ID A0A423WPT5_9PEZI Unreviewed; 607 AA.
AC A0A423WPT5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN ORFNames=VSDG_00360 {ECO:0000313|EMBL:ROW05391.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW05391.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW05391.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW05391.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROW05391.1}.
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DR EMBL; LJZO01000001; ROW05391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WPT5; -.
DR STRING; 252740.A0A423WPT5; -.
DR Proteomes; UP000284375; 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:UP000284375};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR011791}.
FT DOMAIN 184..261
FT /note="PX"
FT /evidence="ECO:0000259|Pfam:PF00787"
FT DOMAIN 319..498
FT /note="Sorting nexin/Vps5-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09325"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..607
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 80..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 66379 MW; 096E4C35D6D5B409 CRC64;
MDYSASIQDA DHPAGASPWG TSPVSSPQAH RTTFSAVAAE PPASPTPFDS QIPRNGFGAA
HDEGGFGAPE HGYERPGTAP SVSESDTQAH TTETAPGPGD PSAGQQQPGS SEDENVSPSR
AHESNRLSGD TTHANQAEHQ VRKPTQPTYK LQAKITGLER AARKDPILRF DVHTNLPNFR
TTQFRDVRRL HSEFVKLAEH LISANPEALV PAVPPPLTSA GAGTDEDEIR VKALMQRWFN
YVCSNEVLAR DDEMVLFVES DFGYSPMIKK KQPATGVRRK LLKQFAPPPD DTPELSDARP
VVKLFYLGSM DAGHKVDKLV KSRLGLSQSE FGVRLGGMHI QEPHQGLANA YRKLGKFVQT
VGDSQQAQAT AEAFTIGDPF QYHSSDAFIV KETLTNRQLL IREFLQAQEN TRGKLNAADR
LKASSNVRRE KVDEAITALD EARQSEAYLY QKTQRVTQNL VHERRKWFAR TTADLRASIR
EFVCKEIEAE RRTLALLENV RPDVRAIDSS GGLSRLGREA HPVVRRTTLA SSQGPKGDAW
SGVPRRTADT MGRSMSGSFM SNVGDEGDGE EEGARSPAGG LLGLGEEDDE DRVDARNAAS
RLATSTF
//