ID   CCZ1_ASHGO              Reviewed;         663 AA.
AC   Q75EN9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Vacuolar fusion protein CCZ1;
GN   Name=CCZ1; OrderedLocusNames=AAR040C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50405.1; -; Genomic_DNA.
DR   RefSeq; NP_982581.1; NM_207934.1.
DR   AlphaFoldDB; Q75EN9; -.
DR   STRING; 33169.AAS50405; -.
DR   EnsemblFungi; AAS50405; AAS50405; AGOS_AAR040C.
DR   GeneID; 4618721; -.
DR   KEGG; ago:AGOS_AAR040C; -.
DR   eggNOG; ENOG502QSQV; Eukaryota.
DR   HOGENOM; CLU_418686_0_0_1; -.
DR   InParanoid; Q75EN9; -.
DR   OMA; YNCLFWY; -.
DR   Proteomes; UP000000591; Chromosome I.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR013176; Ccz1.
DR   InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR   InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR   PANTHER; PTHR13056; PTHR13056; 1.
DR   Pfam; PF19031; Intu_longin_1; 1.
DR   Pfam; PF19033; Intu_longin_3; 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..663
FT                   /note="Vacuolar fusion protein CCZ1"
FT                   /id="PRO_0000278848"
FT   REGION          503..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  76332 MW;  472CF8240DA87D1E CRC64;
     MDFIAVYNPA VYAKEADSEA WRQLLLYHSF KEDAEEPTPQ NEKLSLIGMI QGIWQFAHNF
     SEPETRGSVR YVDTQLERRR VIAVEVEDGH FMAFGVEDGK RYGCEYYVRE LLQSYHVFRL
     HCGSMSEFAD RGELTDRLNE HVVGYWQALK LVPEAIYAST LASVCWHDGY KVSELELRDR
     AWESYIKNEI LLDSESFLGL KDMCIYKLPR DGRRSAAEYG LLRSFAPEFL SLPELSNWVY
     HLDRLFETAL SSHVLAGHVR LSIGGDEQEE EGELRHDSQP ASDVGARMWR NVTMPISMTY
     DTMSEVGNLT GINTLMSGLN SLTSGFSSMT SRLVRRADRQ NSDTASLSLH VDHGFLISPL
     ALEALPESYR YRRFQLRFST DEPQWYRLLF WYYKDYLCIF IFHENFDKIW DPDYLQAIDA
     KLYDAMLQLE GSVVTEDNKP GRFAYGVFNK TTKRIECSLP LLRFSDKRSD EKSRQPLKMV
     VAGIDETLQF LTAGTFATNM ATSRTNDEHM GPSATNTLRM PEPTDAPSSS WTLDITKLNL
     FQGLNENLRL EKMADTDSGT FLDSLSSEKL LQLNVELCRL YTGIRRSEYN KAGIQEEQLL
     RLNNGILFYI STSPTEDVLI LKNWFMDDKY TKAENKRSTS ASLLHSLGGD VRRWWNARTN
     REQ