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TS101_DICDI
ID   TS101_DICDI             Reviewed;         478 AA.
AC   Q54LJ3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=ESCRT-I complex subunit tsg101;
GN   Name=tsg101; ORFNames=DDB_G0286797;
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).
CC   -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC       trafficking process. Required for the sorting of endocytic
CC       ubiquitinated cargos into multivesicular bodies. May be involved in
CC       cell growth and differentiation. Acts as a negative growth regulator
CC       (By similarity). {ECO:0000250|UniProtKB:Q99816}.
CC   -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC       required for transport I). {ECO:0000250|UniProtKB:Q99816}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Late
CC       endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
CC   -!- DOMAIN: The UEV domain is required for the interaction of the complex
CC       with ubiquitin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000089; EAL64154.1; -; Genomic_DNA.
DR   RefSeq; XP_637568.1; XM_632476.1.
DR   AlphaFoldDB; Q54LJ3; -.
DR   SMR; Q54LJ3; -.
DR   STRING; 44689.DDB0234022; -.
DR   PaxDb; Q54LJ3; -.
DR   PRIDE; Q54LJ3; -.
DR   ABCD; Q54LJ3; 3 sequenced antibodies.
DR   EnsemblProtists; EAL64154; EAL64154; DDB_G0286797.
DR   GeneID; 8625708; -.
DR   KEGG; ddi:DDB_G0286797; -.
DR   dictyBase; DDB_G0286797; tsg101.
DR   eggNOG; KOG2391; Eukaryota.
DR   HOGENOM; CLU_017548_2_0_1; -.
DR   InParanoid; Q54LJ3; -.
DR   OMA; LWLPEPY; -.
DR   PhylomeDB; Q54LJ3; -.
DR   Reactome; R-DDI-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   PRO; PR:Q54LJ3; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0000813; C:ESCRT I complex; ISS:dictyBase.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR   GO; GO:0001778; P:plasma membrane repair; IMP:dictyBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0009611; P:response to wounding; IDA:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR037202; ESCRT_assembly_dom.
DR   InterPro; IPR017916; SB_dom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR008883; UEV_N.
DR   Pfam; PF05743; UEV; 1.
DR   Pfam; PF09454; Vps23_core; 1.
DR   SUPFAM; SSF140111; SSF140111; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS51312; SB; 1.
DR   PROSITE; PS51322; UEV; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Endosome; Growth regulation; Membrane; Nucleus;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..478
FT                   /note="ESCRT-I complex subunit tsg101"
FT                   /id="PRO_0000365724"
FT   DOMAIN          24..172
FT                   /note="UEV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT   DOMAIN          386..454
FT                   /note="SB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT   REGION          144..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          321..372
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        144..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..222
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..237
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  54919 MW;  294FE5E2DDF54A8C CRC64;
     MYGHHGYPMH AHQQQMVNPT LAIVDNKMHT LSTFLNYIRA YRDPLRISKD LKETFHLFPN
     LSPFYENIPN RVNLICIKGT IPICFKGINY YLPIIVWVPL NYPQEFPTMV LDPTPEMRIV
     KNHHHVNLQG LVYHPYISSW SSNSTMETRV SQQQQPQPPQ NNISPPPYGS SPTNNNVAAQ
     QQQPPPPYGS SPSTSNSSSY TQPPPSYDSI KNKTNNTSSL PPPKQPQTSP PPPPTQQQQQ
     QQNNNIIPPP QQPSPPPAYT EPTAAKQQQQ QTSPSVKPLP PLPPQPVIDK KSEMVDQCTI
     KLQELLSKFY DTTSLEIKDF EAHNKSLEEL SKKKLLEKEE LSNQLATYNS QIDQLNENIE
     QLEKWINEND KSDSNIDIDQ ILGPKDSLSK QLLKLVSDDS TIEDLLYYLD KALHSNRISL
     EEYLKNVRSL SRDQFIIRAT VKKVQFIIRQ NQQQLQQQQQ QQNSPQRQQY NQQQYFSK
 
 
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