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Database: UniProt
Entry: A0A1V6T9R6_9EURO
LinkDB: A0A1V6T9R6_9EURO
Original site: A0A1V6T9R6_9EURO 
ID   A0A1V6T9R6_9EURO        Unreviewed;       582 AA.
AC   A0A1V6T9R6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN   ORFNames=PENFLA_c012G06864 {ECO:0000313|EMBL:OQE22754.1};
OS   Penicillium flavigenum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE22754.1, ECO:0000313|Proteomes:UP000191342};
RN   [1] {ECO:0000313|Proteomes:UP000191342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQE22754.1}.
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DR   EMBL; MLQL01000012; OQE22754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6T9R6; -.
DR   STRING; 254877.A0A1V6T9R6; -.
DR   OrthoDB; 1708746at2759; -.
DR   Proteomes; UP000191342; 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   Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW   Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT   DOMAIN          118..230
FT                   /note="PX"
FT                   /evidence="ECO:0000259|SMART:SM00312"
FT   REGION          1..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          482..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  63936 MW;  54882B58629F60FC CRC64;
     MDYSVISTDP DHPTGTSPWG SPRAERGTFP TSNNDIPSSP LPGQEQSADV GSVGNGDPQS
     PDLSAQLQSA QLGDPDYPDA HFPFGVHQSP NVQQQQSPTP AQYQTGARQD SRPAAPTYRI
     QGKITGLERT GKKDPILRFD VHTNIPKFRT TQYRDVRRTH SEFVKLADHL VSANPEALVP
     AVPSPVTPAG AGTEEDEIRI KSAMQRWLNV VLSNEVLIQD DEVVLFVESD FGYSPVLRMK
     QPATGVRRKM LKQFAPPPDD TPELQAARPT AKMFYLGSMD SSHKVDRVVK ARRGLGLAEA
     DFGVKLGQMS VQETHPGLGA AYRKLGKIVQ TVGDYHAVQA TAEATTLGEP LNYHSSDAFI
     VKETLTNRHI LLRDLLQAQQ SARSKRAAAD RLKVSSSVRP DKVDEAINAL EEAQNHEDYL
     TKRTQRVTSN LLQEKRRWFD RTTHDLLFSL REYTLRQIEA ERRTLATLES VRPDIRAIDA
     SGGLSRLGRE SHPATRRPNM VSSQGPKGDS WSGVPRRNDN VGRSMSGSFT APSLPDDDDE
     ANGQGSGKGR NRASSQVGSI AEEDDDRLDA RNAASRLATS TF
//
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