DSC3_SCHPO
ID DSC3_SCHPO Reviewed; 250 AA.
AC Q9HE10;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 3;
DE AltName: Full=Defective for SREBP cleavage protein 3;
GN Name=dsc3; ORFNames=SPAC20H4.02;
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:0000269|PubMed:16823372}; Multi-pass membrane protein. Golgi
CC apparatus membrane {ECO:0000269|PubMed:21504829}; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the dsc3 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC19732.1; -; Genomic_DNA.
DR RefSeq; NP_593622.1; NM_001019053.2.
DR AlphaFoldDB; Q9HE10; -.
DR BioGRID; 278474; 320.
DR STRING; 4896.SPAC20H4.02.1; -.
DR PaxDb; Q9HE10; -.
DR EnsemblFungi; SPAC20H4.02.1; SPAC20H4.02.1:pep; SPAC20H4.02.
DR GeneID; 2541990; -.
DR KEGG; spo:SPAC20H4.02; -.
DR PomBase; SPAC20H4.02; dsc3.
DR VEuPathDB; FungiDB:SPAC20H4.02; -.
DR eggNOG; ENOG502S5B3; Eukaryota.
DR HOGENOM; CLU_035821_1_1_1; -.
DR InParanoid; Q9HE10; -.
DR OMA; HCSLGDA; -.
DR PhylomeDB; Q9HE10; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9HE10; -.
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 InterPro; IPR045226; Dsc3.
DR InterPro; IPR025390; Dsc3_C.
DR InterPro; IPR019413; Dsc3_ub-like_dom.
DR PANTHER; PTHR28049; PTHR28049; 1.
DR Pfam; PF10302; DUF2407; 1.
DR Pfam; PF13373; DUF2407_C; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..250
FT /note="DSC E3 ubiquitin ligase complex subunit 3"
FT /id="PRO_0000350755"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 105..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 250 AA; 28263 MW; 1AD18FD0D28F3E63 CRC64;
MSSSALKKWE IVIRFASSIP DLSLEISDAQ TTTIHSLFKI VRNRIPECRD KQLKMVFQGR
LLSPGFTVER AVRGNWQRDE NDDPNIVQKA FIHCIVGPTL TEEELASQDQ AQSGLNSNSE
SPDDLQNAQT GETLRGFDRL REAGFTETEV NNLRSQFHRL RGTNLDSLTE DAIREAEDDW
IDNGGQNSSA DELDMSYETL LAGVLIGFFG GAIACYFLWE RTMFSLRMQL SILVGIICNF
AYGLLHSYRW
