ID A0A0D2FKE6_9EURO Unreviewed; 704 AA.
AC A0A0D2FKE6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Sorting nexin MVP1 {ECO:0000256|ARBA:ARBA00014268};
GN ORFNames=PV05_00823 {ECO:0000313|EMBL:KIW60619.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW60619.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW60619.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW60619.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-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}.
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DR EMBL; KN847317; KIW60619.1; -; Genomic_DNA.
DR RefSeq; XP_013321204.1; XM_013465750.1.
DR AlphaFoldDB; A0A0D2FKE6; -.
DR STRING; 348802.A0A0D2FKE6; -.
DR GeneID; 25322731; -.
DR HOGENOM; CLU_009058_1_0_1; -.
DR OrthoDB; 45524at2759; -.
DR Proteomes; UP000054342; 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:UP000054342};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 324..439
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77778 MW; 88BA2A321CECC3F6 CRC64;
MSLFGSSPTE TAPLNSKSLF GDESAQTPSA SSLFAEDGGE SPWSMPTPKR NARQNLVKNL
LPATDVPEYY VDAYDVVLNG SERTGVGVSL TAIRSIIQSS NLSEQEQHKI QNFVIPGGQE
SANGVGRSEF NVLLALIGLG QEGEDITLDG VDERRRKLPE PKVGYIDELR SHARPQPSLP
QASKPTPVKP QKPRQESFGN DPTSDPWASP SNNRLPPPST AAHTMASNGL PDDVKSVPNG
IGRTTSIFTT KGDQSSTNSG SPNDTSSGSA GAGWNSYNGS SGGFPAPSTL GGGFGDQGDD
QSNAPGHRPQ ASVSQSITLP PGTGESVTVT MLPEKEGMFL FQHRNYEVKT IRRGSTVVRR
YSDFVWLLDC LQKRYPFRRL PLLPPKRVQV NGTHLSADAA VFLEKRRRGL VRFTNALVQH
PILSQETLVV MFLTVPTELS VWRKQATISV QEEFTGKSLP PTLEDSLPDN LPEIFEEVRA
GVKRSAEIYI NLCILLERLV KRNENIAAEN AKFSTALSHL TEATTATYAI DTNDVPLLNE
GITSTSKHLS TYQTLLDDEA KAWDTGVLED LKAIRDSYVS MRDMFDRRDR YARDNIPQLE
RRIEASEHKL QQLRQKPQGQ VKPGEMEKVE SSIMADKESI VQQHARGVFI KECVRDEIVT
FQTSIYAITR MHQDWSQERV KYAELQASNW RSMVDQLESM PVQD
//
