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 03-AUG-2022, entry version 89.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016816; AAS51063.1; -; Genomic_DNA.
DR RefSeq; NP_983239.1; NM_208592.1.
DR AlphaFoldDB; P62583; -.
DR SMR; P62583; -.
DR STRING; 33169.AAS51063; -.
DR EnsemblFungi; AAS51063; AAS51063; AGOS_ACL165C.
DR GeneID; 4619359; -.
DR KEGG; ago:AGOS_ACL165C; -.
DR eggNOG; KOG3983; Eukaryota.
DR HOGENOM; CLU_036311_1_1_1; -.
DR InParanoid; P62583; -.
DR OMA; IANWIDL; -.
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:0000139; C:Golgi membrane; IEA:GOC.
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:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR GO; GO:0035269; P:protein O-linked mannosylation; IEA:EnsemblFungi.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; 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;
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 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..194
FT /note="Beta-hairpin required for oligomerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
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
