ID A0A068S766_9FUNG Unreviewed; 515 AA.
AC A0A068S766;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Sorting nexin-4 {ECO:0000256|ARBA:ARBA00040748};
DE AltName: Full=Autophagy-related protein 24 {ECO:0000256|ARBA:ARBA00041273};
GN ORFNames=LCOR_08063.1 {ECO:0000313|EMBL:CDH57076.1};
OS Lichtheimia corymbifera JMRC:FSU:9682.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH57076.1, ECO:0000313|Proteomes:UP000027586};
RN [1] {ECO:0000313|EMBL:CDH57076.1, ECO:0000313|Proteomes:UP000027586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA Voigt K.;
RT "Gene expansion shapes genome architecture in the human pathogen
RT Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT terrestrial Mucorales (Mucoromycotina).";
RL Submitted (AUG-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:CDH57076.1}.
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DR EMBL; CBTN010000043; CDH57076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068S766; -.
DR STRING; 1263082.A0A068S766; -.
DR VEuPathDB; FungiDB:LCOR_08063.1; -.
DR OrthoDB; 51972at2759; -.
DR Proteomes; UP000027586; 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 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:UP000027586}.
FT DOMAIN 106..229
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 42..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 264..291
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 420..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 66..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 58901 MW; 2E592B9CCC986BA0 CRC64;
MNDDYENVEW NVHATTDVYT PLAEAQDPLT ALSNSYDAKT FTQESSPLSA NHYYSPPPPP
STTTPVMPTN GSAESLHDDT NSPRSYSIPT PPQNNVDENP PYHAKKMTIQ VTDPQKHSEG
PQGAYISYLV TTMTTVETFA SSHPRPVRRR FQDFVWLHNA LTLEFPACIV PPLPEKHRLE
YIKGDRFGSD FVERRRVGLQ WFLDRIARHP ELQQSQCCRV FLESGDFRND KHMQHVPPTT
SVFESLSDTL LNAFTKIKKP DERFVEMKDT IDKLEDNLNT VERLYSRISK RQTDLQQDYH
SFGMSIQGLA GLETGISQQL HGFSEAVLNY VKAMSEMSHK EDLLFLNDIH ELLAYCNSAK
AVLRARDQKQ VDFEELSAFL HRTIQERERT LHPGRHINGG LNISEIVTDK LNEVRGVNMQ
VSRREKLARL DRKVKELETE VSHSNDVSNA FSNQVLKEYE VFQRAKTDEL KEGLKAYADS
HVTFYEKGVS IWESVLPILE SIQVDEESES NKPST
//
