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 03-AUG-2022, entry version 102.
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}.
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DR EMBL; AE016816; AAS51214.2; -; Genomic_DNA.
DR RefSeq; NP_983390.2; NM_208743.2.
DR AlphaFoldDB; Q75CC3; -.
DR SMR; Q75CC3; -.
DR STRING; 33169.AAS51214; -.
DR EnsemblFungi; AAS51214; AAS51214; AGOS_ACL014C.
DR GeneID; 4619515; -.
DR KEGG; ago:AGOS_ACL014C; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_009058_2_0_1; -.
DR InParanoid; Q75CC3; -.
DR OMA; YLENKMV; -.
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:0042802; F:identical protein binding; 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; 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..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 REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
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 187
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 211
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 226
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 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
