ID A0A0M8N0H9_9HYPO Unreviewed; 521 AA.
AC A0A0M8N0H9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN ORFNames=ESCO_003153 {ECO:0000313|EMBL:KOS18054.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18054.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS18054.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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}.
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:KOS18054.1}.
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DR EMBL; LGSR01000022; KOS18054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8N0H9; -.
DR STRING; 150374.A0A0M8N0H9; -.
DR OrthoDB; 1708746at2759; -.
DR Proteomes; UP000053831; 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; 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 SUPFAM; SSF64268; PX domain; 1.
PE 3: Inferred from homology;
KW Protein transport {ECO:0000256|PIRNR:PIRNR011791};
KW Reference proteome {ECO:0000313|Proteomes:UP000053831};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR011791}.
FT DOMAIN 82..162
FT /note="PX"
FT /evidence="ECO:0000259|Pfam:PF00787"
FT DOMAIN 218..401
FT /note="Sorting nexin/Vps5-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09325"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 57136 MW; FF95E586C639A8AD CRC64;
MAPPVPSAEP HEEAAFEQPA PERPLPSQEE AAPDAPAEEP AQLRKSTQPQ FRLQAKITGL
ERTGKKDPIL RFDVHTNLPR FRTTQYRDVR RLHSEFIKLA EHLISANPEA LVPAVPPPLT
SAGAGTDEDE SRVKALMQRW FNYVCGSEAL MMDDEMVLFV ESDFGYSPLV KRKQPATGVR
RKILKQFAPP PDDTPELADA RPTVKLFYLG TMDAGHKVDK LVKARRGLGL AESDYGVKLG
RMHVQEPHPG LANAYKKLGR VVQAVGDYHA AQATAEATTI GDPFQHHSQD AFIVKETLTN
RQILIREFLQ AQEVTRGKLN SADRLKASSS VRREKVDEAI AALDEARENE LQLYNKTSRV
TRNLVQERRK WFDRTATDLR MEIREFVLRE IEAERRTLAL LESVRGDIRS IDGTGGLSRL
GREAHPVGRR TSLAASQGPK GDAWSGAPRR SDATSRTASG SFVAKVPEEG DGDEGQDAAG
SVHGGAGAAG AGAAGLVGLE EDDEDRVDAR NAASRLATST F
//