ID   MVP1_KLULA              Reviewed;         512 AA.
AC   Q6CUC4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Sorting nexin MVP1;
GN   Name=MVP1; OrderedLocusNames=KLLA0C06006g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01316.1; -; Genomic_DNA.
DR   RefSeq; XP_452465.1; XM_452465.1.
DR   AlphaFoldDB; Q6CUC4; -.
DR   SMR; Q6CUC4; -.
DR   STRING; 28985.XP_452465.1; -.
DR   EnsemblFungi; CAH01316; CAH01316; KLLA0_C06006g.
DR   GeneID; 2892476; -.
DR   KEGG; kla:KLLA0_C06006g; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_009058_2_0_1; -.
DR   InParanoid; Q6CUC4; -.
DR   OMA; YLENKMV; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0097320; P:plasma membrane tubulation; IEA:EnsemblFungi.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:EnsemblFungi.
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..512
FT                   /note="Sorting nexin MVP1"
FT                   /id="PRO_0000238599"
FT   DOMAIN          130..248
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174
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         176
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         200
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         215
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   512 AA;  59656 MW;  BA0B610DFBBF1A02 CRC64;
     MDLEADPWRV NSEENGNNIS GSVWEPDNSS VNALKSYSAD SLQQEANKRV NDDYLGVNIF
     SNGDNIVRGT ASNVYQNDVL WDRPNIGSTT QETDIRGVNR FQATDTPQYA ANDEYKNWVE
     SVRKTYFPLA EDIVSVEEIP EREGLVFKHT NYLVKHLTPL PNTDPSDDRT VVRRYSDFDW
     LQDVLLRKYP FRMVPELPPK KIGSQNADPL FLAKRRKGLS RFINLVMKHP VLRSDDLVLT
     FLTVPTDLSG WRKQAHYDTT DEFTDKHISS SFMNLWRKEF SEQWNKADER IDIALDTWVK
     VTVLIERYEK RMKQVAHERK LLGQILNAIP DTTEALYPQS TATVSQINEG VGLIVEHLNS
     CADVIERENE EVDSGLSVRF KAFIDVIIAL KGLFERYKMM AGNNIPQLQR RVEINQERLN
     TLESNPDVKG AEYDRVKQSI SRDKRSILDQ MNRSWLIREC ILEEFTIFHE TQFLITDCFQ
     RWIEINLRYT NNNVDNWEKI CKKLRDMPLQ RH