YFK7_SCHPO
ID YFK7_SCHPO Reviewed; 1029 AA.
AC Q1K9C4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable E3 ubiquitin protein ligase C167.07c;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase C167.07c;
GN ORFNames=SPAC167.07c, SPAC57A7.03c;
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 INDUCTION.
RX PubMed=12529438; DOI=10.1091/mbc.e02-08-0499;
RA Chen D., Toone W.M., Mata J., Lyne R., Burns G., Kivinen K., Brazma A.,
RA Jones N., Baehler J.;
RT "Global transcriptional responses of fission yeast to environmental
RT stress.";
RL Mol. Biol. Cell 14:214-229(2003).
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).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase which mediates
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250}.
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=2.3.2.26;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: By stress. {ECO:0000269|PubMed:12529438}.
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DR EMBL; CU329670; CAB08761.1; -; Genomic_DNA.
DR RefSeq; NP_593378.1; NM_001018810.2.
DR AlphaFoldDB; Q1K9C4; -.
DR SMR; Q1K9C4; -.
DR BioGRID; 279220; 14.
DR STRING; 4896.SPAC167.07c.1; -.
DR iPTMnet; Q1K9C4; -.
DR MaxQB; Q1K9C4; -.
DR PaxDb; Q1K9C4; -.
DR PRIDE; Q1K9C4; -.
DR EnsemblFungi; SPAC167.07c.1; SPAC167.07c.1:pep; SPAC167.07c.
DR GeneID; 2542770; -.
DR KEGG; spo:SPAC167.07c; -.
DR PomBase; SPAC167.07c; -.
DR VEuPathDB; FungiDB:SPAC167.07c; -.
DR eggNOG; KOG0942; Eukaryota.
DR HOGENOM; CLU_002173_2_1_1; -.
DR InParanoid; Q1K9C4; -.
DR OMA; FRIHLLQ; -.
DR PhylomeDB; Q1K9C4; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q1K9C4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR044611; E3B/C.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR45700; PTHR45700; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1029
FT /note="Probable E3 ubiquitin protein ligase C167.07c"
FT /id="PRO_0000351435"
FT DOMAIN 46..75
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 692..1029
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 997
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1029 AA; 117767 MW; C389DB538902D8BA CRC64;
MPLSFEGTFK AKRNVNLGGK RVSNDRAQLL RKAAMERKNR EEERKAENNS VAVQSLSRGF
LARRKFKQDF RERWIYKYTK SGRTSIRFNT LEDIKCSISL LVLFAEPDID LPFVSQVAHN
ILVWLENLIP LSNGMDDTPK SHLKVKILKV QETLSNSNDS WLWQRFSSLL LNCLVSSINS
HRIEGTDTSA ETSLLHCLAY VAPYLKSSEL STYYDSVMTF YAQIYPKQNM TNLEDIMSLS
LLTPVSSKTD ENANSSSAFL FHVLASDCFS SIENCIPPDL IIDKVFSSSL QLSEEACISS
LLNLGMIKVF SLAGNCLHLL HTEYKNSSLW KFCSYILDAL YVFSGESVNS RIQVVSDVDD
DEDDENAFSQ NYYSHLQMVA KHFSKNYANQ SGIVQRSFAE CISSTFITKA FKLVSSNTLQ
AMSHFYATMI KLFPSNRTSI LMYISLVETN EGSLTRSFSR FSWDMFSESP VYQLFHKKFD
VQNVLKNDSG YWFQLQLLID VYSRMLFTMI DDEFHNDKQN PLYPVMAEFC TVLKNLVLGL
YWDVQAAKDV DCKSVVDISQ LRVSSTSLLQ QLYRINSRKQ FLPEDFFLMS EYFNLNEFEA
NALQESELAS HAEAEINITY KFDNFSESRP RLNILNNCSF FLPFHFRIHL LQQLLLLDKQ
ANGYAQPFGH LKHAVIRRNR IFDDGFDAFY NFGKLLKGPI RITFVDEHGV VEEGIDGGGL
TKEFLTSICK TVFDINYGLF SETKAHLLYP NTHAYAQDVE RLRCYEFLGM LIGKCIYEGI
QIDAAFASFF VAKWLGHPSY FDDLTSLDPN LYEGLVFLKN YDGDVENDMA LNFTVVHEEF
GVRNVIDLIP NGSNISVTNE NRLQYIHLVS NYYLNARLSR QCRAFTNGFT QIIDPHWLAM
FHESEIQILV GGDPVPIDID DLRRHTVYAG GYEPNSPTIV LFWEVLREFE EEDKRSFVKF
VTSVARPPIL GFKALMPSFC IRVNGEDETR LPTASTCVNL LKLPMYSTKQ TLRDKLLTAV
RSGVGFGFS
