DSC1_SCHPO
ID DSC1_SCHPO Reviewed; 695 AA.
AC O43085;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 1;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Defective for SREBP cleavage protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase DSC1 {ECO:0000305};
DE Flags: Precursor;
GN Name=dsc1; ORFNames=SPBC947.10;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
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 [4]
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: Catalytic component of the DSC E3 ubiquitin ligase complex
CC which is required for the sre1 transcriptional activator proteolytic
CC cleavage to release the soluble transcription factor from the membrane
CC in low oxygen or sterol conditions. The complex also plays an important
CC role 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: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein.
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DR EMBL; CU329671; CAA17038.2; -; Genomic_DNA.
DR PIR; T40772; T40772.
DR RefSeq; NP_595266.2; NM_001021173.2.
DR AlphaFoldDB; O43085; -.
DR BioGRID; 277765; 300.
DR STRING; 4896.SPBC947.10.1; -.
DR SwissPalm; O43085; -.
DR MaxQB; O43085; -.
DR PaxDb; O43085; -.
DR EnsemblFungi; SPBC947.10.1; SPBC947.10.1:pep; SPBC947.10.
DR GeneID; 2541251; -.
DR KEGG; spo:SPBC947.10; -.
DR PomBase; SPBC947.10; dsc1.
DR VEuPathDB; FungiDB:SPBC947.10; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_1_0_1; -.
DR InParanoid; O43085; -.
DR OMA; MLTPCHH; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O43085; -.
DR Proteomes; UP000002485; Chromosome II.
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:0005794; C:Golgi apparatus; ISO:PomBase.
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:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Membrane; Metal-binding;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..695
FT /note="DSC E3 ubiquitin ligase complex subunit 1"
FT /id="PRO_0000310840"
FT TOPO_DOM 26..319
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..382
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..509
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..572
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 634..689
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 419..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 79185 MW; 20027683638594E6 CRC64;
MDRRRWVPST PVVTLLLLFM LFAPAPRLPS RNGESSEKSI KAEKRAFSEI KNATFLNIPE
RVEHSLTFPT EIWETRDGLF EEPVGKGDSH LNHTSVMTGN WNILPYPSFG KVSPNVTWHT
TLRNIVMSQS GRFSANLYEY VDGNSDGISF VLNLENNNDT SVYHMTFHGD RVKPINVFLG
STDVTPNFGG VDVIPWLLKD SPYKDAPPLD GTEYFPLLQN RSLERIETRL QDAQTVGWSP
LVFEEEEVTC SAFVFLHNKN TGLDKETLKA IENEFYHPQG VSTQKMPEVF VSGLVYSPDC
NVAFTFSNTK GPRNFVLENH LVRFSSLYIF IVLSQIFVLL RQMRINSPSH VQRLSFLTIA
MQAGLDAYIA IFFLSTNAVI EKGYLPFVSV AFLSLVPSVM FTMRYLALIL RVQNSNMPPP
APRPVTNNSS NNNTNQSNAS NENSPNAPSA ANDNTETTTV NPPQEDDQPM TQHERDQRDW
SAVCLRFYFI ILVVCIASLY SAFWPVIYRF YFISALIFTS YSFWIPQIIQ NVKQGTSRSF
TWTYILGASV LRLYLPLAIF IDSELILGFP PKYFFALGLV LWMLFQVLVL LVQDTLGPRF
FLPKKFFLSS PVYDYHPVIQ QDDLEAFMRD ANVCPICMQP IELVSTGSTL NPASMMVRRN
YMLTPCHHLY HRQCLLQWME TRSICPVCRC HLPAV
