ID   VAM6_YEAST              Reviewed;        1049 AA.
AC   Q07468; D6VRS2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Vacuolar morphogenesis protein 6;
DE   AltName: Full=Vacuolar protein sorting-associated protein 39;
GN   Name=VAM6; Synonyms=CVT4, VPL18, VPL22, VPS39; OrderedLocusNames=YDL077C;
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].
RX   PubMed=9111041; DOI=10.1074/jbc.272.17.11344;
RA   Nakamura N., Hirata A., Ohsumi Y., Wada Y.;
RT   "Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the
RT   vacuolar membranes and involved in the vacuolar assembly in the yeast
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 272:11344-11349(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   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   [5]
RP   IDENTIFICATION IN THE HOPS COMPLEX, FUNCTION OF THE HOPS COMPLEX, AND
RP   INTERACTION WITH VAM7.
RX   PubMed=16601699; DOI=10.1038/sj.emboj.7601051;
RA   Stroupe C., Collins K.M., Fratti R.A., Wickner W.;
RT   "Purification of active HOPS complex reveals its affinities for
RT   phosphoinositides and the SNARE Vam7p.";
RL   EMBO J. 25:1579-1589(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=32801125; DOI=10.1242/jcs.245555;
RA   Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA   Ishikawa Y., Izawa S., Abe F.;
RT   "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT   high hydrostatic pressure.";
RL   J. Cell Sci. 133:jcs245555-jcs245555(2020).
CC   -!- FUNCTION: Required for vacuolar assembly. Acts as component of the HOPS
CC       complex that acts during the docking stage of vacuole fusion. HOPS is
CC       an effector for the vacuolar Rab GTPase YPT7 and is required for
CC       vacuolar SNARE complex assembly. It remains bound to SNARE complexes
CC       after vacuole fusion. {ECO:0000269|PubMed:16601699}.
CC   -!- SUBUNIT: Component of the HOPS complex which is composed of PEP5,
CC       VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with
CC       phosphoinositides and the PX domain of VAM7. Interacts with VPS41 and
CC       VAM7. {ECO:0000269|PubMed:16601699}.
CC   -!- INTERACTION:
CC       Q07468; P20795: VPS33; NbExp=6; IntAct=EBI-20422, EBI-20395;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Sensitive to high hydrostatic pressure
CC       (mechanical stress). {ECO:0000269|PubMed:32801125}.
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VAM6/VPS39 family. {ECO:0000305}.
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DR   EMBL; Z74125; CAA98643.1; -; Genomic_DNA.
DR   EMBL; D83058; BAA11758.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11782.1; -; Genomic_DNA.
DR   PIR; S67613; S67613.
DR   RefSeq; NP_010206.1; NM_001180136.1.
DR   AlphaFoldDB; Q07468; -.
DR   BioGRID; 31984; 1273.
DR   ComplexPortal; CPX-1625; HOPS complex.
DR   DIP; DIP-1002N; -.
DR   IntAct; Q07468; 11.
DR   MINT; Q07468; -.
DR   STRING; 4932.YDL077C; -.
DR   iPTMnet; Q07468; -.
DR   MaxQB; Q07468; -.
DR   PaxDb; Q07468; -.
DR   PRIDE; Q07468; -.
DR   EnsemblFungi; YDL077C_mRNA; YDL077C; YDL077C.
DR   GeneID; 851482; -.
DR   KEGG; sce:YDL077C; -.
DR   SGD; S000002235; VAM6.
DR   VEuPathDB; FungiDB:YDL077C; -.
DR   eggNOG; KOG2063; Eukaryota.
DR   GeneTree; ENSGT00530000063596; -.
DR   HOGENOM; CLU_293239_0_0_1; -.
DR   InParanoid; Q07468; -.
DR   OMA; FWAPPQL; -.
DR   BioCyc; YEAST:G3O-29488-MON; -.
DR   PRO; PR:Q07468; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q07468; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0030897; C:HOPS complex; IPI:SGD.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; IPI:SGD.
DR   GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR   GO; GO:0035542; P:regulation of SNARE complex assembly; IDA:SGD.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR   GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR   GO; GO:0099022; P:vesicle tethering; IDA:SGD.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR   InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR   InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR   PANTHER; PTHR12894; PTHR12894; 1.
DR   Pfam; PF10366; Vps39_1; 1.
DR   Pfam; PF10367; Vps39_2; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   1: Evidence at protein level;
KW   Membrane; Protein transport; Reference proteome; Transport; Vacuole.
FT   CHAIN           1..1049
FT                   /note="Vacuolar morphogenesis protein 6"
FT                   /id="PRO_0000065903"
FT   REPEAT          730..896
FT                   /note="CHCR"
SQ   SEQUENCE   1049 AA;  122882 MW;  EE8D94E7E2F5F078 CRC64;
     MLRAQKLHSL KSSDITAILP TEQSQKLVLA KKNGDVEVYS RDGNTLKLFQ VYPDLLQNAK
     NDPLPPVIEN FYFANELSTI FAQCKETLIL LSTTNLHEYD RIIDRRGINH CWLFERSHKN
     KEEKNTYLIY STINTAKMRV LIWEGRTYKN MMEASLSYRK ETIRSIYPGE TGITLATDLG
     IYHWPYNKPS LIRIEKTVKN KFPKDMISAL TELKEQAEKV IEKKPKKNSH FDAQSFSSMD
     RMSRKSSMSS LWYRTIRNER GNKIRYTFEL DGNDATPMII DGATKKIFKV ELMHNNEEPF
     LIATDHATFS ESNSEFDHMQ YLSSNLLMLY NSSTIKFVDY ENGFTFLQQK IPEGIKWVKN
     LSGTYFLVWT SNDEVQLFSY HVDDGSEDDD QESICGDIND PDFYQLWRKV LFYKFFIDSP
     HSKELCVSDN PEESLDICAM KLRDLTVMWC LRIFDKFQNY MVQLERSRNS RMIRSKCEEM
     IIKSIFDLFI KFWAPPQLVI LKVFPSAISS LVLEITGQEH HCLLKEAEEV KETYDIPPHL
     LNRWCLPYLT DTRRHLQNLL SKENDDESRI TWCYRDREIK QSFDFFLISN HDDVDLNTML
     TLIDTVLFKC YLYYNPPMVG PFIRVENHCD SHVIVTELKI RHMFKDLIDF YYKRGNHEEA
     LKFLTDLVDE LENDNTDQKQ RQKIDHGVKI LVIYYLKKLS NPQLDVIFTY TDWLLNRHND
     SIKEILSSIF FYDSQACSSR DHLKVYGYIK KFDKLLAIQY LEFAISTFRL EGNKLHTVLI
     KLYLENLDIP STRIKLKSLL ETTSVYEPRT ILKLLNDAIE SGSDQLPTNQ LNFVKYLKIF
     PLSKLENHKE AVHILLDEID DYKAATSYCN DVYQSDSTKG EELLLYLYSK LVSIYDSNRN
     SKLILNFLQD HGSKLNSAEI YKNLPQDISL YDIGRVVSQL LKKHTSKMDE TRLEKALLQV
     ELVATTYKLN ERMSSYGVLS DSHKCPICKK VISNFGTDSI SWFTREGRNI ITHYNCGKVL
     QERFNAKNEK SSRIKQKTLG EVINELNNK