(data stored in ACNUC7421 zone)

SWISSPROT: VPS74_ASHGO

ID   VPS74_ASHGO             Reviewed;         331 AA.
AC   P62583; Q75CT4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Vacuolar protein sorting-associated protein 74;
GN   Name=VPS74; OrderedLocusNames=ACL165C;
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.
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: Phosphatidylinositol-4-phosphate-binding protein that links
CC       Golgi membranes to the cytoskeleton and may participate in the tensile
CC       force required for vesicle budding from the Golgi. Thereby, may play a
CC       role in Golgi membrane trafficking and could indirectly give its
CC       flattened shape to the Golgi apparatus. May also bind to the coatomer
CC       to regulate Golgi membrane trafficking. May play a role in anterograde
CC       transport from the Golgi to the plasma membrane and regulate secretion.
CC       Mediates the cis and medial Golgi localization of mannosyltransferases
CC       through direct binding of their cytosolic domains. Involved in vacuolar
CC       protein sorting (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and
CC       oligomerization participate in the recruitment onto Golgi membranes.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
DR   EMBL; AE016816; AAS51063.1; -; Genomic_DNA.
DR   RefSeq; NP_983239.1; NM_208592.1.
DR   SMR; P62583; -.
DR   STRING; 33169.AAS51063; -.
DR   PRIDE; P62583; -.
DR   EnsemblFungi; AAS51063; AAS51063; AGOS_ACL165C.
DR   GeneID; 4619359; -.
DR   KEGG; ago:AGOS_ACL165C; -.
DR   HOGENOM; HOG000209848; -.
DR   InParanoid; P62583; -.
DR   KO; K15620; -.
DR   OMA; LMKINYQ; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR   GO; GO:0031985; C:Golgi cisterna; IBA:GO_Central.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005797; C:Golgi medial cisterna; IEA:EnsemblFungi.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IEA:EnsemblFungi.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IBA:GO_Central.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR   GO; GO:0048194; P:Golgi vesicle budding; IBA:GO_Central.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IEA:EnsemblFungi.
DR   GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IEA:EnsemblFungi.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR   Gene3D; 1.10.3630.10; -; 1.
DR   InterPro; IPR008628; GPP34-like.
DR   InterPro; IPR038261; GPP34-like_sf.
DR   PANTHER; PTHR12704; PTHR12704; 1.
DR   Pfam; PF05719; GPP34; 1.
PE   3: Inferred from homology;
DR   PRODOM; P62583.
DR   SWISS-2DPAGE; P62583.
KW   Golgi apparatus; Lipid-binding; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..331
FT                   /note="Vacuolar protein sorting-associated protein 74"
FT                   /id="PRO_0000123822"
FT   REGION          183..194
FT                   /note="Beta-hairpin required for oligomerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /note="PtdIns4P"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /note="PtdIns4P"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /note="PtdIns4P"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  37764 MW;  AF97508FE10B75A5 CRC64;
     MSLQRRRVNK TAGNETVGGA SLNRSDEEEG MTHKVAYDPE EQKLRENTRE PTLTLMEEVL
     LMGLKDKEGY LSFLNENISY ALRGCILIEL ALRGRIQVVD DAMRRRFDPS ERLIEVVDGS
     KTGEALLDEA LTLMKGSEPL TIVNWMDLLS GETWNFLKIN YQLRQVRERL AKGLVDKGVL
     RTEMKNFFLF DMPTHPVADT SCKESIKRRI LSVLVPRNVE LQYTELFPET VAFKYLRTIA
     LICSAHGANV LEKVLSTLDY EKRDRGFSRA EELLVQFSQY PFALDKDIET GISVNLNRLV
     QEELDRNPGT ALNLEVVAGV LKVYSRMDDL L
//

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