TGO1_DROME
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 03-AUG-2022, entry version 155.
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};
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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; Q9VMA7; -.
DR PRIDE; Q9VMA7; -.
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 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; 332147at2759; -.
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 tissues.
DR ExpressionAtlas; Q9VMA7; baseline and differential.
DR Genevisible; Q9VMA7; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:FlyBase.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR001452; SH3_domain.
DR PROSITE; PS50002; SH3; 1.
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
