MVP1_ASPFU
ID MVP1_ASPFU Reviewed; 729 AA.
AC Q4WZF1; Q876N2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sorting nexin mvp1;
GN Name=mvp1; ORFNames=25d9-1, AFUA_2G17180;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12136012; DOI=10.1093/genetics/161.3.1077;
RA Firon A., Beauvais A., Latge J.-P., Couve E., Grosjean-Cournoyer M.-C.,
RA D'Enfert C.;
RT "Characterization of essential genes by parasexual genetics in the human
RT fungal pathogen Aspergillus fumigatus: impact of genomic rearrangements
RT associated with electroporation of DNA.";
RL Genetics 161:1077-1087(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Required for vacuolar protein sorting. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AY080962; AAM08674.1; -; Genomic_DNA.
DR EMBL; AAHF01000001; EAL94014.1; -; Genomic_DNA.
DR RefSeq; XP_756052.1; XM_750959.1.
DR AlphaFoldDB; Q4WZF1; -.
DR SMR; Q4WZF1; -.
DR STRING; 746128.CADAFUBP00003218; -.
DR EnsemblFungi; EAL94014; EAL94014; AFUA_2G17180.
DR GeneID; 3513397; -.
DR KEGG; afm:AFUA_2G17180; -.
DR VEuPathDB; FungiDB:Afu2g17180; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_009058_1_0_1; -.
DR InParanoid; Q4WZF1; -.
DR OMA; MWHELRV; -.
DR OrthoDB; 793604at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 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; PTHR47554; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..729
FT /note="Sorting nexin mvp1"
FT /id="PRO_0000238594"
FT DOMAIN 356..464
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="E -> K (in Ref. 1; AAM08674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 80642 MW; 0430C2396A6B3271 CRC64;
MSLFGTSPDD PSMGDSVHQR SRSSLFADEP LPGGAGAGNS ANLGSSSLFA DDDGFQSSSP
WNSNANKRAA RHELVKTLLP DADVPESYID AYDLVLNEGD RVGGVVGLTS VREILSSSGL
SASDQAKIFN LVVSGDGDSA NGLGRGQFNV LLALIGLAQE GEDLTFDAVD DRRKKLPLPK
SSYLDRLRDR QQPSAPSHPE ERPTTPPPPP AAINDPPSAR SRQSRETLGG LDADPWGSPQ
LHRGHNHVQT EPEPPVLNGF GSVRSATNAW SSGAGEDETQ HEVPSGLRAN GRTDGAPSTS
SGSGWGGSYR NTTAGDGFGG PIRAGLGNLG APSSGQEEPN ARRRLGIGIS TSSQVEETVT
VNLLPEKEGM FMFQHRNYEV KSSRRGSTVI RRYSDFVWLL DCLQKRYPFR QLPLLPPKRI
AADSNSFLEK RRRGLVRFTN ALVRHPVLSQ EQLVVMFLTV PTELSVWRKQ ATISVQDEFT
GRVLPPDLED SLPANLTDIF ETVRSGVKRS AEIYINLCTL LERLAKRNEG LAADHLRFSL
ALQSLTEVTK DTYAVDTNDV PILNEGIMAT ARHLSNSQSL LEDEARAWEN GILEDLKFQR
DCLVSVREMF DRRDRYARNN IPQLERRIES NERKLEELRT RPQGAVKPGE IEKVEESIFK
DKESIVQQHA RGVFIKECIR DELVHFQRSQ YHISRLHQDW SQERVKYSEL QADNWRSLSD
QVEGMPLGE
