ID A0A072PWQ6_9EURO Unreviewed; 488 AA.
AC A0A072PWQ6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Sorting nexin-4 {ECO:0000256|ARBA:ARBA00040748};
DE AltName: Full=Autophagy-related protein 24 {ECO:0000256|ARBA:ARBA00041273};
GN ORFNames=A1O9_04890 {ECO:0000313|EMBL:KEF60040.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF60040.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF60040.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF60040.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF60040.1}.
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DR EMBL; AMGV01000003; KEF60040.1; -; Genomic_DNA.
DR RefSeq; XP_013262630.1; XM_013407176.1.
DR AlphaFoldDB; A0A072PWQ6; -.
DR STRING; 1182545.A0A072PWQ6; -.
DR GeneID; 25279817; -.
DR VEuPathDB; FungiDB:A1O9_04890; -.
DR HOGENOM; CLU_027221_0_0_1; -.
DR OrthoDB; 51972at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd07628; BAR_Atg24p; 1.
DR CDD; cd06863; PX_Atg24p; 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; IPR015404; Vps5_C.
DR PANTHER; PTHR45949; SORTING NEXIN-4; 1.
DR PANTHER; PTHR45949:SF2; SORTING NEXIN-4; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF09325; Vps5; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT DOMAIN 68..190
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 55578 MW; 211F7C661F8618DF CRC64;
MDDHGDFDSV SWQRDDPRQS ESSAPFSHPS DLPTRSASGR RSDSLSSEPQ VGEQADNVDL
AGIGRDGSLE VTVDTPLKEN DGTKDAYVSY LVTTHTDFKS FQKSDFSVRR RFTDFVFLRQ
TLHKDYQACA IPPLPEKNNM AYVRGDRFSN EFTQRRAWSL HRFIKRCTSH PVLRRAPILI
LFLETADWNA QMKLRPSRSN TVGENTNNPA APSGFFDNVA DTMLNAFSKV HKPDKRFIEV
TERANKLDED LSHVEKIIAR VARREGDLEA DYADLANNMR KLTPLEPAIE AQLQTFAGCV
EESSRGWKGL KDHTDQNYLG SLRDMEAYIG SVKSLLKTRE QKQLDFEGLT DYLSKATSER
DMLASSNPYS HGSNLNPATF IRNKVEDIRG VDHETARRER ARKLELKIAE LNREVDGAKG
TSEMFDEQVV REVNDFERIK GLEFRDSLGV LATQHMEFYQ SVISTWERFL VDMDADKHLH
KDKGRAST
//
