ID A0A317WHH2_9EURO Unreviewed; 595 AA.
AC A0A317WHH2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN ORFNames=BO94DRAFT_98233 {ECO:0000313|EMBL:PWY85823.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY85823.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY85823.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY85823.1,
RC ECO:0000313|Proteomes:UP000246702};
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}.
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:PWY85823.1}.
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DR EMBL; MSFK01000016; PWY85823.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WHH2; -.
DR STRING; 1450535.A0A317WHH2; -.
DR OrthoDB; 1708746at2759; -.
DR Proteomes; UP000246702; 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 SUPFAM; SSF64268; PX domain; 1.
PE 3: Inferred from homology;
KW Protein transport {ECO:0000256|PIRNR:PIRNR011791};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702};
KW Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT DOMAIN 161..242
FT /note="PX"
FT /evidence="ECO:0000259|Pfam:PF00787"
FT DOMAIN 295..478
FT /note="Sorting nexin/Vps5-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09325"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
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 92..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65496 MW; C0DA9200030A21CD CRC64;
MDYSALSHDP DHPAGTSPWA SPRPTQTTFP ASVTGDIPPA PLPPQDHSPY NSAAESQPTE
GPESQENEND SRDLSERLQS AQLGEAGYAG EQPPYTTQQQ PQYGQQPRSQ LPARYQTGPR
QNARQPAPVY KIQAKVTGLE RTGKKDPILR FDVHTNIPKF RTTQYRDVRR THGEFVKLAD
HLISANPETF VPAVPSPLTP AGAGTEEDEI RVKSSLQRWL NVVLSNDVLT HDDEVVLFVE
SDFGYSPVVR MKQPATGVRR KVLKQFAPPP DDTPELQNAR PTVKMFYLGT MDTSHKVDRV
VKARRGLGLA ESDFGVKLGQ MHVQETHPGL SNAYRKLGKI IQTVGDFHAV QATAEATTLG
DPLSYHSSDA FIVKETLTNR HILLRELIQA QQATRSKRAA ADRLKVSSSV RPDKVDEAIN
ALDEAQSHED YLAKRTQRVT SNLLSEKQRW FARTSSDMLA SLREYTMRQI EAERRTLATL
ESVRPDIRAI DASGGLSRLG RESHPAARRP NLGSSQGPKG DAWSGIPRRS DSLGRSLSGS
FVAPSPTEDD DEVNGQGNGK GRLRSASGVS SIVEEDDDDR LDARNAASRL ATSTF
//
