MVP1_YARLI
ID MVP1_YARLI Reviewed; 605 AA.
AC Q6CHY6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sorting nexin MVP1;
GN Name=MVP1; OrderedLocusNames=YALI0A03443g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382127; CAG83648.1; -; Genomic_DNA.
DR RefSeq; XP_499725.1; XM_499725.1.
DR AlphaFoldDB; Q6CHY6; -.
DR SMR; Q6CHY6; -.
DR STRING; 4952.CAG83648; -.
DR EnsemblFungi; CAG83648; CAG83648; YALI0_A03443g.
DR GeneID; 2906047; -.
DR KEGG; yli:YALI0A03443g; -.
DR VEuPathDB; FungiDB:YALI0_A03443g; -.
DR HOGENOM; CLU_009058_2_0_1; -.
DR InParanoid; Q6CHY6; -.
DR OMA; YLENKMV; -.
DR Proteomes; UP000001300; Chromosome A.
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; 3.30.1520.10; -; 1.
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..605
FT /note="Sorting nexin MVP1"
FT /id="PRO_0000238603"
FT DOMAIN 226..343
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 113..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264
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 266
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 290
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 309
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"
SQ SEQUENCE 605 AA; 68061 MW; 9BAC71F8550D1DD2 CRC64;
MSLFSAATTA VERTGYGSRY DHIFDMFHPI DGRIPAVCYK RLLETINVSG EDKDRLATLA
GSILEGGDGS GGILTSSFTR ESWRAALLLA NVAQDGLPFD DPSQLVNVDT LTPMDFSEEG
ERSSINFSAS TTGRSQTPLF GDDLDDHSIQ SSRSESIIHN NGHSRGHSAL DWNPEEQEAL
QQSQLSQSQL SRSTTPPPLN PQALVPESES GVWTAPPRPD FAPNKADSVT LAIVPEREGM
FLFRHVNYSI SSVSGTDRIT VIRRYSDFSW LQDYLLKKYC FRQVPLLPPK RLAVNGHYLS
SDNYFLERRR RGLTRFINQV LRHPVLGQDE AVRTFVTLRN DISGWKKSVF NTAREEFNGR
TIDPKFVQQW DEQQATALWA GLIVELDRSH DSVVQLCVLL DRVAKRQEAQ AVDSAKIAYN
LGAALPPSAR VLYSVADDGC VQQITRGLSR ASARIETDCQ LQQDEARGSQ VGVLEEAKKY
REALGSMREL FDRLEKYGGN NIPLLEKRIQ QNQGRVTLAR QRKALMSEIE KLDRAIKMDT
EMIAAHKNRT WLIRECITEE IGLFQKTQLQ ISKLLQEFCV DKIKYAELYS DNWGGLDNDV
MDLPV
