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Database: UniProt
Entry: T5AD11_OPHSC
LinkDB: T5AD11_OPHSC
Original site: T5AD11_OPHSC 
ID   T5AD11_OPHSC            Unreviewed;       210 AA.
AC   T5AD11;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Endosomal/vacuolar adapter protein YPT35 {ECO:0000256|ARBA:ARBA00033774};
DE   AltName: Full=PX domain-containing protein YPT35 {ECO:0000256|ARBA:ARBA00033785};
GN   ORFNames=OCS_04672 {ECO:0000313|EMBL:EQK99611.1};
OS   Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS   caterpillar fungus) (Hirsutella sinensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK99611.1, ECO:0000313|Proteomes:UP000019374};
RN   [1] {ECO:0000313|EMBL:EQK99611.1, ECO:0000313|Proteomes:UP000019374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC   TISSUE=Fruit-body {ECO:0000313|EMBL:EQK99611.1};
RX   DOI=10.1007/s11434-013-5929-5;
RA   Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA   Liu X., Wang C.;
RT   "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT   fungus.";
RL   Chin. Sci. Bull. 58:2846-2854(2013).
CC   -!- FUNCTION: Recruits the lipid transfer protein VPS13 to endosomal and
CC       vacuolar membranes. {ECO:0000256|ARBA:ARBA00033728}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000256|ARBA:ARBA00004148};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004148}.
CC   -!- SIMILARITY: Belongs to the YPT35 family.
CC       {ECO:0000256|ARBA:ARBA00007426}.
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DR   EMBL; KE653251; EQK99611.1; -; Genomic_DNA.
DR   AlphaFoldDB; T5AD11; -.
DR   eggNOG; ENOG502S5IQ; Eukaryota.
DR   HOGENOM; CLU_070610_1_2_1; -.
DR   Proteomes; UP000019374; Unassembled WGS sequence.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR   CDD; cd07280; PX_YPT35; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR037917; Ypt35_PX.
DR   PANTHER; PTHR45949; SORTING NEXIN-4; 1.
DR   PANTHER; PTHR45949:SF2; SORTING NEXIN-4; 1.
DR   Pfam; PF00787; PX; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   DOMAIN          120..210
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          29..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  22472 MW;  F18CFE479AC6390F CRC64;
     MVSAVDRHRG AAFPGPGAHL DALGIAAAAA PRSTPPATIE TCSDLDSDSD HDDHGVDSSP
     SSHSAAAVMS PPYWIVSSAA PRLNASSLSV DSGPPAGAIT LRDNDTSEHS DRNDACWAKS
     VEVVDSTVVN GSATNIGAFV VWNVRVETLS GSYMTVRKRY SEFDELRAQL TVSFPSFEAA
     MPVLPPKSII SRFRPRFLER RRAGLQYFLK
//
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