VAC8_KLULA
ID VAC8_KLULA Reviewed; 579 AA.
AC Q6CX49;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Vacuolar protein 8;
GN Name=VAC8; OrderedLocusNames=KLLA0A11286g;
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: 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; CR382121; CAH03078.1; -; Genomic_DNA.
DR RefSeq; XP_451490.1; XM_451490.1.
DR AlphaFoldDB; Q6CX49; -.
DR SMR; Q6CX49; -.
DR STRING; 28985.XP_451490.1; -.
DR EnsemblFungi; CAH03078; CAH03078; KLLA0_A11286g.
DR GeneID; 2896638; -.
DR KEGG; kla:KLLA0_A11286g; -.
DR eggNOG; KOG4224; Eukaryota.
DR HOGENOM; CLU_021483_0_0_1; -.
DR InParanoid; Q6CX49; -.
DR OMA; VWDKPDG; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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; 6.
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..579
FT /note="Vacuolar protein 8"
FT /id="PRO_0000256214"
FT REPEAT 39..76
FT /note="ARM 1"
FT REPEAT 77..116
FT /note="ARM 2"
FT REPEAT 118..157
FT /note="ARM 3"
FT REPEAT 159..198
FT /note="ARM 4"
FT REPEAT 200..239
FT /note="ARM 5"
FT REPEAT 241..282
FT /note="ARM 6"
FT REPEAT 284..323
FT /note="ARM 7"
FT REPEAT 325..365
FT /note="ARM 8"
FT REPEAT 409..448
FT /note="ARM 9"
FT REGION 534..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 579 AA; 63770 MW; 9C7ADC9C78693FF7 CRC64;
MGLCCSCLRG ESSLEDSTGL PIAENEREAV TSLLEFLENK DQYDFYSGKP LRALTTLVYS
DNLNLQRSAA LAFAEITEKY VSPVSRDVLE PILMLLTNPD PQIRIASCAA LGNLAVNNEN
KLLIVEMGGL EPLIEQMKSD NVEVQCNAVG CITNLATQDD NKIEIAQSGA LVPLTKLARS
SNIRVQRNAT GALLNMTHSG ENRKELVDAG AVPVLVSLLS SMDADVQYYC TTALSNIAVD
ESNRRYLSKH APKLVTKLVS LMNSTSPRVK CQATLALRNL ASDTNYQLEI VRAGGLPDLV
QLIQSDSLPL VLASVACIRN ISIHPLNEGL IVDAGFLPPL VKLLDYQESE EIQCHAVSTL
RNLAASSEKN RAEFFQSGVI EKFKQLALTC PISVQSEISA CFAILALSDN TKYDLLQQDV
LKVLIPMTMS QDQEISGNSA AAVANLISRV SNLEKILEYW GQPNDGIKGF LIRFLSSDFP
TYEHIALWTI LQLFECHNET IYKLIKEDQK LVNGVKKIAD ENYAVAREYM QDGQDTNIDH
NGNSNNIEGN GRSNKQSSEK EDASFELYNI TQQIIQFLV
