GOLP3_DROME
ID GOLP3_DROME Reviewed; 294 AA.
AC Q9VQ93;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Golgi phosphoprotein 3 homolog sauron {ECO:0000305};
DE AltName: Full=Protein rotini {ECO:0000312|FlyBase:FBgn0267378};
GN Name=sau {ECO:0000312|FlyBase:FBgn0267378};
GN Synonyms=GOLPH3 {ECO:0000312|FlyBase:FBgn0267378},
GN l(2)s5379 {ECO:0000312|FlyBase:FBgn0267378},
GN rti {ECO:0000312|FlyBase:FBgn0267378};
GN ORFNames=CG7085 {ECO:0000312|FlyBase:FBgn0267378};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP LIPID-BINDING.
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 [5]
RP FUNCTION IN TRAFFICKING, DISRUPTION PHENOTYPE, INTERACTION WITH BOTV; EXT2;
RP TTV; VTI1, AND SUBCELLULAR LOCATION.
RX PubMed=23720043; DOI=10.1242/dev.087171;
RA Chang W.L., Chang C.W., Chang Y.Y., Sung H.H., Lin M.D., Chang S.C.,
RA Chen C.H., Huang C.W., Tung K.S., Chou T.B.;
RT "The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan
RT sulfate proteoglycans by modulating the retrograde trafficking of
RT exostosins.";
RL Development 140:2798-2807(2013).
RN [6]
RP FUNCTION, INTERACTION WITH VPS35; RAB5; CHC; RAB11; ZIP; PAV AND SEP1,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-167;
RP ARG-170 AND GLU-273.
RX PubMed=24786584; DOI=10.1371/journal.pgen.1004305;
RA Sechi S., Colotti G., Belloni G., Mattei V., Frappaolo A., Raffa G.D.,
RA Fuller M.T., Giansanti M.G.;
RT "GOLPH3 is essential for contractile ring formation and Rab11 localization
RT to the cleavage site during cytokinesis in Drosophila melanogaster.";
RL PLoS Genet. 10:E1004305-E1004305(2014).
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 (PubMed:19837035,
CC PubMed:24786584). Thereby, may play a role in Golgi membrane
CC trafficking and could indirectly give its flattened shape to the Golgi
CC apparatus (By similarity). May also bind to the coatomer to regulate
CC Golgi membrane trafficking (PubMed:23720043, PubMed:24786584). May play
CC a role in anterograde transport from the Golgi to the plasma membrane
CC and regulate secretion (By similarity). Also involved in the control of
CC the localization of Golgi enzymes through interaction with their
CC cytoplasmic part (By similarity). Functions in cytokinesis by
CC regulating contractile ring formation and vesicle trafficking during
CC cleavage furrow ingression (PubMed:24786584). May also have a role in
CC the intital steps of central spindle formation (PubMed:24786584). Can
CC also bind phosphatidylinositol-3-phosphate and phosphatidylinositol-5-
CC phosphate in vitro (PubMed:24786584). {ECO:0000250|UniProtKB:Q9H4A6,
CC ECO:0000269|PubMed:23720043, ECO:0000269|PubMed:24786584}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with botv, Ext2 and
CC ttv (PubMed:23720043). Interacts with Vti1 (PubMed:23720043). Interacts
CC with Vps35, Rab5, Chc, Rab11, zip, Pav and Sep1 (PubMed:24786584).
CC {ECO:0000250, ECO:0000269|PubMed:23720043,
CC ECO:0000269|PubMed:24786584}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:24786584, ECO:0000305|PubMed:23720043}; Peripheral
CC membrane protein {ECO:0000305|PubMed:23720043}; Cytoplasmic side
CC {ECO:0000305|PubMed:23720043}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:24786584}. Cleavage furrow
CC {ECO:0000269|PubMed:24786584}. Note=Phosphatidylinositol 4-phosphate-
CC binding and oligomerization participate in the recruitment onto Golgi
CC membranes (PubMed:23720043). In dividing cells associates with vesicles
CC in polar regions of the cells during metaphase and anaphase, and
CC localizes to the cleavage furrow during telophase (PubMed:24786584).
CC {ECO:0000269|PubMed:24786584, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Lethal (PubMed:23720043, PubMed:24786584).
CC Embryos display an aberrant pattern of denticles with some additional
CC dorsalization and twisting (PubMed:23720043). It is associated with a
CC defect in heparan sulfate proteoglycan synthesis which in turn alters
CC hedgehog signaling (PubMed:23720043). {ECO:0000269|PubMed:23720043,
CC ECO:0000269|PubMed:24786584}.
CC -!- SIMILARITY: Belongs to the GOLPH3/VPS74 family. {ECO:0000305}.
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DR EMBL; AE014134; AAF51284.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10452.2; -; Genomic_DNA.
DR EMBL; AE014134; AAX53593.1; -; Genomic_DNA.
DR EMBL; AY058532; AAL13761.1; -; mRNA.
DR RefSeq; NP_001014460.1; NM_001014460.3.
DR RefSeq; NP_001027220.1; NM_001032049.2.
DR RefSeq; NP_608658.1; NM_134814.5.
DR AlphaFoldDB; Q9VQ93; -.
DR SMR; Q9VQ93; -.
DR BioGRID; 59630; 19.
DR IntAct; Q9VQ93; 2.
DR STRING; 7227.FBpp0100140; -.
DR PaxDb; Q9VQ93; -.
DR PRIDE; Q9VQ93; -.
DR DNASU; 33402; -.
DR EnsemblMetazoa; FBtr0077840; FBpp0100138; FBgn0267378.
DR EnsemblMetazoa; FBtr0100673; FBpp0100140; FBgn0267378.
DR EnsemblMetazoa; FBtr0100674; FBpp0100141; FBgn0267378.
DR GeneID; 33402; -.
DR KEGG; dme:Dmel_CG7085; -.
DR UCSC; CG7085-RA; d. melanogaster.
DR CTD; 33402; -.
DR FlyBase; FBgn0267378; sau.
DR VEuPathDB; VectorBase:FBgn0267378; -.
DR eggNOG; KOG3983; Eukaryota.
DR GeneTree; ENSGT00390000007153; -.
DR HOGENOM; CLU_036311_0_0_1; -.
DR InParanoid; Q9VQ93; -.
DR OMA; DNQDAMD; -.
DR OrthoDB; 1117244at2759; -.
DR PhylomeDB; Q9VQ93; -.
DR SignaLink; Q9VQ93; -.
DR BioGRID-ORCS; 33402; 3 hits in 3 CRISPR screens.
DR ChiTaRS; sau; fly.
DR GenomeRNAi; 33402; -.
DR PRO; PR:Q9VQ93; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0267378; Expressed in thoracico-abdominal ganglion (Drosophila) and 37 other tissues.
DR ExpressionAtlas; Q9VQ93; baseline and differential.
DR Genevisible; Q9VQ93; DM.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:FlyBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:FlyBase.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:FlyBase.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:FlyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:FlyBase.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:FlyBase.
DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
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:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007110; P:meiosis I cytokinesis; IMP:FlyBase.
DR GO; GO:0007111; P:meiosis II cytokinesis; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:FlyBase.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:FlyBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0007053; P:spindle assembly involved in male meiosis; IMP:FlyBase.
DR GO; GO:0046718; P:viral entry into host cell; HMP:FlyBase.
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 Cytoplasmic vesicle; Golgi apparatus; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..294
FT /note="Golgi phosphoprotein 3 homolog sauron"
FT /id="PRO_0000424384"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..197
FT /note="Beta-hairpin required for oligomerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
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 86
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"
FT BINDING 170
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 MUTAGEN 167
FT /note="K->A: Prevents binding to PI(4)P and abolishes sau
FT localization to the Golgi membranes and cleavage furrow;
FT when associated with L-170."
FT /evidence="ECO:0000269|PubMed:24786584"
FT MUTAGEN 170
FT /note="R->L: Prevents binding to PI(4)P and abolishes sau
FT localization to the Golgi membranes and cleavage furrow;
FT when associated with A-167."
FT /evidence="ECO:0000269|PubMed:24786584"
FT MUTAGEN 273
FT /note="E->K: In Z2217; Impairs cytokinesis. Prevents
FT binding to PI(4)P and PI(5)P."
FT /evidence="ECO:0000269|PubMed:24786584"
SQ SEQUENCE 294 AA; 33511 MW; 7F3C52EE18597B5E CRC64;
MNRSDGLVRR SVKPRENGGA EGGLNANTPD DNQDALDNLK DQEDNIDDGD SKETRLTLME
EVLLLGLKDK EGYTSFWNDC ISSGLRGCIL IELGLRGRVM IEKSGMRRRG LCTRKLILKS
DQQTGDVLLD EALKHIKETD PPETVQSWIE YLSGETWNPL KLRYQLKNVR ERLAKNLVEK
GVLTTEKQNF LLFDMTTHPL SDNVVKCRLV KKIQDSVLSK WVNDPQRMDK RMLALIFLAH
ASDVIENAFA PLNDDDYEVA MKRVRELLDL DFEAESAKPN ANEILWAVFM AFTK
