ID A2R3P5_ASPNC Unreviewed; 576 AA.
AC A2R3P5;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Vacuolar protein 8 {ECO:0000256|ARBA:ARBA00026209, ECO:0000256|RuleBase:RU369097};
GN ORFNames=An14g05020 {ECO:0000313|EMBL:CAK42063.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK42063.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42063.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Functions in both vacuole inheritance and protein targeting
CC from the cytoplasm to vacuole. {ECO:0000256|ARBA:ARBA00024821,
CC ECO:0000256|RuleBase:RU369097}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}. Vacuole membrane
CC {ECO:0000256|ARBA:ARBA00004592, ECO:0000256|RuleBase:RU369097}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004592, ECO:0000256|RuleBase:RU369097}.
CC -!- SIMILARITY: Belongs to the beta-catenin family.
CC {ECO:0000256|ARBA:ARBA00005462, ECO:0000256|RuleBase:RU369097}.
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DR EMBL; AM270324; CAK42063.1; -; Genomic_DNA.
DR RefSeq; XP_001401125.1; XM_001401088.2.
DR AlphaFoldDB; A2R3P5; -.
DR SMR; A2R3P5; -.
DR EnsemblFungi; CAK42063; CAK42063; An14g05020.
DR GeneID; 4987360; -.
DR KEGG; ang:An14g05020; -.
DR VEuPathDB; FungiDB:An14g05020; -.
DR HOGENOM; CLU_021483_0_0_1; -.
DR OrthoDB; 2721872at2759; -.
DR Proteomes; UP000006706; Chromosome 1R.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:AspGD.
DR GO; GO:0000329; C:fungal-type vacuole 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:0071562; P:nucleus-vacuole junction assembly; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; 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:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045156; Vac8.
DR PANTHER; PTHR47249; VACUOLAR PROTEIN 8; 1.
DR PANTHER; PTHR47249:SF1; VACUOLAR PROTEIN 8; 1.
DR Pfam; PF00514; Arm; 8.
DR SMART; SM00185; ARM; 9.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS50176; ARM_REPEAT; 7.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU369097};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554, ECO:0000256|RuleBase:RU369097}.
FT REPEAT 106..148
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 147..189
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 188..230
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 229..271
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 272..314
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 313..355
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 354..397
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
SQ SEQUENCE 576 AA; 62544 MW; 61B7B6A0ACE64BF4 CRC64;
MSGITNACLS CFSTVDRWCH ISACLGPIGG RSRDGIYETT LADNEREAVS DLLGYLENRT
ETDFFAGEPL RALSTLVYSD NVDLQRSASL TFAEITERDV REVDRDTLEP ILFLLQSSDI
EVQRAASAAL GNLAVNADNK VLIVALGGLA PLIRQMMSPN VEVQCNAVGC ITNLATHEDN
KAKIARSGAL GPLIRLAKSK DMRVQRNATG ALLNMTHSDD NRQQLVNAGA IPVLVQLLSS
PDVDVQYYCT TALSNIAVDS SNRKRLAQTE SRLVQSLVHL MDSSTPKVQC QAALALRNLA
SDEKYQLEIV RAKGLPPLLR LLQSSYLPLI LSAVACIRNI SIHPLNESPI IDAGFLKPLV
DLLGSTDNEE IQCHAISTLR NLAASSDRNK ELVLQAGAVQ KCKDLVLRVP LSVQSEMTAA
IAVLALSDEL KPHLLNLGVF DVLIPLTESE SIEVQGNSAA ALGNLSSKVG DYSIFVRDWA
DPNGGIHGYL NRFLASGDPT FQHIAIWTLL QLLESEDQRL IGYIAKSDDI VQMVKSISDK
NIESDEEDAE DGEGEVIALA RRCLEFLGNG HKLVEA
//
