TOM1_DICDI
ID TOM1_DICDI Reviewed; 663 AA.
AC Q54GH3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Target of Myb protein 1;
DE AltName: Full=DdTom1;
GN Name=tom1; ORFNames=DDB_G0290163;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH UBIQUITIN, EPS15, TSG101
RP AND CHCA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 514-PRO--PRO-517.
RX PubMed=19054384; DOI=10.1111/j.1600-0854.2008.00855.x;
RA Blanc C., Charette S.J., Mattei S., Aubry L., Smith E.W., Cosson P.,
RA Letourneur F.;
RT "Dictyostelium Tom1 participates in an ancestral ESCRT-0 complex.";
RL Traffic 10:161-171(2009).
CC -!- FUNCTION: May contribute to the sorting of ubiquitinated proteins and
CC transfer them for further sorting/trafficking processes to the
CC endosomal multivesicular bodies (MVBs) pathway. Binds to phospholipids,
CC such as phosphatidylinositol PtdIns(3)P and PtdIns(3,5)P2. These
CC phospholipids are involved in the recruitment of the ESCRT machinery to
CC endosomal membranes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19054384}.
CC -!- SUBUNIT: Interacts (via GAT domain) with ubiquitin. Interacts with
CC eps15 and chcA. Interacts with tsg101 (via UEV domain).
CC {ECO:0000269|PubMed:19054384}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19054384}. Membrane
CC {ECO:0000305|PubMed:19054384}; Peripheral membrane protein
CC {ECO:0000305|PubMed:19054384}. Note=Localized to discrete punctae
CC throughout the cytoplasm which are distinct from endocytic vacuoles
CC expressing endosomal protein p80.
CC -!- DOMAIN: The VHS domain binds phosphatidylinositol PtdIns(3)P and
CC PtdIns(4)P.
CC -!- DOMAIN: The GAT domain binds phosphatidylinositol PtdIns(3)P,
CC PtdIns(4)P, PI(3,5)P2 and PtdIns(4,5)P2.
CC -!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
CC involved in the endocytic pathway, are known to interact with the EH
CC domain. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells show no change in the morphology of
CC endocytic compartments. {ECO:0000269|PubMed:19054384}.
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; AAFI02000158; EAL62353.1; -; Genomic_DNA.
DR RefSeq; XP_635855.1; XM_630763.1.
DR AlphaFoldDB; Q54GH3; -.
DR SMR; Q54GH3; -.
DR STRING; 44689.DDB0232160; -.
DR PaxDb; Q54GH3; -.
DR EnsemblProtists; EAL62353; EAL62353; DDB_G0290163.
DR GeneID; 8627511; -.
DR KEGG; ddi:DDB_G0290163; -.
DR dictyBase; DDB_G0290163; tom1.
DR eggNOG; KOG1087; Eukaryota.
DR HOGENOM; CLU_414164_0_0_1; -.
DR InParanoid; Q54GH3; -.
DR OMA; TRNGPAM; -.
DR PRO; PR:Q54GH3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:dictyBase.
DR GO; GO:0043130; F:ubiquitin binding; IDA:dictyBase.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:InterPro.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR044836; TOL_plant.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR45898; PTHR45898; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..663
FT /note="Target of Myb protein 1"
FT /id="PRO_0000367434"
FT DOMAIN 9..136
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 194..284
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REPEAT 386..388
FT /note="1"
FT REPEAT 458..460
FT /note="2"
FT REPEAT 528..530
FT /note="3"
FT REGION 162..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..356
FT /note="Interaction with chcA"
FT REGION 357..663
FT /note="Interaction with tsg101"
FT REGION 384..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 386..388
FT /note="NPF 1"
FT MOTIF 458..460
FT /note="NPF 2"
FT MOTIF 528..530
FT /note="NPF 3"
FT COMPBIAS 297..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 514..517
FT /note="PSAP->AAAA: Abolishes interaction with tsg101."
FT /evidence="ECO:0000269|PubMed:19054384"
SQ SEQUENCE 663 AA; 75375 MW; DA0D1F4FCADCAC96 CRC64;
MVTELVDKAT NELLIQTDWT TVLQISDILN RDPIHARGVV RQVTKKLKDR SRVILLALEL
ADSLLQNCHC THVYFAERTF QTELCRLIMN KKTKLNVKEK TLEIVESWGN AFQARHDVPG
FYETYSFIKR SGYKFPPKPS DAPILNFNNS PAKRTVSTTI LTNNSHSTTP PQANVPSFNN
VSSVGSNNAG GGGSSSQPIK NQEISSIKGS TSVFNEMISF LNVEDEDPQE NDLIKELFET
CKQSQIRVKE MIESGSTNER DLNVLLKLND EINNALNDHE ACIKRRRAFV ENGYKPVPPP
QQQQQQQQQQ QQQQQQQQQQ QSHSNNHNGT TTTTTTNNNN KNPSYLTKHK ELEEIDFFKA
PDGISPYSVQ QQLQPFQQQQ FNSTYNPFAQ PQPQQFQQQP QQQLQQQPQQ QQGFNQRIQQ
PQQQADAFDL FVANRQQSNN NNNNNNINNT TSSFGANNPF ANNSSNNNNT NGAIQPYIPN
TAKSLPPVSQ QLQQPMQNQF SPQPQKFVGS SITPSAPPPF KPNTTQSNPF NTSPPLNNMN
NHNNNMMQQQ QPQQQQQQQP QQQFNPMYNN NAMAPSYPNY NAIGADNQHN TNPYGMMNHQ
QQQQQQQQQQ PMMNQMNNFS APTYSQFTNY AQPNQQPYNN NYGGMNQSNM YPNNNMSGKS
SLI
