ID   CCZ1_CANGA              Reviewed;         679 AA.
AC   Q6FX38;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Vacuolar fusion protein CCZ1;
GN   Name=CCZ1; OrderedLocusNames=CAGL0C00561g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: In complex with MON1, is required for multiple vacuole
CC       delivery pathways including the cytoplasm to vacuole transport (Cvt),
CC       autophagy, pexophagy and endocytosis. The CCZ1-MON1 complex acts at the
CC       fusion of vesicles with the vacuole, through its regulation of the
CC       SNARE complex during the coordinated priming and docking stages of
CC       fusion, and particularly at the stage of tethering/docking.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with MON1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Prevacuolar
CC       compartment membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Vacuole membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CCZ1 family. {ECO:0000305}.
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DR   EMBL; CR380949; CAG58110.1; -; Genomic_DNA.
DR   RefSeq; XP_445206.1; XM_445206.1.
DR   AlphaFoldDB; Q6FX38; -.
DR   STRING; 5478.XP_445206.1; -.
DR   EnsemblFungi; CAG58110; CAG58110; CAGL0C00561g.
DR   GeneID; 2886768; -.
DR   KEGG; cgr:CAGL0C00561g; -.
DR   CGD; CAL0127504; CAGL0C00561g.
DR   VEuPathDB; FungiDB:CAGL0C00561g; -.
DR   eggNOG; ENOG502QSQV; Eukaryota.
DR   HOGENOM; CLU_418686_0_0_1; -.
DR   InParanoid; Q6FX38; -.
DR   OMA; YNCLFWY; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0035658; C:Mon1-Ccz1 complex; IEA:EnsemblFungi.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:EnsemblFungi.
DR   GO; GO:0097352; P:autophagosome maturation; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IEA:EnsemblFungi.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0044395; P:protein targeting to vacuolar membrane; IEA:EnsemblFungi.
DR   GO; GO:0048278; P:vesicle docking; IEA:EnsemblFungi.
DR   InterPro; IPR013176; Ccz1.
DR   InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR   PANTHER; PTHR13056; PTHR13056; 1.
DR   Pfam; PF19031; Intu_longin_1; 1.
DR   PIRSF; PIRSF011668; DUF1712_fun; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..679
FT                   /note="Vacuolar fusion protein CCZ1"
FT                   /id="PRO_0000278849"
SQ   SEQUENCE   679 AA;  78350 MW;  DC883BFCF44ADDAA CRC64;
     MSQSQSHGSG SPLKYVIVFR PGENKGEQED SVVSEQLLLH HAFEDTELIT LSAKLGKIGI
     IQALWTLSED TNDTCKIIET EQETMITIKV EGEFYITLAI GVDPDLLAIP NPIFEGHLWN
     CYHFFTIKYG DFTSFEKHVL TDLLNEHFVS FWNDLYRKPE SLTRNFLQYL CHDFYKVADL
     DPNGDKQWEA TIIQDLLVQT ENYLGIKDIL VYNIPSTEST YVGKCKYGLI RNFCNEFEDL
     GHFSNWLQHI HTVFGKISSH VLAENVHYEL HSGQLEQTNS DGIRDGNDLN LSDNNNETDS
     NTFSQLSTNF MHNLTLPITF AYDAIQEVGN TTGINNSVSL FMNYLPKWQN NSTASENEKN
     KTKARYGYLI SPLAFDSLPK SYKLKKMHLK FNGEERKPYH VLFWYYNDVL VVIICNESFD
     SIWSKEYLNE LNKHLENSIK TLYDQNLYDL PNTDNHSNKK NDILNFAYLI TDKKRNKLYS
     SFPDLSWFNE QQETLYRTTL ELVSNGLEQL RPQITANELS ITTIDSNKQW GLDIMGNILS
     MLPSNSPVPV TKDASIPLMK KLNFLDKLNE KVLRDISIET LRAIETLSQS INSNIQEEKL
     LKTSDGILLY IRNDCNNLTI ILKNWIQDTK HQTRALKYKN HTLNSYSTSI EDSNLFKNLG
     PDVISWYSEY KQILQDDSS