA; 29314 MW; 82D56C7F6DE3ED0B CRC64;
MAKSGLRQDP QSTAAATVLK RAVELDSESR YPQALVCYQE GIDLLLQVLK GTKDNTKRCN
LREKISKYMD RAENIKKYLD QEKEDGKYHK QIKIEENATG FSYESLFREY LNETVTEVWI
EDPYIRHTHQ LYNFLRFCEM LIKRPCKVKT IHLLTSLDEG IEQVQQSRGL QEIEESLRSH
GVLLEVQYSS SIHDREIRFN NGWMIKIGRG LDYFKKPQSR FSLGYCDFDL RPCHETTVDI
FHKKHTKNI
//
