DSC2_SCHPO
ID DSC2_SCHPO Reviewed; 372 AA.
AC Q9UTK7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 2;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Defective for SREBP cleavage protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase DSC2 {ECO:0000305};
DE AltName: Full=UBA domain-containing protein 14;
GN Name=dsc2; Synonyms=ucp14; ORFNames=SPAC1486.02c;
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 [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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND THR-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE DCS COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21504829; DOI=10.1016/j.molcel.2011.02.035;
RA Stewart E.V., Nwosu C.C., Tong Z., Roguev A., Cummins T.D., Kim D.U.,
RA Hayles J., Park H.O., Hoe K.L., Powell D.W., Krogan N.J., Espenshade P.J.;
RT "Yeast SREBP cleavage activation requires the Golgi Dsc E3 ligase
RT complex.";
RL Mol. Cell 42:160-171(2011).
CC -!- FUNCTION: Component of the DSC E3 ubiquitin ligase complex which is
CC required for the sre1 transcriptional activator proteolytic cleavage to
CC release the soluble transcription factor from the membrane in low
CC oxygen or sterol conditions. The complex also plays an important role
CC in the multivesicular body (MVB) pathway and functions in a post-
CC endoplasmic reticulum pathway for protein degradation.
CC {ECO:0000269|PubMed:21504829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the DSC E3 ubiquitin ligase complex composed of
CC dsc1, dsc2, dsc3 and dsc4. {ECO:0000269|PubMed:21504829}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:21504829}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21504829}.
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DR EMBL; CU329670; CAB62412.1; -; Genomic_DNA.
DR PIR; T50071; T50071.
DR RefSeq; NP_594090.1; NM_001019514.2.
DR AlphaFoldDB; Q9UTK7; -.
DR SMR; Q9UTK7; -.
DR BioGRID; 279329; 182.
DR STRING; 4896.SPAC1486.02c.1; -.
DR iPTMnet; Q9UTK7; -.
DR PaxDb; Q9UTK7; -.
DR PRIDE; Q9UTK7; -.
DR EnsemblFungi; SPAC1486.02c.1; SPAC1486.02c.1:pep; SPAC1486.02c.
DR GeneID; 2542884; -.
DR KEGG; spo:SPAC1486.02c; -.
DR PomBase; SPAC1486.02c; dsc2.
DR VEuPathDB; FungiDB:SPAC1486.02c; -.
DR eggNOG; KOG4463; Eukaryota.
DR HOGENOM; CLU_057574_2_1_1; -.
DR InParanoid; Q9UTK7; -.
DR OMA; YDMISGR; -.
DR PhylomeDB; Q9UTK7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9UTK7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; IDA:PomBase.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IDA:PomBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..372
FT /note="DSC E3 ubiquitin ligase complex subunit 2"
FT /id="PRO_0000314098"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 332..368
FT /note="UBA"
FT REGION 246..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 372 AA; 42239 MW; E4E030447955DE82 CRC64;
MSSANIVPSN MGITKFLLLT ISTSSVVAGV FALKPFFHIN FGLHLLSHYQ YWRILLWQFI
YWNSTEVFQA LFIIYQARDV ERLLGSHRFA SFCVYMFILG MFVTPIFSFL YSLLFKNLDY
IQPGPTFLIF AILYQYYYIV PSTVFVRLFN IKFTDKFQMV IPMIGLAFSH FPSTFINAFL
GWTMGMFYHL SLLPGTSWRL PIRFVKPALS PTHVFIRPPY SDMQNASTFN PETLFALPTG
LDAERTENEN QVENPVSNAD ANDSPTRQNA RATAIASSSN TAASFRNRQQ ISHPPLGRTS
SSSVLPTGPA SQLYDMLSGR SERPELGNIR EEDINTVQTI MQTSRAQAIQ ALSQTNDVQR
AVELLLEQTA DY
