CUT8_SCHPO
ID CUT8_SCHPO Reviewed; 262 AA.
AC P38937;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Tethering factor for nuclear proteasome cut8;
DE AltName: Full=Cell untimely torn protein 8;
GN Name=cut8 {ECO:0000303|PubMed:8065367};
GN ORFNames=SPAC17C9.13c {ECO:0000312|PomBase:SPAC17C9.13c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8065367; DOI=10.1128/mcb.14.9.6361-6371.1994;
RA Samejima I., Yanagida M.;
RT "Identification of cut8+ and cek1+, a novel protein kinase gene, which
RT complement a fission yeast mutation that blocks anaphase.";
RL Mol. Cell. Biol. 14:6361-6371(1994).
RN [2]
RP ERRATUM OF PUBMED:8065367.
RA Samejima I., Yanagida M.;
RL Mol. Cell. Biol. 14:7683-7683(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11084332; DOI=10.1016/s0960-9822(00)00773-9;
RA Tatebe H., Yanagida M.;
RT "Cut8, essential for anaphase, controls localization of 26S proteasome,
RT facilitating destruction of cyclin and Cut2.";
RL Curr. Biol. 10:1329-1338(2000).
RN [5]
RP FUNCTION, PROTEASOME-BINDING, AND UBIQUITINATION.
RX PubMed=16096059; DOI=10.1016/j.cell.2005.05.023;
RA Takeda K., Yanagida M.;
RT "Regulation of nuclear proteasome by Rhp6/Ubc2 through ubiquitination and
RT destruction of the sensor and anchor Cut8.";
RL Cell 122:393-405(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28974540; DOI=10.1083/jcb.201612194;
RA Salas-Pino S., Gallardo P., Barrales R.R., Braun S., Daga R.R.;
RT "The fission yeast nucleoporin Alm1 is required for proteasomal degradation
RT of kinetochore components.";
RL J. Cell Biol. 216:3591-3608(2017).
CC -!- FUNCTION: Together with nucleoporin alm1, tethers the proteasome to the
CC nuclear envelope (PubMed:28974540, PubMed:11084332, PubMed:16096059).
CC Involved in ubiquitin-mediated protein degradation and facilitates the
CC degradation of nuclear proteins like mitotic cyclin and cut2
CC (PubMed:11084332, PubMed:16096059). Required for normal progression of
CC anaphase (PubMed:8065367, PubMed:11084332).
CC {ECO:0000269|PubMed:11084332, ECO:0000269|PubMed:16096059,
CC ECO:0000269|PubMed:28974540, ECO:0000269|PubMed:8065367}.
CC -!- SUBUNIT: Binds the proteasome. {ECO:0000269|PubMed:16096059}.
CC -!- INTERACTION:
CC P38937; P38937: cut8; NbExp=3; IntAct=EBI-1152591, EBI-1152591;
CC P38937; P87048: rpn1; NbExp=4; IntAct=EBI-1152591, EBI-1152810;
CC P38937; P50524: rpn12; NbExp=2; IntAct=EBI-1152591, EBI-1152607;
CC P38937; P40303: PRE6; Xeno; NbExp=2; IntAct=EBI-1152591, EBI-13980;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:11084332,
CC ECO:0000269|PubMed:28974540}.
CC -!- PTM: The N-terminal part (residues 1 to 72) is polyubiquitinated by
CC rhp6, which is required for the interaction with the proteasome.
CC {ECO:0000269|PubMed:16096059}.
CC -!- SIMILARITY: Belongs to the cut8/STS1 family. {ECO:0000305}.
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DR EMBL; D31772; BAA06550.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA97343.1; -; Genomic_DNA.
DR PIR; T11593; T11593.
DR RefSeq; NP_594593.1; NM_001020021.2.
DR PDB; 3Q5W; X-ray; 2.75 A; A/B=1-225.
DR PDB; 3Q5X; X-ray; 2.98 A; A=1-225.
DR PDBsum; 3Q5W; -.
DR PDBsum; 3Q5X; -.
DR AlphaFoldDB; P38937; -.
DR SMR; P38937; -.
DR BioGRID; 278659; 19.
DR DIP; DIP-37445N; -.
DR IntAct; P38937; 5.
DR STRING; 4896.SPAC17C9.13c.1; -.
DR PaxDb; P38937; -.
DR PRIDE; P38937; -.
DR EnsemblFungi; SPAC17C9.13c.1; SPAC17C9.13c.1:pep; SPAC17C9.13c.
DR GeneID; 2542184; -.
DR KEGG; spo:SPAC17C9.13c; -.
DR PomBase; SPAC17C9.13c; cut8.
DR VEuPathDB; FungiDB:SPAC17C9.13c; -.
DR eggNOG; ENOG502RNK4; Eukaryota.
DR HOGENOM; CLU_1062295_0_0_1; -.
DR InParanoid; P38937; -.
DR OMA; SSLGWMH; -.
DR PhylomeDB; P38937; -.
DR EvolutionaryTrace; P38937; -.
DR PRO; PR:P38937; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032934; F:sterol binding; IDA:PomBase.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:InterPro.
DR GO; GO:0031144; P:proteasome localization; IEA:InterPro.
DR Gene3D; 1.20.58.1590; -; 1.
DR InterPro; IPR013868; Cut8/Sts1_fam.
DR InterPro; IPR038422; Cut8/Sts1_sf.
DR PANTHER; PTHR28032; PTHR28032; 1.
DR Pfam; PF08559; Cut8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..262
FT /note="Tethering factor for nuclear proteasome cut8"
FT /id="PRO_0000079568"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:3Q5W"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3Q5W"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3Q5X"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:3Q5W"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 160..178
FT /evidence="ECO:0007829|PDB:3Q5W"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:3Q5W"
FT TURN 201..205
FT /evidence="ECO:0007829|PDB:3Q5W"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:3Q5W"
SQ SEQUENCE 262 AA; 30622 MW; 20A7C1C554CD8C0C CRC64;
METLSYSQIK KRKADFDEDI SKRARQLPVG EQLPLSRLLQ YSDKQQLFTI LLQCVEKHPD
LARDIRGILP APSMDTCVET LRKLLINLND SFPYGGDKRG DYAFNRIREK YMAVLHALND
MVPCYLPPYS TCFEKNITFL DAATNVVHEL PEFHNPNHNV YKSQAYYELT GAWLVVLRQL
EDRPVVPLLP LEELEEHNKT SQNRMEEALN YLKQLQKNEP LVHERSHTFQ QTNPQNNFHR
HTNSMNIGND NGMGWHSMHQ YI
