ID   A0A319A634_ASPLB        Unreviewed;       588 AA.
AC   A0A319A634;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   08-NOV-2023, entry version 17.
DE   RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN   ORFNames=BO96DRAFT_370039 {ECO:0000313|EMBL:PYH54841.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH54841.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH54841.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH54841.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the membrane-associated retromer complex which
CC       is essential in endosome-to-Golgi retrograde transport.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SUBUNIT: Component of the retromer complex.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
CC   -!- SIMILARITY: Belongs to the VPS17 family.
CC       {ECO:0000256|PIRNR:PIRNR011791}.
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DR   EMBL; KZ821356; PYH54841.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319A634; -.
DR   OrthoDB; 1708746at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd07625; BAR_Vps17p; 1.
DR   CDD; cd06891; PX_Vps17p; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR014461; Retromer_complex_Vps17.
DR   InterPro; IPR037907; Vps17_PX.
DR   InterPro; IPR015404; Vps5_C.
DR   PANTHER; PTHR47433; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   PANTHER; PTHR47433:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 17; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   PIRSF; PIRSF011791; Vps17; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
PE   3: Inferred from homology;
KW   Protein transport {ECO:0000256|PIRNR:PIRNR011791};
KW   Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT   DOMAIN          123..235
FT                   /note="PX"
FT                   /evidence="ECO:0000259|SMART:SM00312"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  64869 MW;  56038A9135D21054 CRC64;
     MDYSAISNDP DHPAGTSPWA SPRPTQTTFP ASVTSDIPPA PLPPQDPYNA ESQPTETPGF
     QENEIGSPDL SARLQGAQLG EPGYVDEHSQ HTQQQHGQQP RSQLPARYQT GPRQNPRQPA
     PVYRIQAKVT GLERTGKKDP ILRFDVHTNI PKFRTTQYRD VRRTHAEFVK LADHLISANP
     EALVPAVPPP LTPAGAGTEE DEIRVKSSLQ RWLNVVLSNE VLIHDDEVVL FVESDFGYSP
     VVRMKQPATG VRRKVLKQFA PPPDDTPELQ NARPIVKMFY LGTMDTSHKV DRVVKARRGL
     GLAESDFGVK LGQMHVQETH PGLSNAYRKL GKIIQTVGDF HAVQATAEAT TLGDPLSYHS
     SDAFIVKETL TNRHILLRDL IQAQQATRSK RAAADRLKVS SSVRPDKVDE AINALDEAQG
     HEDYLTKRTQ RVTSNLLAEK QRWFDRTTND MLASLREYTL RQIESERRTL ATLESVRPDI
     RAIDASGGLS RLGRESHPTA RRPNLGSSQG PKGDAWSGIP RRSDSLGRSL SGSFVAPTPT
     EDDEEVNGHG TGKGRLRSAS GVSSIVEEDD DDRLDARNAA SRLATSTF
//