GOLP3_RAT
ID GOLP3_RAT Reviewed; 298 AA.
AC Q9ERE4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Golgi phosphoprotein 3;
DE AltName: Full=Coat protein GPP34;
DE AltName: Full=Trans-Golgi protein GMx33;
GN Name=Golph3; Synonyms=Gmx33, Gpp34;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11208086; DOI=10.1111/j.1600-0854.2000.11206.x;
RA Wu C.C., Taylor R.S., Lane D.R., Ladinsky M.S., Weisz J.A., Howell K.E.;
RT "GMx33: a novel family of trans-Golgi proteins identified by proteomics.";
RL Traffic 1:963-975(2000).
RN [2]
RP PROTEIN SEQUENCE OF 91-100; 124-138 AND 270-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=16236792; DOI=10.1091/mbc.e05-07-0682;
RA Snyder C.M., Mardones G.A., Ladinsky M.S., Howell K.E.;
RT "GMx33 associates with the trans-Golgi matrix in a dynamic manner and sorts
RT within tubules exiting the Golgi.";
RL Mol. Biol. Cell 17:511-524(2006).
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 Has also been involved in the control of the localization of Golgi
CC enzymes through interaction with their cytoplasmic part. May play an
CC indirect role in cell migration. Has also been involved in the
CC modulation of mTOR signaling. May also be involved in the regulation of
CC mitochondrial lipids biosynthesis.
CC -!- SUBUNIT: Homodimer. Interacts with the coatomer complex. Interacts with
CC MYO18A; the interaction is direct and may link Golgi membranes to the
CC actin cytoskeleton. Interacts with GCNT1; may control its retention in
CC the Golgi. Interacts with VPS35 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion
CC intermembrane space. Cell membrane {ECO:0000250}. Endosome
CC {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and
CC oligomerization participate in the recruitment onto Golgi membranes.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11208086}.
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; AF311954; AAG33623.1; -; mRNA.
DR AlphaFoldDB; Q9ERE4; -.
DR SMR; Q9ERE4; -.
DR STRING; 10116.ENSRNOP00000017276; -.
DR PhosphoSitePlus; Q9ERE4; -.
DR jPOST; Q9ERE4; -.
DR PaxDb; Q9ERE4; -.
DR RGD; 621226; Golph3.
DR eggNOG; KOG3983; Eukaryota.
DR InParanoid; Q9ERE4; -.
DR PhylomeDB; Q9ERE4; -.
DR PRO; PR:Q9ERE4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; ISO:RGD.
DR GO; GO:0060352; P:cell adhesion molecule production; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0072752; P:cellular response to rapamycin; ISS:UniProtKB.
DR GO; GO:0010467; P:gene expression; ISS:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0048194; P:Golgi vesicle budding; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Endosome;
KW Golgi apparatus; Lipid-binding; Membrane; Mitochondrion; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..298
FT /note="Golgi phosphoprotein 3"
FT /id="PRO_0000123821"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..201
FT /note="Beta-hairpin required for oligomerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
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 90
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 171
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 174
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 DISULFID 84..108
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33780 MW; 316112612ABF6374 CRC64;
MTSLTQRSSG LVQRRTEASR NAADKERAAG GGGGNGEDEA QSRRDEQDDD DKGDSKETRL
TLMEEVLLLG LKDREGYTSF WNDCISSGLR GCMLIELALR GRLQLEACGM RRKSLLTRKV
ICKSDAPTGD VLLDEALKHV KETQPPETVQ NWIELLSGET WNPLKLHYQL RNVRERLAKN
LVEKGVLTTE KQNFLLFDMT THPLTNNNIK QRLIKKVQEA VLDKWVNDPH RMDKRLLALI
YLAHASDVLE NAFAPLLDEQ YDLATKRVRQ LLDLDPEVEC LKANTNEVLW AVVAAFTK
