DSC4_SCHPO
ID DSC4_SCHPO Reviewed; 281 AA.
AC O14175;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 4;
DE AltName: Full=Defective for SREBP cleavage protein 4;
GN Name=dsc4; ORFNames=SPAC4D7.11;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 -!- 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: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:21504829}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372};
CC Multi-pass membrane protein {ECO:0000255}.
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DR EMBL; CU329670; CAB11283.1; -; Genomic_DNA.
DR PIR; T38802; T38802.
DR RefSeq; NP_594964.1; NM_001020395.2.
DR AlphaFoldDB; O14175; -.
DR BioGRID; 279818; 259.
DR STRING; 4896.SPAC4D7.11.1; -.
DR PaxDb; O14175; -.
DR EnsemblFungi; SPAC4D7.11.1; SPAC4D7.11.1:pep; SPAC4D7.11.
DR GeneID; 2543396; -.
DR KEGG; spo:SPAC4D7.11; -.
DR PomBase; SPAC4D7.11; dsc4.
DR VEuPathDB; FungiDB:SPAC4D7.11; -.
DR eggNOG; ENOG502S4TY; Eukaryota.
DR HOGENOM; CLU_990982_0_0_1; -.
DR InParanoid; O14175; -.
DR OMA; FFRCLDM; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O14175; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0035103; P:sterol regulatory element binding protein cleavage; IEA:InterPro.
DR InterPro; IPR038967; Dsc4-like.
DR InterPro; IPR013715; DUF1746.
DR PANTHER; PTHR39405; PTHR39405; 1.
DR Pfam; PF08508; DUF1746; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..281
FT /note="DSC E3 ubiquitin ligase complex subunit 4"
FT /id="PRO_0000116701"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 145..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31717 MW; 19D8E822C52A03F9 CRC64;
MDTIVLDQRG EVFSFFRSLD MLCYAIIAQQ YFQDPTVLLL LLKVFVQLSY LTPKPFSQLN
ALPLFYPLLL NFLISLMVRM FFNLPTAGES LDGYLYGGSI INFIGEKNES SRIDFITSDL
VLFCLQIFMA LILIASNKRP TQASHIQASQ SGLSNVDGDE EPSDLITEDS RDTQQGQRQE
DLQRQLENER SRLIARFSHS LYSFQHGLSF GSPQNRNTPL QRQSADSYST PVCIEVDSED
WKDLVWKSQY ATENANTNSI NNSPLSSNTT GVPNSVLTNP I
