ID   VAC8_ASHGO              Reviewed;         568 AA.
AC   Q757R0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Vacuolar protein 8;
GN   Name=VAC8; OrderedLocusNames=AEL048W;
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: Functions in both vacuole inheritance and protein targeting
CC       from the cytoplasm to vacuole. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52637.1; -; Genomic_DNA.
DR   RefSeq; NP_984813.1; NM_210167.1.
DR   AlphaFoldDB; Q757R0; -.
DR   SMR; Q757R0; -.
DR   STRING; 33169.AAS52637; -.
DR   EnsemblFungi; AAS52637; AAS52637; AGOS_AEL048W.
DR   GeneID; 4621006; -.
DR   KEGG; ago:AGOS_AEL048W; -.
DR   eggNOG; KOG4224; Eukaryota.
DR   HOGENOM; CLU_021483_0_0_1; -.
DR   InParanoid; Q757R0; -.
DR   OMA; VWDKPDG; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:EnsemblFungi.
DR   GO; GO:0045121; C:membrane raft; IEA:EnsemblFungi.
DR   GO; GO:0071563; C:Myo2p-Vac17p-Vac8p transport complex; IEA:EnsemblFungi.
DR   GO; GO:0071561; C:nucleus-vacuole junction; IEA:EnsemblFungi.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0071255; P:Cvt vesicle assembly; IEA:EnsemblFungi.
DR   GO; GO:0071562; P:nucleus-vacuole junction assembly; IBA:GO_Central.
DR   GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR   GO; GO:1903044; P:protein localization to membrane raft; IEA:EnsemblFungi.
DR   GO; GO:0034517; P:ribophagy; IEA:EnsemblFungi.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
DR   GO; GO:0000011; P:vacuole inheritance; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR045156; Vac8.
DR   PANTHER; PTHR47249; PTHR47249; 1.
DR   Pfam; PF00514; Arm; 7.
DR   SMART; SM00185; ARM; 9.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   PROSITE; PS50176; ARM_REPEAT; 7.
PE   3: Inferred from homology;
KW   Lipoprotein; Membrane; Myristate; Palmitate; Reference proteome; Repeat;
KW   Vacuole.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..568
FT                   /note="Vacuolar protein 8"
FT                   /id="PRO_0000256205"
FT   REPEAT          37..74
FT                   /note="ARM 1"
FT   REPEAT          75..114
FT                   /note="ARM 2"
FT   REPEAT          116..155
FT                   /note="ARM 3"
FT   REPEAT          157..196
FT                   /note="ARM 4"
FT   REPEAT          198..237
FT                   /note="ARM 5"
FT   REPEAT          241..280
FT                   /note="ARM 6"
FT   REPEAT          282..321
FT                   /note="ARM 7"
FT   REPEAT          323..363
FT                   /note="ARM 8"
FT   REPEAT          407..446
FT                   /note="ARM 9"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           4
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           5
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   568 AA;  61973 MW;  C8C9C0F66303A7AF CRC64;
     MGGCCSCLKE SQDDATVLPI AENEREAVTS LLGYLEDKDN YDFYSGGPLK ALTTLVYSDN
     LNLQRSAALA FAEITEKYVR PVDREVLEPI LILLQSHDPQ IQIAACAALG NLAVNNENKI
     LIVEMGGLEP LIEQMKSNNV EVQCNAVGCI TNLATQDDNK AKIAHSGALV PLTKLAKSKN
     IRVQRNATGA LLNMTHSGEN RKELVDAGAV PVLVSLLSSS DADVQYYCTT ALSNIAVDES
     NRRKLSQTEP RLVSKLVVLT DSPSARVKCQ ATLALRNLAS DTGYQLEIVR AGGLSHLVKL
     IQCNSMPLVL ASVACIRNIS IHPLNEGLIV DAGFLKPLVK LLDYNDNEEI QCHAVSTLRN
     LAASSEKNRQ EFFESGAVEK CKQLALVSPI SVQSEISACF AILALADNSK LELLDANILE
     ALIPMTFSTN QEVAGNAAAA LANLCSRINN YEKIIESWTE PSKGVCGFLI RFLQSEYPTF
     EHIALWTILQ LLESHNETML GLIKSNKEIV KSIKRLSDIN YENAQKASSL HSRLQQVNGG
     SVASGSEQYE HASLELYNIT QQIMQFLN