GOLP3_HUMAN
ID GOLP3_HUMAN Reviewed; 298 AA.
AC Q9H4A6; Q9UIW5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Golgi phosphoprotein 3;
DE AltName: Full=Coat protein GPP34;
DE AltName: Full=Mitochondrial DNA absence factor;
DE Short=MIDAS;
GN Name=GOLPH3; Synonyms=GPP34;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11042173; DOI=10.1074/jbc.m006143200;
RA Bell A.W., Ward M.A., Blackstock W.P., Freeman H.N.M., Choudhary J.S.,
RA Lewis A.P., Chotai D., Fazel A., Gushue J.N., Paiement J., Palcy S.,
RA Chevet E., Lafreniere-Roula M., Solari R., Thomas D.Y., Rowley A.,
RA Bergeron J.J.M.;
RT "Proteomics characterization of abundant Golgi membrane proteins.";
RL J. Biol. Chem. 276:5152-5165(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Placenta, and Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-298.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16263763; DOI=10.1242/jcs.02645;
RA Nakashima-Kamimura N., Asoh S., Ishibashi Y., Mukai Y., Shidara Y., Oda H.,
RA Munakata K., Goto Y., Ohta S.;
RT "MIDAS/GPP34, a nuclear gene product, regulates total mitochondrial mass in
RT response to mitochondrial dysfunction.";
RL J. Cell Sci. 118:5357-5367(2005).
RN [7]
RP FUNCTION IN GOLGI MEMBRANE BUDDING, INTERACTION WITH MYO18A, LIPID-BINDING,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-90; ARG-171 AND ARG-174.
RX PubMed=19837035; DOI=10.1016/j.cell.2009.07.052;
RA Dippold H.C., Ng M.M., Farber-Katz S.E., Lee S.K., Kerr M.L.,
RA Peterman M.C., Sim R., Wiharto P.A., Galbraith K.A., Madhavarapu S.,
RA Fuchs G.J., Meerloo T., Farquhar M.G., Zhou H., Field S.J.;
RT "GOLPH3 bridges phosphatidylinositol-4- phosphate and actomyosin to stretch
RT and shape the Golgi to promote budding.";
RL Cell 139:337-351(2009).
RN [8]
RP FUNCTION IN MTOR SIGNALING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP VPS35.
RX PubMed=19553991; DOI=10.1038/nature08109;
RA Scott K.L., Kabbarah O., Liang M.C., Ivanova E., Anagnostou V., Wu J.,
RA Dhakal S., Wu M., Chen S., Feinberg T., Huang J., Saci A., Widlund H.R.,
RA Fisher D.E., Xiao Y., Rimm D.L., Protopopov A., Wong K.K., Chin L.;
RT "GOLPH3 modulates mTOR signalling and rapamycin sensitivity in cancer.";
RL Nature 459:1085-1090(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP FUNCTION IN SECRETION.
RX PubMed=22745132; DOI=10.1074/jbc.m112.346569;
RA Bishe B., Syed G.H., Field S.J., Siddiqui A.;
RT "Role of phosphatidylinositol 4-phosphate (PI4P) and its binding protein
RT GOLPH3 in hepatitis C virus secretion.";
RL J. Biol. Chem. 287:27637-27647(2012).
RN [12]
RP FUNCTION, INTERACTION WITH GCNT1, AND SUBCELLULAR LOCATION.
RX PubMed=23027862; DOI=10.1074/jbc.m112.346528;
RA Ali M.F., Chachadi V.B., Petrosyan A., Cheng P.W.;
RT "Golgi phosphoprotein 3 determines cell binding properties under dynamic
RT flow by controlling Golgi localization of core 2 N-
RT acetylglucosaminyltransferase 1.";
RL J. Biol. Chem. 287:39564-39577(2012).
RN [13]
RP MUTAGENESIS OF ARG-7 AND 14-ARG--ARG-15, AND COATOMER-BINDING.
RX PubMed=22889169; DOI=10.1111/j.1600-0854.2012.01403.x;
RA Tu L., Chen L., Banfield D.K.;
RT "A conserved N-terminal arginine-motif in GOLPH3-family proteins mediates
RT binding to coatomer.";
RL Traffic 13:1496-1507(2012).
RN [14]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=23500462; DOI=10.1016/j.bbrc.2013.03.003;
RA Zhou X., Zhan W., Bian W., Hua L., Shi Q., Xie S., Yang D., Li Y.,
RA Zhang X., Liu G., Yu R.;
RT "GOLPH3 regulates the migration and invasion of glioma cells though RhoA.";
RL Biochem. Biophys. Res. Commun. 433:338-344(2013).
RN [15]
RP INTERACTION WITH MYO18A.
RX PubMed=23990465; DOI=10.1074/jbc.m113.497180;
RA Taft M.H., Behrmann E., Munske-Weidemann L.C., Thiel C., Raunser S.,
RA Manstein D.J.;
RT "Functional Characterization of Human Myosin-18A and its Interaction with
RT F-actin and GOLPH3.";
RL J. Biol. Chem. 288:30029-30041(2013).
RN [16]
RP FUNCTION, INTERACTION WITH MYO18A, SUBCELLULAR LOCATION, AND LIPID-BINDING.
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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 52-298, LIPID-BINDING,
RP OLIGOMERIZATION, DISULFIDE BOND, AND MUTAGENESIS OF TRP-81; ARG-90; ARG-171
RP AND ARG-174.
RX PubMed=20026658; DOI=10.1083/jcb.200909063;
RA Wood C.S., Schmitz K.R., Bessman N.J., Setty T.G., Ferguson K.M.,
RA Burd C.G.;
RT "PtdIns4P recognition by Vps74/GOLPH3 links PtdIns 4-kinase signaling to
RT retrograde Golgi trafficking.";
RL J. Cell Biol. 187:967-975(2009).
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. {ECO:0000269|PubMed:16263763,
CC ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:19837035,
CC ECO:0000269|PubMed:22745132, ECO:0000269|PubMed:23027862,
CC ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23500462}.
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. {ECO:0000269|PubMed:19553991,
CC ECO:0000269|PubMed:19837035, ECO:0000269|PubMed:23027862,
CC ECO:0000269|PubMed:23345592, ECO:0000269|PubMed:23990465}.
CC -!- INTERACTION:
CC Q9H4A6; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-2465479, EBI-714543;
CC Q9H4A6; Q02742: GCNT1; NbExp=6; IntAct=EBI-2465479, EBI-8766035;
CC Q9H4A6; Q92614: MYO18A; NbExp=6; IntAct=EBI-2465479, EBI-949059;
CC Q9H4A6; P13010: XRCC5; NbExp=2; IntAct=EBI-2465479, EBI-357997;
CC Q9H4A6; P12520: vpr; Xeno; NbExp=3; IntAct=EBI-2465479, EBI-6164519;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi
CC network membrane; Peripheral membrane protein; Cytoplasmic side.
CC Mitochondrion intermembrane space. Cell membrane {ECO:0000250}.
CC Endosome {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding
CC and oligomerization participate in the recruitment onto Golgi
CC membranes. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in muscle fibers of patients with
CC mitochondrial diseases; not detected in normal muscle fibers.
CC -!- INDUCTION: Activated by depletion of mitochondrial DNA.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Modulates sensitivity to rapamycin. Tumors expressing
CC this protein are more sensitive to rapamycin in vivo.
CC -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
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DR EMBL; AJ296152; CAC13124.1; -; mRNA.
DR EMBL; AK075156; BAC11438.1; -; mRNA.
DR EMBL; AL356292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012123; AAH12123.1; -; mRNA.
DR EMBL; BC033725; AAH33725.1; -; mRNA.
DR EMBL; BC063586; AAH63586.1; -; mRNA.
DR EMBL; AL133078; CAB61398.1; -; mRNA.
DR CCDS; CCDS3896.1; -.
DR PIR; T42677; T42677.
DR RefSeq; NP_071413.1; NM_022130.3.
DR PDB; 3KN1; X-ray; 2.90 A; A=52-298.
DR PDBsum; 3KN1; -.
DR AlphaFoldDB; Q9H4A6; -.
DR SMR; Q9H4A6; -.
DR BioGRID; 122048; 88.
DR IntAct; Q9H4A6; 46.
DR MINT; Q9H4A6; -.
DR STRING; 9606.ENSP00000265070; -.
DR iPTMnet; Q9H4A6; -.
DR MetOSite; Q9H4A6; -.
DR PhosphoSitePlus; Q9H4A6; -.
DR BioMuta; GOLPH3; -.
DR DMDM; 50400651; -.
DR EPD; Q9H4A6; -.
DR jPOST; Q9H4A6; -.
DR MassIVE; Q9H4A6; -.
DR MaxQB; Q9H4A6; -.
DR PaxDb; Q9H4A6; -.
DR PeptideAtlas; Q9H4A6; -.
DR PRIDE; Q9H4A6; -.
DR ProteomicsDB; 80811; -.
DR Antibodypedia; 22696; 296 antibodies from 37 providers.
DR DNASU; 64083; -.
DR Ensembl; ENST00000265070.7; ENSP00000265070.6; ENSG00000113384.14.
DR GeneID; 64083; -.
DR KEGG; hsa:64083; -.
DR MANE-Select; ENST00000265070.7; ENSP00000265070.6; NM_022130.4; NP_071413.1.
DR UCSC; uc003jhp.2; human.
DR CTD; 64083; -.
DR DisGeNET; 64083; -.
DR GeneCards; GOLPH3; -.
DR HGNC; HGNC:15452; GOLPH3.
DR HPA; ENSG00000113384; Low tissue specificity.
DR MIM; 612207; gene.
DR neXtProt; NX_Q9H4A6; -.
DR OpenTargets; ENSG00000113384; -.
DR PharmGKB; PA28812; -.
DR VEuPathDB; HostDB:ENSG00000113384; -.
DR eggNOG; KOG3983; Eukaryota.
DR GeneTree; ENSGT00390000007153; -.
DR HOGENOM; CLU_036311_0_0_1; -.
DR InParanoid; Q9H4A6; -.
DR OMA; IANWIDL; -.
DR OrthoDB; 1117244at2759; -.
DR PhylomeDB; Q9H4A6; -.
DR TreeFam; TF314360; -.
DR PathwayCommons; Q9H4A6; -.
DR SignaLink; Q9H4A6; -.
DR SIGNOR; Q9H4A6; -.
DR BioGRID-ORCS; 64083; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; GOLPH3; human.
DR EvolutionaryTrace; Q9H4A6; -.
DR GenomeRNAi; 64083; -.
DR Pharos; Q9H4A6; Tbio.
DR PRO; PR:Q9H4A6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H4A6; protein.
DR Bgee; ENSG00000113384; Expressed in secondary oocyte and 207 other tissues.
DR ExpressionAtlas; Q9H4A6; baseline and differential.
DR Genevisible; Q9H4A6; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031985; C:Golgi cisterna; IDA: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; IDA:HPA.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0090164; P:asymmetric Golgi ribbon formation; IMP:CACAO.
DR GO; GO:0060352; P:cell adhesion molecule production; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0072752; P:cellular response to rapamycin; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:CACAO.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0048194; P:Golgi vesicle budding; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IDA: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 3D-structure; Cell membrane; Disulfide bond; Endosome; Golgi apparatus;
KW Lipid-binding; Membrane; Mitochondrion; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..298
FT /note="Golgi phosphoprotein 3"
FT /id="PRO_0000123819"
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:0000305"
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:0000305"
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:0000305"
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:0000305"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT DISULFID 84..108
FT /evidence="ECO:0000269|PubMed:20026658"
FT MUTAGEN 7
FT /note="R->A: Altered binding to coatomer."
FT /evidence="ECO:0000269|PubMed:22889169"
FT MUTAGEN 14..15
FT /note="RR->AA: Loss of binding to coatomer."
FT /evidence="ECO:0000269|PubMed:22889169"
FT MUTAGEN 81
FT /note="W->A: Abolishes phosphoinositide binding and
FT localization to the Golgi apparatus; when associated with
FT A-90."
FT /evidence="ECO:0000269|PubMed:20026658"
FT MUTAGEN 90
FT /note="R->A: Abolishes phosphoinositide binding and
FT localization to the Golgi apparatus; when associated with
FT A-81."
FT /evidence="ECO:0000269|PubMed:19837035,
FT ECO:0000269|PubMed:20026658"
FT MUTAGEN 90
FT /note="R->L: Loss of function in vesicle budding, abolishes
FT phosphoinositide binding and localization to the Golgi
FT apparatus."
FT /evidence="ECO:0000269|PubMed:19837035,
FT ECO:0000269|PubMed:20026658"
FT MUTAGEN 171
FT /note="R->A,L: Abolishes phosphoinositide binding and
FT localization to the Golgi apparatus; when associated with
FT A-174."
FT /evidence="ECO:0000269|PubMed:19837035,
FT ECO:0000269|PubMed:20026658"
FT MUTAGEN 174
FT /note="R->A: Abolishes phosphoinositide binding and
FT localization to the Golgi apparatus; when associated with
FT A-171 or L-171."
FT /evidence="ECO:0000269|PubMed:19837035,
FT ECO:0000269|PubMed:20026658"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 83..99
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3KN1"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3KN1"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:3KN1"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:3KN1"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3KN1"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:3KN1"
SQ SEQUENCE 298 AA; 33811 MW; 34FAD78155CC214A CRC64;
MTSLTQRSSG LVQRRTEASR NAADKERAAG GGAGSSEDDA QSRRDEQDDD DKGDSKETRL
TLMEEVLLLG LKDREGYTSF WNDCISSGLR GCMLIELALR GRLQLEACGM RRKSLLTRKV
ICKSDAPTGD VLLDEALKHV KETQPPETVQ NWIELLSGET WNPLKLHYQL RNVRERLAKN
LVEKGVLTTE KQNFLLFDMT THPLTNNNIK QRLIKKVQEA VLDKWVNDPH RMDRRLLALI
YLAHASDVLE NAFAPLLDEQ YDLATKRVRQ LLDLDPEVEC LKANTNEVLW AVVAAFTK
