ID A0A448YG65_BRENA Unreviewed; 331 AA.
AC A0A448YG65;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Tethering factor for nuclear proteasome STS1 {ECO:0000256|ARBA:ARBA00016204, ECO:0000256|RuleBase:RU368013};
GN ORFNames=BRENAR_LOCUS645 {ECO:0000313|EMBL:VEU19910.1};
OS Brettanomyces naardenensis (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=13370 {ECO:0000313|EMBL:VEU19910.1, ECO:0000313|Proteomes:UP000290900};
RN [1] {ECO:0000313|EMBL:VEU19910.1, ECO:0000313|Proteomes:UP000290900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tiukova I., Dainat J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in ubiquitin-mediated protein degradation.
CC Regulatory factor in the ubiquitin/proteasome pathway that controls the
CC turnover of proteasome substrates. Targets proteasomes to the nucleus
CC and facilitates the degradation of nuclear proteins.
CC {ECO:0000256|RuleBase:RU368013}.
CC -!- SUBUNIT: Binds the proteasome. {ECO:0000256|RuleBase:RU368013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368013}.
CC Nucleus {ECO:0000256|RuleBase:RU368013}.
CC -!- SIMILARITY: Belongs to the cut8/STS1 family.
CC {ECO:0000256|ARBA:ARBA00006199, ECO:0000256|RuleBase:RU368013}.
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DR EMBL; CAACVR010000001; VEU19910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448YG65; -.
DR STRING; 13370.A0A448YG65; -.
DR InParanoid; A0A448YG65; -.
DR Proteomes; UP000290900; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:UniProtKB-UniRule.
DR GO; GO:0031144; P:proteasome localization; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.1590; Tethering factor for nuclear proteasome Cut8/Sts1; 1.
DR InterPro; IPR013868; Cut8/Sts1_fam.
DR InterPro; IPR038422; Cut8/Sts1_sf.
DR PANTHER; PTHR28032; FI02826P; 1.
DR PANTHER; PTHR28032:SF1; FI02826P; 1.
DR Pfam; PF08559; Cut8; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU368013};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368013};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU368013};
KW Reference proteome {ECO:0000313|Proteomes:UP000290900};
KW Transport {ECO:0000256|RuleBase:RU368013}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 37800 MW; 2CB9E7B2983AECAA CRC64;
MQRESNFTPK ITKPQIASRC TSKRRLSGDL ENYIHSLSED SYGAMPSKYK HSLRGKVTRQ
PSSSSSSYLR LKKQKNPEVF GQKLSLNRIL ETLDREGLQQ LIMNIVSEHP QLSTEVTNLS
PKVTLKDAVS VLRSKLQLII DNIPYKVDPT SDYSFLRVKG YVLDLFQTLS DYTLNYLPPV
ENDLTISIQF LGEFLTQVFH KLPKFQAVEF RYYYKLTVDK FNSIFLDTIS RFVNERKQNI
LLVINENWLE KFDEINELND NHFAAASEYL KQEIEAYKSS GSVILDTSHA DDGEESGDSK
NRLEGIDGLL NFSSDNNPLN GSVLGNVYDA I
//