ID H6BQM2_EXODN Unreviewed; 488 AA.
AC H6BQM2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Sorting nexin-4 {ECO:0000256|ARBA:ARBA00040748};
DE AltName: Full=Autophagy-related protein 24 {ECO:0000256|ARBA:ARBA00041273};
GN ORFNames=HMPREF1120_02020 {ECO:0000313|EMBL:EHY53839.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY53839.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY53839.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY53839.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH226131; EHY53839.1; -; Genomic_DNA.
DR RefSeq; XP_009154300.1; XM_009156052.1.
DR AlphaFoldDB; H6BQM2; -.
DR STRING; 858893.H6BQM2; -.
DR GeneID; 20306659; -.
DR VEuPathDB; FungiDB:HMPREF1120_02020; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_2_0_1; -.
DR InParanoid; H6BQM2; -.
DR OMA; WSLHRFI; -.
DR OrthoDB; 51972at2759; -.
DR Proteomes; UP000007304; 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:UP000007304}.
FT DOMAIN 66..188
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 392..426
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 55627 MW; 6BAF55D7D44E9732 CRC64;
MDDHGDFDSV SWQREDTQQA ESSAPFQANL PTRPGDGRRS DSMSSEPQAG EHADNVDLAG
IGRDGILEVT VDSPLKENDG TKDAYVSYLV TTHTDFKTFQ KTDFSVRRRF TDFVFLRQTL
HRDYPACAVP PLPEKNNMAY VRGDRFSTEF TQRRACSLHR FLKRCTLHPV LRRAPILLLF
LETTDWNSQM RLRPSRGTVS GEGSGNTAAP TGFFDNVADT MLNAFSKVHK PDKRFIEVTE
RANKLDEDLS HVEKIVARVV RREGDLELDY ADLATNMRKL TPLEPAIEAP IQTFAGCVEE
TSRGWKGLKD HTDQNYLGSL RDMEAYINSV KSLLKTREQK QLDFEGLTEY LQKATAERDM
LASNNPYSHG SHLNPATFIR NKVEDMRGVD HETARKDRAR KLELKIAELN REVESAKSTS
EMFDEQVVRE VADFERIKGL EFRDTLGALA TQHIDFYQNV ISTWERFLVD MDLDADKHLH
KDKGKAET
//