GOLP3_MOUSE
ID GOLP3_MOUSE Reviewed; 298 AA.
AC Q9CRA5; A6BLP3; Q99KY1; Q9D636;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Golgi phosphoprotein 3;
DE AltName: Full=Coat protein GPP34;
GN Name=Golph3; Synonyms=Gpp34;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=17629635; DOI=10.1016/j.gene.2007.06.007;
RA Nagano-Ito M., Yoshikawa S., Tamura M., Tsurumaki M., Ichikawa S.;
RT "Identification and characterization of a novel alternative splice variant
RT of mouse GMx33alpha/GPP34.";
RL Gene 400:82-88(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=23345592; DOI=10.1091/mbc.e12-07-0525;
RA Ng M.M., Dippold H.C., Buschman M.D., Noakes C.J., Field S.J.;
RT "GOLPH3L antagonizes GOLPH3 to determine Golgi morphology.";
RL Mol. Biol. Cell 24:796-808(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 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 (By similarity). {ECO:0000250}.
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: [Isoform 2]: Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:17629635}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17629635}; Cytoplasmic side
CC {ECO:0000269|PubMed:17629635}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:17629635}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17629635}; Cytoplasmic side
CC {ECO:0000269|PubMed:17629635}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:17629635}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CRA5-1; Sequence=Displayed;
CC Name=2; Synonyms=GMx33alphaV, GPP34V;
CC IsoId=Q9CRA5-2; Sequence=VSP_037833, VSP_037834;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including brain,
CC heart, kidney, liver, lung, salivary gland, skeletal muscle, small
CC intestine, spleen, stomach, skin and testis (at protein level).
CC {ECO:0000269|PubMed:23345592}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB29486.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB271918; BAF64720.1; -; mRNA.
DR EMBL; AK005996; BAB24357.1; -; mRNA.
DR EMBL; AK014644; BAB29486.1; ALT_FRAME; mRNA.
DR EMBL; AK015543; BAB29889.1; -; mRNA.
DR EMBL; BC003961; AAH03961.1; -; mRNA.
DR EMBL; BC051035; AAH51035.1; -; mRNA.
DR CCDS; CCDS27389.1; -. [Q9CRA5-1]
DR RefSeq; NP_079949.1; NM_025673.2. [Q9CRA5-1]
DR AlphaFoldDB; Q9CRA5; -.
DR SMR; Q9CRA5; -.
DR BioGRID; 211608; 5.
DR IntAct; Q9CRA5; 1.
DR STRING; 10090.ENSMUSP00000057375; -.
DR iPTMnet; Q9CRA5; -.
DR PhosphoSitePlus; Q9CRA5; -.
DR EPD; Q9CRA5; -.
DR MaxQB; Q9CRA5; -.
DR PaxDb; Q9CRA5; -.
DR PeptideAtlas; Q9CRA5; -.
DR PRIDE; Q9CRA5; -.
DR ProteomicsDB; 271030; -. [Q9CRA5-1]
DR ProteomicsDB; 271031; -. [Q9CRA5-2]
DR Antibodypedia; 22696; 296 antibodies from 37 providers.
DR DNASU; 66629; -.
DR Ensembl; ENSMUST00000059680; ENSMUSP00000057375; ENSMUSG00000022200. [Q9CRA5-1]
DR Ensembl; ENSMUST00000226517; ENSMUSP00000153929; ENSMUSG00000022200. [Q9CRA5-2]
DR GeneID; 66629; -.
DR KEGG; mmu:66629; -.
DR UCSC; uc007vhn.1; mouse. [Q9CRA5-1]
DR CTD; 64083; -.
DR MGI; MGI:1913879; Golph3.
DR VEuPathDB; HostDB:ENSMUSG00000022200; -.
DR eggNOG; KOG3983; Eukaryota.
DR GeneTree; ENSGT00390000007153; -.
DR HOGENOM; CLU_036311_0_0_1; -.
DR InParanoid; Q9CRA5; -.
DR OMA; IANWIDL; -.
DR OrthoDB; 1117244at2759; -.
DR PhylomeDB; Q9CRA5; -.
DR TreeFam; TF314360; -.
DR BioGRID-ORCS; 66629; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Golph3; mouse.
DR PRO; PR:Q9CRA5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CRA5; protein.
DR Bgee; ENSMUSG00000022200; Expressed in parotid gland and 248 other tissues.
DR ExpressionAtlas; Q9CRA5; baseline and differential.
DR Genevisible; Q9CRA5; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; ISO:MGI.
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:MGI.
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:MGI.
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 Alternative splicing; Cell membrane; 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_0000123820"
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 MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 84..108
FT /evidence="ECO:0000250"
FT VAR_SEQ 76..81
FT /note="GYTSFW -> VRRGIH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17629635"
FT /id="VSP_037833"
FT VAR_SEQ 82..298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17629635"
FT /id="VSP_037834"
SQ SEQUENCE 298 AA; 33752 MW; 09AC126ED98F6370 CRC64;
MTSLTQRSSG LVQRRTEASR NAADKERAAG GGGGSGEDEA 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
