ID A0A0M9F3B3_FUSLA Unreviewed; 738 AA.
AC A0A0M9F3B3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Sorting nexin MVP1 {ECO:0000256|ARBA:ARBA00014268};
GN ORFNames=FLAG1_01936 {ECO:0000313|EMBL:KPA45112.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA45112.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA45112.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA45112.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for vacuolar protein sorting.
CC {ECO:0000256|ARBA:ARBA00002474}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:KPA45112.1}.
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DR EMBL; JXCE01000017; KPA45112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9F3B3; -.
DR OrthoDB; 45524at2759; -.
DR Proteomes; UP000037904; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; cd07597; BAR_SNX8; 1.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 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; IPR028662; SNX8/Mvp1.
DR InterPro; IPR035704; SNX8/Mvp1_PX.
DR InterPro; IPR045734; Snx8_BAR_dom.
DR PANTHER; PTHR47554; SORTING NEXIN MVP1; 1.
DR PANTHER; PTHR47554:SF1; SORTING NEXIN MVP1; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; 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 Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 359..473
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 81357 MW; 93EE7AB2638CD647 CRC64;
MSLFGSSPTE DSPVLSSPGP ARRGGAGLFD EESASKPSNS LFADDDDSQD SPWDMPTPRK
QQSRADLIRS LLAGSDVPDS YIEIFDTVVR EDGSGGQVTS GGIAKLFATA RLGADAQARI
MSLVAPGGGD IKLGRNEFNV LLALVGLAQE GEIISLDGVD ERRKRLPQPK LAGLTAEPIL
PPVAELSAKP PQTPPKDNPP QQQQTPPAQP QPQPQPKQFR PAMEDPEDDP WGSPDMHKTH
DHGPAKSNGA QRHNTNGHAG FSQTPPTTVI DAPPLTHVAS PPTTSPNSRR QPSTNSVTGP
AGWGYFDGTN PTVGGFGESP TAAAVQNPFA TGPTATPNMQ PPPGLPHHAS SGRVSRGAEE
KVIVTLMPEK EGVFMFQHHN YEISSARRGS KVIRRYSDFV WLLDCLHKRY PFRILPLLPP
KRVGVNGSHL SNDGAFIEKR RRGLARFLNA LIRHPVLNQE QLVVMFLTVP TELSVWRKQA
TISVQDEFTD RALPPGLEDS LPAELEELFS RTRSGVKRSA ELYINVCNIM DRLVKRTEGV
AADHARIAMS LASLTETSED TYSTDTNEVP LLNDGLVAMS KHLRTCQALM EDESRGWDEG
VLEDLKRQRD ALVSVRELFE RRERLDKDNI PYLERRIQTN ESKLTSLRAK PEGMVKAGEI
DRIAENIIKD KESIVQQHNS SIFVKECIRD ELSTFQSTQY LVSRWNQDWA GERVKYAEML
ADNWRRLLDE LEGMPLGD
//
