ID A7EVQ8_SCLS1 Unreviewed; 542 AA.
AC A7EVQ8;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN ORFNames=SS1G_09417 {ECO:0000313|EMBL:EDN93550.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN93550.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476633; EDN93550.1; -; Genomic_DNA.
DR RefSeq; XP_001589695.1; XM_001589645.1.
DR AlphaFoldDB; A7EVQ8; -.
DR STRING; 665079.A7EVQ8; -.
DR EnsemblFungi; EDN93550; EDN93550; SS1G_09417.
DR GeneID; 5485597; -.
DR KEGG; ssl:SS1G_09417; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_028982_0_0_1; -.
DR InParanoid; A7EVQ8; -.
DR OMA; HEPQNEN; -.
DR OrthoDB; 1708746at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IEA:EnsemblFungi.
DR GO; GO:0030905; C:retromer, tubulation complex; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd06891; PX_Vps17p; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR 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 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 PIRSF; PIRSF011791; Vps17; 2.
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:UP000001312};
KW Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT DOMAIN 144..256
FT /note="PX"
FT /evidence="ECO:0000259|SMART:SM00312"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 59176 MW; 1072A0C7E69B0326 CRC64;
MDYSASINDA DNPAGASPWG SSPTSSPQPP RTSTFPSRDI VSPTPYNPDQ SGGAGYPQED
MIGAGGFNRP DSSAGVSVSD VESRRPDTAG STQSDAEAHQ GTGQQYQQQT AQQQQYPAGQ
HRSEPHRYHH SSARQGHHAS APHYKLQAKI TGLERTGRKD PILRFDVHTN LPKFRTTQFR
DVRRTHSEFI KLADHLISSN PEAIVPAVPP ALTSAGAGTD EDEARVKASL QRWLNYVCSN
DVLMRDDEMV LFVESLGLAE SDFGVKLGAM NIQEPHQGLA NAYRKLGKTI QSTGDFHAAQ
GTAEATTIGD PLQYHSQDAF IVKETLTNRH ILLRELIQAQ QLTRSKLNAA DRLKASSSVR
REKVDEAISA LDEARSNEVY LHNKTQRVTA NLLLEKQRWF ARTATDLRLS IREYVIREIE
AERRTLATLE SIRPDIRAID ASGGLSRLGR ESHPAARRAS LAASQGPKGD SWSGVPRRPD
GLNRSISGSF MSTPEGANGE EEGVGRERSL SGSTGGLPGL KEEDDEDRVD ARNAASRLAN
VL
//
