MVP1_USTMA
ID MVP1_USTMA Reviewed; 683 AA.
AC Q4PHC3; A0A0D1D130;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sorting nexin MVP1;
GN Name=MVP1; ORFNames=UMAG_00490;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003140; KIS72068.1; -; Genomic_DNA.
DR RefSeq; XP_011386342.1; XM_011388040.1.
DR AlphaFoldDB; Q4PHC3; -.
DR SMR; Q4PHC3; -.
DR STRING; 5270.UM00490P0; -.
DR EnsemblFungi; KIS72068; KIS72068; UMAG_00490.
DR GeneID; 23561775; -.
DR KEGG; uma:UMAG_00490; -.
DR VEuPathDB; FungiDB:UMAG_00490; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_009058_1_1_1; -.
DR InParanoid; Q4PHC3; -.
DR OMA; WEELIWF; -.
DR OrthoDB; 793604at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
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..683
FT /note="Sorting nexin MVP1"
FT /id="PRO_0000238602"
FT DOMAIN 302..418
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 338
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 340
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 364
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 385
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 683 AA; 77206 MW; 1B66D9E79172DA09 CRC64;
MSRHHRPFTW GGAQPGASFS NPTSPTLEAS TFGFEPSVPD IYRRAWILVT KDASAELFAD
TSDADIHLGL LHKLLTSAGG LGPGSAEQIV NSACKGSRCS RSDFYCALGL LHQMQQGEEL
DVHLVQQRLT MGSLSAPVLD LSDATLNPHS HHTFPPTAPS GPSRIDPRPS TFMREMSDPW
NANSSGSYNG IDTRPAYNQY DAMPQQYDTL NSHDSALPAG FAGNVSSGSF ERIKFNAGDD
RRSHQLLAHN QGSSTDTFLA PDRTEARARQ PNTRQERPFS YMSDTAETNA VDAAEDPAAD
LPEDQVTVRL RSELEGFIIK HNVYIVSSSL RKSQVTRRYS DWLWLAECLV KRYPFRCLPV
LPPKRIAMPI AGRHLSADDL FIERRRRGLE RFLRMLTCHP MLREDKLVEV FFTEPRPIAE
WKSSAPALFL DEEGLIKTVD EAERMSIPED LQLKLTQQRQ AIPELLERWT AMVALFERIV
KRNDAAAADY SRLNFSLLSV IETSARRWRP GSDNGKKTEE IMSTMASIFQ DHSDTTSSRV
SAVSLSTLEG MKAQRDLILS FRDLIGRIDR QLVDPIDMLK KRIEASQKRI TTLAASANSN
SASIQQEQAT LSAQVKQDTQ SIQKYLNRRI HAKKTVWEEL IWFHHRFKAV EEDMQKFVRD
ETFFLSTLTR MWEATEMKMK MIR
