TS101_RAT
ID TS101_RAT Reviewed; 391 AA.
AC Q6IRE4; Q7TSE5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tumor susceptibility gene 101 protein;
DE AltName: Full=ESCRT-I complex subunit TSG101;
GN Name=Tsg101;
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 [MRNA], AND INTERACTION WITH AATF.
RC STRAIN=Fischer 344;
RX PubMed=14761944; DOI=10.1074/jbc.m313703200;
RA Burgdorf S., Leister P., Scheidtmann K.H.;
RT "TSG101 interacts with apoptosis-antagonizing transcription factor and
RT enhances androgen receptor-mediated transcription by promoting its
RT monoubiquitination.";
RL J. Biol. Chem. 279:17524-17534(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Binds to ubiquitinated cargo proteins and is
CC required for the sorting of endocytic ubiquitinated cargos into
CC multivesicular bodies (MVBs). Mediates the association between the
CC ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis;
CC the function requires CEP55. May be involved in cell growth and
CC differentiation. Acts as a negative growth regulator. Required for the
CC exosomal release of SDCBP, CD63 and syndecan (By similarity). It may
CC also play a role in the extracellular release of microvesicles that
CC differ from the exosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q99816}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry.
CC Interacts with VPS37A, VPS37B and VPS37C. Interacts with DMAP1.
CC Interacts with ubiquitin (By similarity). Interacts with AATF
CC (PubMed:14761944). Interacts with stathmin and GMCL (By similarity).
CC Component of an ESCRT-I complex (endosomal sorting complex required for
CC transport I) which consists of TSG101, VPS28, VPS37A and UBAP1 in a
CC 1:1:1:1 stoichiometry. Interacts with HGS; the interaction mediates the
CC association with the ESCRT-0 complex. Interacts with GGA1 and GGA3.
CC Interacts (via UEV domain) with PDCD6IP/AIP1. Interacts with VPS28,
CC SNF8 and VPS36. Self-associates. Interacts with MVB12A; the association
CC appears to be mediated by the TSG101-VPS37 binary subcomplex. Interacts
CC with VPS37D. Interacts with LRSAM1. Interacts with CEP55; the
CC interaction is required for cytokinesis. Interacts with PDCD6.
CC Interacts with LITAF. Interacts with MGRN1 (By similarity). Interacts
CC with ARRDC1; recruits TSG101 to the plasma membrane (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q99816,
CC ECO:0000269|PubMed:14761944}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99816}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q99816}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q99816}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q99816}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q99816}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q99816}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q99816}. Midbody,
CC Midbody ring {ECO:0000250|UniProtKB:Q99816}. Nucleus
CC {ECO:0000250|UniProtKB:Q99816}. Note=Mainly cytoplasmic. Membrane-
CC associated when active and soluble when inactive. Nuclear localization
CC is cell cycle-dependent. Interaction with CEP55 is required for
CC localization to the midbody during cytokinesis.
CC {ECO:0000250|UniProtKB:Q99816}.
CC -!- DOMAIN: The UEV domain is required for the interaction of the complex
CC with ubiquitin. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domain may interact with stathmin.
CC {ECO:0000250}.
CC -!- PTM: Monoubiquitinated at multiple sites by LRSAM1 and by MGRN1.
CC Ubiquitination inactivates it, possibly by regulating its shuttling
CC between an active membrane-bound protein and an inactive soluble form.
CC Ubiquitination by MGRN1 requires the presence of UBE2D1.
CC {ECO:0000250|UniProtKB:Q99816}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000305}.
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DR EMBL; AY293306; AAP45008.1; -; mRNA.
DR EMBL; BC070951; AAH70951.1; -; mRNA.
DR RefSeq; NP_853659.2; NM_181628.2.
DR AlphaFoldDB; Q6IRE4; -.
DR SMR; Q6IRE4; -.
DR BioGRID; 254034; 3.
DR IntAct; Q6IRE4; 1.
DR STRING; 10116.ENSRNOP00000018194; -.
DR iPTMnet; Q6IRE4; -.
DR PhosphoSitePlus; Q6IRE4; -.
DR jPOST; Q6IRE4; -.
DR PRIDE; Q6IRE4; -.
DR Ensembl; ENSRNOT00000112656; ENSRNOP00000080071; ENSRNOG00000013381.
DR GeneID; 292925; -.
DR KEGG; rno:292925; -.
DR UCSC; RGD:3909; rat.
DR CTD; 7251; -.
DR RGD; 3909; Tsg101.
DR eggNOG; KOG2391; Eukaryota.
DR GeneTree; ENSGT00940000153903; -.
DR HOGENOM; CLU_017548_1_1_1; -.
DR InParanoid; Q6IRE4; -.
DR OMA; YMNFPQP; -.
DR OrthoDB; 1435538at2759; -.
DR PhylomeDB; Q6IRE4; -.
DR Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:Q6IRE4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013381; Expressed in ovary and 20 other tissues.
DR Genevisible; Q6IRE4; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0046790; F:virion binding; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:RGD.
DR GO; GO:1990182; P:exosomal secretion; ISO:RGD.
DR GO; GO:0006858; P:extracellular transport; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:RGD.
DR GO; GO:2000397; P:positive regulation of ubiquitin-dependent endocytosis; ISO:RGD.
DR GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; ISO:RGD.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:1903551; P:regulation of extracellular exosome assembly; ISO:RGD.
DR GO; GO:0043405; P:regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0046755; P:viral budding; ISS:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endosome; Growth regulation; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99816"
FT CHAIN 2..391
FT /note="Tumor susceptibility gene 101 protein"
FT /id="PRO_0000082608"
FT DOMAIN 2..145
FT /note="UEV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT DOMAIN 323..391
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT REGION 159..163
FT /note="Interaction with CEP55"
FT /evidence="ECO:0000250"
FT REGION 195..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 238..317
FT /evidence="ECO:0000255"
FT MOTIF 321..324
FT /note="PTAP motif"
FT COMPBIAS 200..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99816"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99816"
FT CONFLICT 45
FT /note="N -> S (in Ref. 1; AAP45008)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> A (in Ref. 1; AAP45008)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="S -> F (in Ref. 1; AAP45008)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="A -> V (in Ref. 1; AAP45008)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="E -> D (in Ref. 1; AAP45008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 44078 MW; 9403128B347CCF73 CRC64;
MAVSESQLKK MMSKYKYRDL TVRQTVNVIA MYKDLKPVLD SYVFNDGSSR ELVNLTGTIP
VRYRGNIYNI PICLWLLDTY PYNPPICFVK PTSSMTIKTG KHVDANGKIY LPYLHDWKHP
RSELLELIQI MIVIFGEEPP VFSRPTVSAS YPPYTAAGPP NTSYLPSMPS GISAYPSGYP
PNPSGYPGCP YPPAGPYPAT TSSQYPSQPP VTTAGPSRDG TISEDTIRAS LISAVSDKLR
WRMKEEMDGA QAELNALKRT EEDLKKGHQK LEEMVTRLDQ EVAEVDKNIE LLKKKDEELS
SALEKMENQS ENNDIDEVII PTAPLYKQIL NLYAEENAIE DTIFYLGEAL RRGVIDLDVF
LKHVRLLSRK QFQLRALMQK ARKTAGLSDL Y
