ID   CCZ1_KLULA              Reviewed;         618 AA.
AC   Q6CRH6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Vacuolar fusion protein CCZ1;
GN   Name=CCZ1; OrderedLocusNames=KLLA0D08998g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382124; CAH00559.1; -; Genomic_DNA.
DR   RefSeq; XP_453463.1; XM_453463.1.
DR   AlphaFoldDB; Q6CRH6; -.
DR   STRING; 28985.XP_453463.1; -.
DR   PRIDE; Q6CRH6; -.
DR   EnsemblFungi; CAH00559; CAH00559; KLLA0_D08998g.
DR   GeneID; 2893556; -.
DR   KEGG; kla:KLLA0_D08998g; -.
DR   eggNOG; ENOG502QSQV; Eukaryota.
DR   HOGENOM; CLU_418686_0_0_1; -.
DR   InParanoid; Q6CRH6; -.
DR   OMA; YNCLFWY; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0035658; C:Mon1-Ccz1 complex; IEA:InterPro.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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..618
FT                   /note="Vacuolar fusion protein CCZ1"
FT                   /id="PRO_0000278850"
FT   REGION          490..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  71655 MW;  6A91002677CBB1BE CRC64;
     MSVQFIVLFR DDDDNKDDSC KLLLYHDLTA HMLSTNEKEQ KIGIIKGMWR FSNEFSQSND
     YCHVELDSYS MLVLEVEPSY YLALGFENTH NSQWPKYKVR LSQCYQFFAM QHGKMQDIED
     KTLSGLLNEH FIPFWDEINL IPDYFLMQDI NTAIDDKMFP CCQFADALNS ISEVKDWQNY
     LKNNVLLSEE NYLNIKDVCV YHLPKNNKNT KEYGFITNFD PQFKSLPTLS NWLVGIDSMY
     GTVSSHGLAG TMSLTETEQQ IELDAEEAHH EQPPNIKTVW DNVTLPITFT MDALKDIGQL
     TGVSNSLSLF TNMKPSWNLW SSSSENGAGS AKLDDKDEYS WLISPLNPSF LPKVYQMRKF
     YLQFDDWSQY NILFWKFKDV IVAVIVDPSF KKISEESFLM KLQEELWNGI SLFYENTGFE
     KRQCSFDYTI LFKEEGKYYS SIPRWKNGLD ESDTALKLVI KGLDETLQFL TNNANRKSSV
     ATVTEVGHDM SLTDHPIPSD PSKGEDGTEK TDKSESSIFS KLNESQLVEL NKELMVILGT
     RSLTVWYKDA NTKERMLKLN NGLMVYLLEN NRKLVLIIKN WFIDSQQKTK SKRSTDMIES
     LGKDVSTWWN RIKDHEPL