ID TGO1_DROME Reviewed; 1430 AA. AC Q9VMA7; Q8SY42; Q9VMA8; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 2. DT 24-JAN-2024, entry version 160. DE RecName: Full=Transport and Golgi organization protein 1 {ECO:0000303|PubMed:16452979}; DE Flags: Precursor; GN Name=Tango1 {ECO:0000312|FlyBase:FBgn0286898}; GN ORFNames=CG11098 {ECO:0000312|FlyBase:FBgn0286898}; 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=Head; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1430. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-865; SER-868; SER-1345; RP SER-1348; SER-1390 AND SER-1392, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16452979; DOI=10.1038/nature04377; RA Bard F., Casano L., Mallabiabarrena A., Wallace E., Saito K., Kitayama H., RA Guizzunti G., Hu Y., Wendler F., Dasgupta R., Perrimon N., Malhotra V.; RT "Functional genomics reveals genes involved in protein secretion and Golgi RT organization."; RL Nature 439:604-607(2006). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=23369713; DOI=10.1016/j.devcel.2012.12.005; RA Lerner D.W., McCoy D., Isabella A.J., Mahowald A.P., Gerlach G.F., RA Chaudhry T.A., Horne-Badovinac S.; RT "A Rab10-dependent mechanism for polarized basement membrane secretion RT during organ morphogenesis."; RL Dev. Cell 24:159-168(2013). CC -!- FUNCTION: Required for protein secretion (PubMed:16452979, CC PubMed:23369713). May participate in cargo loading by binding to COPII CC coat subunits and guiding SH3-bound proteins into a growing carrier CC (PubMed:16452979). At basal transitional ER sites in follicle CC epithelial cells, mediates the exit of basal membrane protein such as CC vkg, LanB1 and Trol, from the endoplasmic reticulum (ER) to basal Golgi CC clusters (PubMed:23369713). {ECO:0000269|PubMed:16452979, CC ECO:0000269|PubMed:23369713}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:16452979, ECO:0000269|PubMed:23369713}; Single-pass CC type I membrane protein {ECO:0000269|PubMed:16452979}. Golgi apparatus, CC trans-Golgi network {ECO:0000269|PubMed:23369713}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in basal membrane CC proteins such as vkg, LanB1 and Trol accumulating in the basal ER. CC {ECO:0000269|PubMed:23369713}. CC -!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL68225.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAL68225.1; Type=Miscellaneous discrepancy; Note=Deletion of 12 residues at position 1268 causing a frameshift.; Evidence={ECO:0000305}; CC Sequence=AAL68225.1; Type=Miscellaneous discrepancy; Note=Deletion of 172 residues at position 924.; Evidence={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; AE014134; AAF52414.2; -; Genomic_DNA. DR EMBL; AE014134; AAF52413.3; -; Genomic_DNA. DR EMBL; BT003314; AAO25074.1; -; mRNA. DR EMBL; AY075391; AAL68225.1; ALT_SEQ; mRNA. DR RefSeq; NP_609058.2; NM_135214.4. DR RefSeq; NP_723198.2; NM_164697.3. DR AlphaFoldDB; Q9VMA7; -. DR SMR; Q9VMA7; -. DR BioGRID; 60084; 7. DR IntAct; Q9VMA7; 1. DR STRING; 7227.FBpp0078925; -. DR TCDB; 9.B.113.1.3; the collagen secretory protein, mia3 (mia3) family. DR iPTMnet; Q9VMA7; -. DR PaxDb; 7227-FBpp0078925; -. DR EnsemblMetazoa; FBtr0079295; FBpp0078925; FBgn0286898. DR EnsemblMetazoa; FBtr0303224; FBpp0292316; FBgn0286898. DR GeneID; 33930; -. DR KEGG; dme:Dmel_CG11098; -. DR UCSC; CG11098-RA; d. melanogaster. DR UCSC; CG11098-RB; d. melanogaster. DR AGR; FB:FBgn0286898; -. DR CTD; 33930; -. DR FlyBase; FBgn0286898; Tango1. DR VEuPathDB; VectorBase:FBgn0286898; -. DR eggNOG; ENOG502QU27; Eukaryota. DR GeneTree; ENSGT00950000182767; -. DR HOGENOM; CLU_005232_0_0_1; -. DR InParanoid; Q9VMA7; -. DR OMA; PNEYYKQ; -. DR OrthoDB; 3045415at2759; -. DR PhylomeDB; Q9VMA7; -. DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-DME-5694530; Cargo concentration in the ER. DR Reactome; R-DME-8957275; Post-translational protein phosphorylation. DR BioGRID-ORCS; 33930; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 33930; -. DR PRO; PR:Q9VMA7; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0286898; Expressed in spermathecum and 24 other cell types or tissues. DR ExpressionAtlas; Q9VMA7; baseline and differential. DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:FlyBase. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase. DR GO; GO:0000137; C:Golgi cis cisterna; IDA:FlyBase. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW. DR GO; GO:0007030; P:Golgi organization; IMP:FlyBase. DR GO; GO:0051047; P:positive regulation of secretion; IMP:FlyBase. DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB. DR GO; GO:0033363; P:secretory granule organization; IMP:FlyBase. DR GO; GO:0035459; P:vesicle cargo loading; IBA:GO_Central. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1. DR PANTHER; PTHR23158:SF33; TRANSPORT AND GOLGI ORGANIZATION PROTEIN 1; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9VMA7; DM. PE 1: Evidence at protein level; KW Coiled coil; ER-Golgi transport; Exocytosis; Golgi apparatus; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; SH3 domain; Signal; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..34 FT /evidence="ECO:0000255" FT CHAIN 35..1430 FT /note="Transport and Golgi organization protein 1" FT /id="PRO_0000370510" FT TOPO_DOM 35..796 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 797..817 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 818..1430 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 50..112 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 252..272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 284..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 445..524 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 568..673 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1105..1126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1312..1430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 494..620 FT /evidence="ECO:0000255" FT COILED 869..1245 FT /evidence="ECO:0000255" FT COMPBIAS 284..298 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..356 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 451..465 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 498..524 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 568..586 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..625 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..654 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1312..1330 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1333..1348 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1368..1383 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1384..1406 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 865 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 868 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 1345 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 1348 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 1390 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 1392 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" SQ SEQUENCE 1430 AA; 159052 MW; FCF9988A95979349 CRC64; MRLTNEKATM QPQLSDLALV LGLLICCLPT LTWAATLSDK RLCADPKCEQ IISMGIAKIT YAIGGEGLIS FKINSPIRVL SKSAGSNMQL WGVDINGRRG YANKDFIMEK KILVRDKDLL YEVPVVGPGS PVQSVETPVQ SVETTVQPVL NASESTDDLA TTTTSPLEIA VDSIVVEHDK LQDQQVPDPT AASKAQVQVI EGTELPLEAI AATTEGSIVP ETAADPQEAT NLDSTVVDTK EPQALNSEAI KLQEEPKAQQ PATEAEKPPP LPQAINAELE DADDFDYGDD ETDDDSQQGS QDNESIVEIA NDNKSINESI ELKPLSVAQL KKTDKVEDSK DETKEKHAEM EVSKQEDSSL PTETLNVTAL EEQIDQKEFP KQVLDAAVEL KSSDPLPVEE VTETVAEPPR TIVEDKINEE IVPVSAKIQA KPATVNPTEP IVAQSDAEIK APSESVISST TPAPVVEEAP QKADPVGLPP LFEKKNFENP NNYYKQLQEE QEKQRLVAEA EEQKRLQEEA DQQKRLQEEA ALNKRLLEEA EQQKRLQEEA EQQKRLQEEA ELNKRLLEEA EKQKRLHEES EQLQRSSEEA EPQLSVQEAN MQQLNDSVDS QSNEIVDNNN RQQPEQYQQH HHHTESAFNH PSTASHTTPT PDAESPYAAV QEETTEASQT DNHREGVGYV EPVALPATAS PVSEVPIKED AAGFGLFATI VDTVNNFIGK DPQSDPADSS DELHRILYPG RPEVPPSQRK AEDFAPADVD GYCARFQAKD EHCHRSISLD NFVEVMADKL VDHSQLLLCV VIAAISSLFF MFAYYCFCNS SQEGALLSKL NHLERSLLAS HKENLIIKHD LMTTRTKLAS IEDNSFGSND MVADLKKQLE SELYEKAKLQ EQVGSLERDL DNAAEAGLEL NKMLSEVLNG QNGDEAFMST VDELQRQLND QEKIIIEINN SLAEKSRENS ELQYTFTEAT TRLNSELKTL QEDNYELEME KSKLQTRLQE IQAETESELA KALEARNYEM QKLQNQIVEL TVKWEREHGD LQTSLAKIEA LEDCLKAVGK DAIHNVQELI TSAKTRGELN AVHKKLVELQ SKVEQEEAHK QRLESQLQQS SQDVEQLKQD FNQSERDKLE AQTRLEVLSG YFREKENDLK KELSLQETKW LQHQGENAST VETQTLMKNE IQTLKSQNDE LRAEIEAQIA SHKAQMGTLE NRAHESWLAA RQSERRCEEA LAEAASLRRK LTTMASGGGG VGGDPGVMEA IAANGTSVLG AELKTAPSPL PLPGSPLLNM PNPLPFLAAP FSPFMGLPPP FLPPTGAGGA RPPPLGRMRS PPPSSRGDRD RERYSDYSDY DDYDDDEEDD RGMDRRRRHS GSWGRRHRGS YSHSPRTYRS LSPSDSRYNY NDTETDFSPP PSPPPVPSGR SATSRPYSEV //