CCZ1_YEAST
ID CCZ1_YEAST Reviewed; 704 AA.
AC P38273; D6VQC8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Vacuolar fusion protein CCZ1;
DE AltName: Full=Autophagy-related protein 11;
DE AltName: Full=Calcium-caffeine-zinc sensitivity protein 1;
DE AltName: Full=Cytoplasm to vacuole targeting protein 16;
GN Name=CCZ1; Synonyms=AUT11, CVT16; OrderedLocusNames=YBR131W;
GN ORFNames=YBR1006;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=10407278;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<987::aid-yea403>3.0.co;2-5;
RA Kucharczyk R., Gromadka R., Migdalski A., Slonimski P.P., Rytka J.;
RT "Disruption of six novel yeast genes located on chromosome II reveals one
RT gene essential for vegetative growth and two required for sporulation and
RT conferring hypersensitivity to various chemicals.";
RL Yeast 15:987-1000(1999).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11069774; DOI=10.1242/jcs.113.23.4301;
RA Kucharczyk R., Dupre S., Avaro S., Haguenauer-Tsapis R., Slonimski P.P.,
RA Rytka J.;
RT "The novel protein Ccz1p required for vacuolar assembly in Saccharomyces
RT cerevisiae functions in the same transport pathway as Ypt7p.";
RL J. Cell Sci. 113:4301-4311(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH YPT7.
RX PubMed=11590240; DOI=10.1242/jcs.114.17.3137;
RA Kucharczyk R., Kierzek A.M., Slonimski P.P., Rytka J.;
RT "The Ccz1 protein interacts with Ypt7 GTPase during fusion of multiple
RT transport intermediates with the vacuole in S. cerevisiae.";
RL J. Cell Sci. 114:3137-3145(2001).
RN [8]
RP FUNCTION.
RX PubMed=12208507; DOI=10.1016/s0014-5793(02)03119-8;
RA Meiling-Wesse K., Barth H., Thumm M.;
RT "Ccz1p/Aut11p/Cvt16p is essential for autophagy and the cvt pathway.";
RL FEBS Lett. 526:71-76(2002).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MON1.
RX PubMed=12364329; DOI=10.1074/jbc.m208191200;
RA Wang C.-W., Stromhaug P.E., Shima J., Klionsky D.J.;
RT "The Ccz1-Mon1 protein complex is required for the late step of multiple
RT vacuole delivery pathways.";
RL J. Biol. Chem. 277:47917-47927(2002).
RN [10]
RP FUNCTION OF THE CCZ1-MON1 COMPLEX.
RX PubMed=14662743; DOI=10.1083/jcb.200308071;
RA Wang C.-W., Stromhaug P.E., Kauffman E.J., Weisman L.S., Klionsky D.J.;
RT "Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the
RT tethering/docking stage.";
RL J. Cell Biol. 163:973-985(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [13]
RP FUNCTION.
RX PubMed=15184059; DOI=10.1016/j.bbrc.2004.05.063;
RA Love S.L., Manlandro C.M.A., Testa C.J., Thomas A.E., Tryggestad K.-E.,
RA Rosenwald A.G.;
RT "The yeast genes, ARL1 and CCZ1, interact to control membrane traffic and
RT ion homeostasis.";
RL Biochem. Biophys. Res. Commun. 319:840-846(2004).
RN [14]
RP FUNCTION.
RX PubMed=15721293; DOI=10.1016/j.bbrc.2005.01.107;
RA Hoffman-Sommer M., Migdalski A., Rytka J., Kucharczyk R.;
RT "Multiple functions of the vacuolar sorting protein Ccz1p in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 329:197-204(2005).
RN [15]
RP FUNCTION.
RX PubMed=20797862; DOI=10.1016/j.cub.2010.08.002;
RA Nordmann M., Cabrera M., Perz A., Broecker C., Ostrowicz C.,
RA Engelbrecht-Vandre S., Ungermann C.;
RT "The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog
RT Ypt7.";
RL Curr. Biol. 20:1654-1659(2010).
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 (PubMed:10407278, PubMed:11069774, PubMed:11590240, PubMed:12208507,
CC PubMed:12364329, PubMed:14662743, PubMed:15184059, PubMed:15721293).
CC The CCZ1-MON1 complex acts as a guanine nucleotide-exchange factor
CC (GEF) for Rab-type GTPase YPT7, promoting nucleotide exchange on YPT7
CC and triggering endosomal maturation by activating YPT7 on late
CC endosomes (PubMed:20797862). {ECO:0000269|PubMed:10407278,
CC ECO:0000269|PubMed:11069774, ECO:0000269|PubMed:11590240,
CC ECO:0000269|PubMed:12208507, ECO:0000269|PubMed:12364329,
CC ECO:0000269|PubMed:14662743, ECO:0000269|PubMed:15184059,
CC ECO:0000269|PubMed:15721293, ECO:0000269|PubMed:20797862}.
CC -!- SUBUNIT: Forms a complex with MON1. Interacts with YPT7.
CC {ECO:0000269|PubMed:11590240, ECO:0000269|PubMed:12364329}.
CC -!- INTERACTION:
CC P38273; P53129: MON1; NbExp=4; IntAct=EBI-21608, EBI-23945;
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body membrane;
CC Peripheral membrane protein. Prevacuolar compartment membrane;
CC Peripheral membrane protein. Vacuole membrane; Peripheral membrane
CC protein. Note=The association of the CCZ1-MON1 complex with the vacuole
CC is regulated by the C-Vps/HOPS complex.
CC -!- MISCELLANEOUS: Present with 2870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CCZ1 family. {ECO:0000305}.
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DR EMBL; X75891; CAA53490.1; -; Genomic_DNA.
DR EMBL; Z36000; CAA85088.1; -; Genomic_DNA.
DR EMBL; AY693208; AAT93227.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07248.1; -; Genomic_DNA.
DR PIR; S46000; S46000.
DR RefSeq; NP_009689.3; NM_001178479.3.
DR AlphaFoldDB; P38273; -.
DR BioGRID; 32832; 444.
DR ComplexPortal; CPX-1674; MON1-CCZ1 complex.
DR DIP; DIP-7853N; -.
DR IntAct; P38273; 4.
DR MINT; P38273; -.
DR STRING; 4932.YBR131W; -.
DR iPTMnet; P38273; -.
DR MaxQB; P38273; -.
DR PaxDb; P38273; -.
DR PRIDE; P38273; -.
DR EnsemblFungi; YBR131W_mRNA; YBR131W; YBR131W.
DR GeneID; 852428; -.
DR KEGG; sce:YBR131W; -.
DR SGD; S000000335; CCZ1.
DR VEuPathDB; FungiDB:YBR131W; -.
DR eggNOG; ENOG502QSQV; Eukaryota.
DR HOGENOM; CLU_418686_0_0_1; -.
DR InParanoid; P38273; -.
DR OMA; YNCLFWY; -.
DR BioCyc; YEAST:G3O-29086-MON; -.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P38273; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38273; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IDA:SGD.
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; IDA:FlyBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:SGD.
DR GO; GO:0097352; P:autophagosome maturation; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IDA:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0044395; P:protein targeting to vacuolar membrane; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0007034; P:vacuolar transport; IMP:SGD.
DR GO; GO:0048278; P:vesicle docking; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW Autophagy; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..704
FT /note="Vacuolar fusion protein CCZ1"
FT /id="PRO_0000202491"
FT REGION 281..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 80732 MW; E037AD8DBFCC3BDB CRC64;
MRLHYITVFD PSRSTNENDT FKQLLLFHYF GTTDSIPSLN EKLSIIGVIQ GIWSLTSSCV
NKDGEDLEKI IELNNDIIFC IKVESRFFIS LAISNISDDQ SAIPLQYLSA YLWLSYRFFK
LLNGSFSGFN KDFRKLTDLL NEFVIPFWND IYLNLETVTN RSFTVMWPGF YKRANFQHSS
YNPGEKNNVE ESWDAIILQN ILLDKKSYLG LKDILVYHLP KRTKAANRES MGTKTYGLVR
NFTSDLNTLP DISNWLYHLH CTYGEISSHI LTGNVHFKEE LQVEEEQERS RDTNGRDEEE
SQEQQRREHQ ETTQNNTSEL SLSERVIHNV TLPISFAYDA IHEVSTTTGV SGSLSMIMDY
VPKPHWPFIS SSNKSADKNN YSNSNDNANS NAPLMAQSEA VGGTIGNSRF GFLISPLNSD
LLPSSYQALK LNLNFENSKD KEDFYNCLFW YFDDFLIVIV CDPDFNKICE RDYLKDLSFQ
LCQSMECLNN EILNSQNCDN VESFAYVIRD NVTKEIDSSV PFGSPKFTSD ESISTLQLAI
NGIDQFINDN SNSLSLANWN PITIMGGSNA ISKKNTTEGF GNGVNDKTQK FKRKYLNFLN
LMSAEKLWDL QVDVLQFLTS LQNSKRDPDY FQEERLLKLN NGVLCYIKEN NSNLIIIIKN
WFQNNGTSKA AKQRNRFSSD SSKGSSLFQS LGRDVTDWWE SREI
