ID   PEP3_SCHPO              Reviewed;         900 AA.
AC   O74925;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Vacuolar membrane protein pep3;
DE   AltName: Full=Vacuolar protein sorting-associated protein 18;
GN   Name=pep3; Synonyms=vps18; ORFNames=SPCC790.02;
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).
CC   -!- FUNCTION: Required for vacuolar biogenesis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS18 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA21292.1; -; Genomic_DNA.
DR   PIR; T41607; T41607.
DR   RefSeq; NP_588498.1; NM_001023488.2.
DR   AlphaFoldDB; O74925; -.
DR   SMR; O74925; -.
DR   STRING; 4896.SPCC790.02.1; -.
DR   MaxQB; O74925; -.
DR   PaxDb; O74925; -.
DR   PRIDE; O74925; -.
DR   EnsemblFungi; SPCC790.02.1; SPCC790.02.1:pep; SPCC790.02.
DR   GeneID; 2539053; -.
DR   KEGG; spo:SPCC790.02; -.
DR   PomBase; SPCC790.02; pep3.
DR   VEuPathDB; FungiDB:SPCC790.02; -.
DR   eggNOG; KOG2034; Eukaryota.
DR   HOGENOM; CLU_003488_0_0_1; -.
DR   InParanoid; O74925; -.
DR   OMA; HVQRESR; -.
DR   PhylomeDB; O74925; -.
DR   PRO; PR:O74925; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0033263; C:CORVET complex; ISO:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:1902500; C:vacuolar HOPS complex; ISS: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:0007033; P:vacuole organization; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR   GO; GO:0099022; P:vesicle tethering; ISO:PomBase.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR007810; Pep3_Vps18.
DR   InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF05131; Pep3_Vps18; 1.
DR   Pfam; PF10367; Vps39_2; 1.
DR   PROSITE; PS50236; CHCR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane; Metal-binding; Reference proteome; Repeat; TPR repeat; Vacuole;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..900
FT                   /note="Vacuolar membrane protein pep3"
FT                   /id="PRO_0000055992"
FT   REPEAT          314..345
FT                   /note="TPR 1"
FT   REPEAT          373..406
FT                   /note="TPR 2"
FT   REPEAT          408..436
FT                   /note="TPR 3"
FT   REPEAT          546..579
FT                   /note="TPR 4"
FT   REPEAT          602..756
FT                   /note="CHCR"
FT   ZN_FING         837..884
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  103720 MW;  3B45DBD29A6B6C68 CRC64;
     MSLAEDWIDP NSSEDSDIQE DAELEYTADN PEKEQRGVFS LEKVQLQFPV SIRCLAVENN
     ILVMALTSDK LMIVDLERPE DIIDIELPKK VLALGLTYKI FLDPSGHYIF VTTTAGDNCL
     FTPSHQGRVL TKLKGHTVEA VQWNLNGGNI LELLIASKSG VLLELVLTLD SANLKRIEKS
     INTLYSFPFM ESPMGILKNI QDDSMTIVTN KRILRFEPKT SRGKDQLYFS PAFQGSMKEI
     LSFSEEETAQ CFSYSPFPKN LAEPYTLALK TSKRIIYLDI MNPVNPDIQD YEFNESPKLS
     VPTVEMNMIL TSFHLAFLDL DTLYIVNRVN GKESYQQRVN LSPHEEILGL CCDHEKNTYW
     LYTTDSLHEL VVNNETREAS LVFLEKGDFE KALECANTAK VRNTVLVGYA EFLMEHEEYE
     RAATLYAETL KSVEEVALKF IELNQKDVLR LYLWKKLRSY KSTMKIQKSL LVNWLLELML
     AKLNSLDEKE RLELFPENVM QQRQQVQREF STLLNQYKDE INREAAYNLA NNYGKEEQLL
     QIATVMKDQS YIMHYWVQRE NYEKALETLN EGVSQETLIQ HATALLTHRP NETVSIWERQ
     TDLDVHALIP SLLSYNQRSH VPVEENAAIR YLRYVTGVLG CVDPSIHNTL FCIYACHSSS
     NESYLMNYIE QQGNHPLYDM DLGIRLCLQF NCRRSAVKIL VLMKLYSQGV ELALEADDCE
     LAATIANIPE EDVVLKKTLW QTIAKYMFSK KSGIKETLRF LENSEVLQLP ELIRLLPEDI
     KLDDLSDNVC DELDHCMKRI EQLDFEIGQA SEVAHEIQTN AENMRNRYIV LEPNESCWHC
     NQPLFSEPFV LFPCQHAFHR SCMLEKTYKL ASEKNILKEC QLCGPSYAVR LINEPFSTDF