ID   PEP5_SCHPO              Reviewed;         906 AA.
AC   Q9P6N4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=E3 ubiquitin-protein ligase pep5 {ECO:0000250|UniProtKB:P12868};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:P12868};
DE   AltName: Full=Carboxypeptidase Y-deficient protein 5 {ECO:0000250|UniProtKB:P12868};
DE   AltName: Full=Histone E3 ligase pep5 {ECO:0000250|UniProtKB:P12868};
DE   AltName: Full=RING-type E3 ubiquitin transferase pep5 {ECO:0000305};
DE   AltName: Full=Vacuolar protein sorting-associated protein 11 {ECO:0000250|UniProtKB:P12868};
GN   Name=vps11 {ECO:0000250|UniProtKB:P12868};
GN   Synonyms=pep5 {ECO:0000250|UniProtKB:P12868}; ORFNames=SPAC823.12;
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] {ECO:0000305}
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: Required for vacuolar biogenesis and for trafficking of
CC       hydrolase precursors to the vacuole. Mediates transport at the vacuolar
CC       membrane where it may be responsible for tethering transport vesicles
CC       on the target membranes. Acts as component of the HOPS complex that
CC       acts during the docking stage of vacuole fusion. HOPS is an effector
CC       for the vacuolar Rab GTPase ypt7 and is required for vacuolar SNARE
CC       complex assembly. It remains bound to SNARE complexes after vacuole
CC       fusion. Acts as component of the CORVET complex that is required for
CC       transport between endosome and vacuole. CORVET is an effector for the
CC       endosomal Rab GTPase ypt5. Probable ubiquitin-protein ligase involved
CC       in the degradation-related ubiquitination of histones. Contributes to
CC       the post-translational regulation of histone protein levels by
CC       polyubiquitination of excess histones for subsequent degradation.
CC       {ECO:0000250|UniProtKB:P12868}.
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:0000250|UniProtKB:P12868};
CC   -!- SUBUNIT: Component of the homotypic vacuole fusion and vacuole protein
CC       sorting (HOPS) complex. Component of the class C core vacuole/endosome
CC       tethering (CORVET) complex. {ECO:0000250|UniProtKB:P12868}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P12868};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P12868}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P12868}. Cytoplasm
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the VPS11 family. {ECO:0000255}.
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DR   EMBL; CU329670; CAB90157.1; -; Genomic_DNA.
DR   RefSeq; NP_593839.1; NM_001019268.2.
DR   AlphaFoldDB; Q9P6N4; -.
DR   STRING; 4896.SPAC823.12.1; -.
DR   iPTMnet; Q9P6N4; -.
DR   MaxQB; Q9P6N4; -.
DR   PaxDb; Q9P6N4; -.
DR   PRIDE; Q9P6N4; -.
DR   EnsemblFungi; SPAC823.12.1; SPAC823.12.1:pep; SPAC823.12.
DR   GeneID; 2543359; -.
DR   KEGG; spo:SPAC823.12; -.
DR   PomBase; SPAC823.12; vps11.
DR   VEuPathDB; FungiDB:SPAC823.12; -.
DR   eggNOG; KOG2114; Eukaryota.
DR   HOGENOM; CLU_001287_0_0_1; -.
DR   InParanoid; Q9P6N4; -.
DR   OMA; WIAHENG; -.
DR   PhylomeDB; Q9P6N4; -.
DR   PRO; PR:Q9P6N4; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0033263; C:CORVET complex; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:1902500; C:vacuolar HOPS complex; ISO:PomBase.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR   GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISO:PomBase.
DR   GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; ISO:PomBase.
DR   GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:PomBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016528; VPS11.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR23323:SF24; PTHR23323:SF24; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   Pfam; PF17122; zf-C3H2C3; 1.
DR   PIRSF; PIRSF007860; VPS11; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Membrane; Metal-binding; Protein transport; Reference proteome;
KW   Transferase; Transport; Ubl conjugation pathway; Vacuole; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..906
FT                   /note="E3 ubiquitin-protein ligase pep5"
FT                   /id="PRO_0000361017"
FT   REPEAT          413..557
FT                   /note="CHCR"
FT   ZN_FING         871..906
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   906 AA;  102524 MW;  74F8B5B4440F3C80 CRC64;
     MSTFIKNWKR ITLFQVKAIE ENIDRLTSSF SSNGELVVFA TAFGDVSIYN SSFKSLQSIK
     VEDESSIQQI LWLDNKTFLL FSNVEGGTGT NSTVIIYAFS QADENEPPQF VLVTTHKFSI
     NESPYPIIAV SQSPIDKTIA CGFGGGLVSC YHGNPLRERG IKNSYSHNLG EPITGLTYLD
     DQSSVLFIAT TNKTYSLSGK SLSCLDNTGV SLNCSSSCKT TPLQSREKNS SSFVCTRSSG
     LTFYDSKREK ICFTFPGEKH YMTVMGSILA LCYTPTLGTD SSTNEGLKKS FSSSSSIRKA
     DASRNPAFPP RLLLVDLSRN LIVWEGHLKD VAVSILPLKH GFLVVTADDN VFELKRITLQ
     EEISLLCQKM MYNLAISLAK KENMDIEFRE SLMRDYASFL FRRGDFSASM DWYIRSIKSI
     DIPSVCLEFL KAQEIKQLIR LLEELIKTGL ATSDHRLLLL SCYVEIHDSP SIRKLIDIGE
     IDFDQAFKIC YDSNLLDEAK HLAIRFNNNE RVLDVLVESE QYSEALRFFE SLPPSNLLPL
     LLKYGRVLLD KLPEKTTNIF IQFYSNSHRG DLSTSESKGE LKTAKSLRQT YLSLLPYAQV
     ANFSLPPSLY EISPSQEENQ RAALFSEDVS YTAPSPQTCF HIFLNHNSEL ISFLEGILPN
     ASPNYKTLIN TCLFEAYIRE SFASSNVEKQ EFWQEKSNSL LKKVEKNVDL NAVFLISQIL
     GFDDGVRFVQ GKSGQTLDIF RSFCQQNDIE RALKMVRVHG PDQQELYIMM LNCFASLENV
     DSWYQDINEI VNIIVSQRLI SPTQLLDILG KSVNIKLEHI SDSMQSVLDN YRESISKQNE
     AIEMGKRDIE EITSQLSILR TRAFVVQESK CSTCGIDLEL PMVHFRCGHS YHQRCVEDEC
     IRCRWL