ID   MVP1_CRYNB              Reviewed;         612 AA.
AC   P0CR59; Q55R65; Q5KF05;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Sorting nexin MVP1;
GN   Name=MVP1; OrderedLocusNames=CNBF1250;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000030; EAL20314.1; -; Genomic_DNA.
DR   RefSeq; XP_774961.1; XM_769868.1.
DR   AlphaFoldDB; P0CR59; -.
DR   SMR; P0CR59; -.
DR   PRIDE; P0CR59; -.
DR   EnsemblFungi; AAW44126; AAW44126; CNF03550.
DR   EnsemblFungi; EAL20314; EAL20314; CNBF1250.
DR   GeneID; 4936677; -.
DR   KEGG; cnb:CNBF1250; -.
DR   VEuPathDB; FungiDB:CNBF1250; -.
DR   HOGENOM; CLU_009058_1_1_1; -.
DR   Proteomes; UP000001435; Chromosome 6.
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; cd06866; PX_SNX8_Mvp1p_like; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
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; PTHR46571; PTHR46571; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF19566; Snx8_BAR_dom; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Membrane; Protein transport; Transport.
FT   CHAIN           1..612
FT                   /note="Sorting nexin MVP1"
FT                   /id="PRO_0000410291"
FT   DOMAIN          226..334
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          35..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         263
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         265
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         289
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         301
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   612 AA;  67744 MW;  F2959B9C3A1855D1 CRC64;
     MFNAPRPMAS SYSYTDPLSN SAAAGAAFGE LDPWSSAPSP AGSVTPARAT ASASEGRNIA
     ANGNKEEGLN GLINDPPALY VSLLDQLDTS GTGEVSLAAV HRLLGTSKLP AVVVEKIIHL
     TSRDKSTLTR PEFFCALALV SLAQSSPDPN DISIEKLSFS LSNLPLPKLK PSDPPSVSSG
     VAASTAAATG FNAWDGTINK GTTYSANNST FRSTDPMVDN AEDRWWKDQE RIVVTLIPEK
     EGWFLQKYRI ESDKRGEGPV ARRYSDFVWL MDVLEKRYPF RILPPLPPKR INPSSAFLEA
     RRLALIRLLS FLTAHPVLRT DACLNIFLTS SSFESWRKRT PVSTDEESLS KKLTTAQEMS
     IPSDLELKLD NLRERLPAML GHYTRLVVMA ERSLVRLQVQ AAEAARMAMS TQSIGELVPR
     CCWRSVQGDD GESGRGVARE CGLCEGVGRG WGDVGDGWVS VGEELEKGVQ LLQKHIESLK
     SQRDLYSSFH ALFYRHNKLS LDNVDVLRKR VDSRFSKIES LKSAKKPGWE GEVDKLASQS
     DRDTAEIQRL LARRVFVRAC MWHELSVVFH SMQAAQGTMG WKDFVKDQKE RTKRLNGVWQ
     GLEETLESMP LE