(data stored in ACNUC7421 zone)

SWISSPROT: MVP1_ASHGO

ID   MVP1_ASHGO              Reviewed;         523 AA.
AC   Q75CC3;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Sorting nexin MVP1;
GN   Name=MVP1; OrderedLocusNames=ACL014C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 355.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016816; AAS51214.2; -; Genomic_DNA.
DR   RefSeq; NP_983390.2; NM_208743.2.
DR   SMR; Q75CC3; -.
DR   STRING; 33169.AAS51214; -.
DR   EnsemblFungi; AAS51214; AAS51214; AGOS_ACL014C.
DR   GeneID; 4619515; -.
DR   KEGG; ago:AGOS_ACL014C; -.
DR   HOGENOM; HOG000000751; -.
DR   InParanoid; Q75CC3; -.
DR   KO; K17922; -.
DR   OMA; FERYKIM; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0097320; P:plasma membrane tubulation; IEA:EnsemblFungi.
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; Phox.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR028662; SNX8/Mvp1.
DR   InterPro; IPR035704; SNX8/Mvp1_PX.
DR   PANTHER; PTHR47554; PTHR47554; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75CC3.
DR   SWISS-2DPAGE; Q75CC3.
KW   Cytoplasm; Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..523
FT                   /note="Sorting nexin MVP1"
FT                   /id="PRO_0000238593"
FT   DOMAIN          141..260
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   BINDING         185
FT                   /note="Phosphatidylinositol 3-phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /note="Phosphatidylinositol 3-phosphate; via amide nitrogen
FT                   and carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /note="Phosphatidylinositol 3-phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /note="Phosphatidylinositol 3-phosphate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  60619 MW;  077E423988F307FC CRC64;
     MMDLDSQELW GRGPSMESPN NAWASVQRTP ADSARTQQIV SPVVRQAESL GSLTLTDSSL
     SAEVKETMRN NYNERKMYEP GTPALEQTVW GAPPSQLDAS ISGLDTSMAP VASQSSMCDE
     LHSEDLENWM NSRRKTYNPL AKNIVVVEEI PEREGILFKH TNYLVKHLVV LPNTNPSSNQ
     TVIRRYSDFN WLQEVLLKKY PFRMIPELPP KKIGAQNADP IFLARRRKGL CRFINLVIMH
     PVLKQDDLVL TFLTVPTDLG SWRKQANYDT TEEFTDQKID KAFISLWHKE LSNQWNKADA
     KIDELLESWI KTSVLVERYE RRMRQVSEER RLLGRVIEEF ADNSVTLYPL EEGTIHDINS
     HISTISKHLN SLADTSKKER QEVEEHLSVK FKTFIDIIIA LKGVFDRYKI MAGNNIAHLQ
     RRVEINMDKL QSMESNPDVK GAEYDKLRQT IQRDKRTIAE QLNRSWLIRK CILEEFVIFQ
     ETQFCITHVF QEWAKMHVKY ANETTESWEK VYANLQDMPL SRS
//

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