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Database: UniProt
Entry: E4UT06_ARTGP
LinkDB: E4UT06_ARTGP
Original site: E4UT06_ARTGP 
ID   E4UT06_ARTGP            Unreviewed;       590 AA.
AC   E4UT06;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Vacuolar protein sorting-associated protein 17 {ECO:0000256|PIRNR:PIRNR011791};
GN   ORFNames=MGYG_03625 {ECO:0000313|EMBL:EFR00619.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS989824; EFR00619.1; -; Genomic_DNA.
DR   RefSeq; XP_003173449.1; XM_003173401.1.
DR   AlphaFoldDB; E4UT06; -.
DR   STRING; 535722.E4UT06; -.
DR   GeneID; 10028728; -.
DR   VEuPathDB; FungiDB:MGYG_03625; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_028982_0_0_1; -.
DR   InParanoid; E4UT06; -.
DR   OMA; FYLGTME; -.
DR   OrthoDB; 1708746at2759; -.
DR   Proteomes; UP000002669; 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:UP000002669};
KW   Transport {ECO:0000256|PIRNR:PIRNR011791}.
FT   DOMAIN          166..242
FT                   /note="PX"
FT                   /evidence="ECO:0000259|Pfam:PF00787"
FT   DOMAIN          297..477
FT                   /note="Sorting nexin/Vps5-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09325"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  65210 MW;  4FA24085B4546ECE CRC64;
     MDYSSISNDP DPTDSSPWGS TSPRAARPFS ASSDVPPAFP SQHQSPYTTD HEGPYHHNGE
     GDERVQSPGL SDHPTDSHHV GSPEAQSAYR HDGQPQHQQE YRQQQQQRSQ APSRYQTGAR
     QQPRPNAPKY KLQAKVTALE RTGKKDPVIR FDVHTNIPKF RTTQFRDVRR THSEFIKLGD
     HLISSNPEAL VPAVPPPLTP AGAGTEEDEM RVKASMQRWL NYVCSNDVLM VDDEMILFVE
     SDSGYSPVVR MKQPATGVRR KVIKQFAPPP DDTPELHDAR PVVKLFYLGT MEAGQKVDRV
     VKARRALALA ESDLGVKLGQ MHVQETHAGL ANAYKKLGKI IQTTGDYHAA QGTAEATTLG
     DPLNYHSSDA FIVKETLTNR HILLRELIQA QQAASSKRAA ADRLKASTSV RPDKVDEAIS
     ALDDARGHEE YLLKKTQRVT NNLLQEKRRW FNRTANDLLL SLREYTLREI EAERRTLSTL
     ESVRADIRSI DSSGGLSRLG RESHPAARRA SLASSQGPKG DAWSGVARRG DSLSRSISGS
     FVAPVPEVDD DVNGSIHGTG RRSRSGTIIE EDDDRVDAKN AASRLAASTF
//
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