ID A0A094I4G9_9PEZI Unreviewed; 1064 AA.
AC A0A094I4G9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Sorting nexin MVP1 {ECO:0000256|ARBA:ARBA00014268};
GN ORFNames=V502_03077 {ECO:0000313|EMBL:KFZ20664.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ20664.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ20664.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ20664.1}.
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DR EMBL; JPKE01001198; KFZ20664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094I4G9; -.
DR STRING; 1420915.A0A094I4G9; -.
DR HOGENOM; CLU_288564_0_0_1; -.
DR OrthoDB; 45524at2759; -.
DR Proteomes; UP000029308; 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 CDD; cd03444; Thioesterase_II_repeat1; 1.
DR CDD; cd03445; Thioesterase_II_repeat2; 1.
DR Gene3D; 2.40.160.210; Acyl-CoA thioesterase, double hotdog domain; 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; IPR049450; ACOT8-like_C.
DR InterPro; IPR042171; Acyl-CoA_hotdog.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR029069; HotDog_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 InterPro; IPR049449; TesB_ACOT8-like_N.
DR PANTHER; PTHR47554; SORTING NEXIN MVP1; 1.
DR PANTHER; PTHR47554:SF1; SORTING NEXIN MVP1; 1.
DR Pfam; PF13622; 4HBT_3; 1.
DR Pfam; PF20789; 4HBT_3C; 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 SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
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:UP000029308};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 345..452
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 117178 MW; 1B3C2BF06595B7A9 CRC64;
MSLFGTSPDE SGAASTPAKS RQTLFDDPSP ANGSQSSLFA DDDSTPGGSP WGMPTPKKAS
KGEVISTLLP GGDTPDSYVD VFETVQSTEF GQSGTVDVAG MTRVMNAAKL GADQQARVMN
TIAPAGNSLR RNEFNVFLAL VGLAQEGEDV TLDGVDERRK KLPQPELHNL ATAPEGLPST
SELASKPPQR PATPPTQSVP TPKSRETRPR RESIIDEDPW GSPALHKGHN HGVPQRAPAP
HSTEGAVPRT NGSFEPSERT TSNFTTESVV ESTNGSRESA RESRPTPNNL WYSYDGNSPT
SYTSGLPTGL EPNAFAGGLG DDPHRPPVSQ NRAIGGGGLT GNGVEENILV TLLPEKEGVF
MFQHHNYQVH SPRRGSKVVR RYSDFVWLLD CLHKRYPFRR LPLLPPKRVG ADSTFIEKRR
RGLVRFVNAL VRHPVLNQEQ LVVMFLTVPT ELAVWRKQAT ISVQEEFTGK ALLPGLEDSL
PPTLNELFET TRSGVRKSAE VYINLCTLMD RLAKRNEGLA ADHGRLSTSL MSLTDASHAT
YAIDTNDVPL LNEGLLTTAK HVTDSQSLLQ DEARAWDEGV LEDLKKQRDA LVSMREMFDR
RERYDKDNIP HLEKRIKSNE DKLANLRSRP DGVKPGDIER TTEAILKDKE SIVAQHARGV
FVKECLRDEL TYFQDSQYQN FTPPHLSSSP LTLATMDHAP IPNAETSFAD LMALEKVPGK
DNTYMSKTPA WAAGGSWNSF GGHVYAQACW AAAQEVPEGL VVHSTHGYFT LPGKIDRPYI
YTITHIGDTR YTCQRSISVR QPRRASVRDQ EAQFAITDAD GEMGDVRFHM ICSFKIATPT
LSAHQETNWG QQYNSSLGGK RPADFDICPD IDMPWYEAHI QKFPEHKTFP GLEIRKADCE
PYNKGKPPGE YRQLHYYRRV GEMSRAEPNL HAAAHLYASD RNSLFLVSKA VGFGDRLAKI
ASLGHSVVFH TDADEMLLEG DGWWTQEAWT TRSAGGRGLH ESKMWSPSGV HVATTLQDGL
VKKAEPGTVA MFEGFGEAFN GGDAEEGGPE TSVDRAQLRE SAKL
//
