TPST_DROME
ID TPST_DROME Reviewed; 499 AA.
AC Q9VYB7; Q58CJ7; Q8MM59;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein-tyrosine sulfotransferase;
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60704};
DE AltName: Full=Transport and Golgi organization protein 13;
DE Short=Tango-13;
DE AltName: Full=Tyrosylprotein sulfotransferase {ECO:0000312|FlyBase:FBgn0086674};
GN Name=Tpst {ECO:0000312|FlyBase:FBgn0086674};
GN Synonyms=Tango13 {ECO:0000312|FlyBase:FBgn0086674};
GN ORFNames=CG32632 {ECO:0000312|FlyBase:FBgn0086674};
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 [MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Moore K.L., Sato-Tomomori C.;
RT "Tyrosylprotein sulfotransferase from Drosophila melanogaster.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC motifs of polypeptides (By similarity). Has a role in protein
CC secretion. {ECO:0000250|UniProtKB:O60704, ECO:0000269|PubMed:16452979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine
CC 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein];
CC Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16452979}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16452979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VYB7-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VYB7-2; Sequence=VSP_018999, VSP_019000;
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AY124548; AAM94031.1; -; mRNA.
DR EMBL; AE014298; AAF48286.2; -; Genomic_DNA.
DR EMBL; AY119073; AAM50933.1; -; mRNA.
DR EMBL; BT021950; AAX51655.1; -; mRNA.
DR RefSeq; NP_001096973.1; NM_001103503.2. [Q9VYB7-2]
DR RefSeq; NP_001259519.1; NM_001272590.1. [Q9VYB7-2]
DR RefSeq; NP_001259520.1; NM_001272591.1. [Q9VYB7-1]
DR RefSeq; NP_001259521.1; NM_001272592.1. [Q9VYB7-2]
DR RefSeq; NP_727717.1; NM_167374.3. [Q9VYB7-1]
DR AlphaFoldDB; Q9VYB7; -.
DR SMR; Q9VYB7; -.
DR BioGRID; 58690; 1.
DR IntAct; Q9VYB7; 7.
DR STRING; 7227.FBpp0302581; -.
DR GlyGen; Q9VYB7; 2 sites.
DR PaxDb; Q9VYB7; -.
DR PRIDE; Q9VYB7; -.
DR DNASU; 32312; -.
DR EnsemblMetazoa; FBtr0073803; FBpp0290842; FBgn0086674. [Q9VYB7-1]
DR EnsemblMetazoa; FBtr0113443; FBpp0112355; FBgn0086674. [Q9VYB7-2]
DR EnsemblMetazoa; FBtr0310432; FBpp0302580; FBgn0086674. [Q9VYB7-2]
DR EnsemblMetazoa; FBtr0310433; FBpp0302581; FBgn0086674. [Q9VYB7-1]
DR EnsemblMetazoa; FBtr0333723; FBpp0305872; FBgn0086674. [Q9VYB7-2]
DR GeneID; 32312; -.
DR KEGG; dme:Dmel_CG32632; -.
DR CTD; 32312; -.
DR FlyBase; FBgn0086674; Tpst.
DR VEuPathDB; VectorBase:FBgn0086674; -.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR InParanoid; Q9VYB7; -.
DR OMA; LNDFRQC; -.
DR PhylomeDB; Q9VYB7; -.
DR BRENDA; 2.8.2.20; 1994.
DR BioGRID-ORCS; 32312; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tpst; fly.
DR GenomeRNAi; 32312; -.
DR PRO; PR:Q9VYB7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0086674; Expressed in saliva-secreting gland and 11 other tissues.
DR ExpressionAtlas; Q9VYB7; baseline and differential.
DR Genevisible; Q9VYB7; DM.
DR GO; GO:0005794; C:Golgi apparatus; 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:0008476; F:protein-tyrosine sulfotransferase activity; IDA:FlyBase.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IDA:FlyBase.
DR GO; GO:0009306; P:protein secretion; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026634; TPST.
DR PANTHER; PTHR12788; PTHR12788; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..499
FT /note="Protein-tyrosine sulfotransferase"
FT /id="PRO_0000189833"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..499
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 103..107
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT REGION 362..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 80..84
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 185
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 197
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 240
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 287..296
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 302
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 287
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..158
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 227..235
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT VAR_SEQ 337..346
FT /note="GKPDAWVQDN -> VKGQSNAVGE (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_018999"
FT VAR_SEQ 347..499
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019000"
SQ SEQUENCE 499 AA; 58050 MW; 5412380E9FAD8DC2 CRC64;
MRLPYRNKKV TLWVLFGIIV ITMFLFKFTE LRPTCLFKVD AANELSSQMV RVEKYLTDDN
QRVYSYNREM PLIFIGGVPR SGTTLMRAML DAHPDVRCGQ ETRVIPRILQ LRSHWLKSEK
ESLRLQEAGI TKEVMNSAIA QFCLEIIAKH GEPAPRLCNK DPLTLKMGSY VIELFPNAKF
LFMVRDGRAT VHSIISRKVT ITGFDLSSYR QCMQKWNHAI EVMHEQCRDI GKDRCMMVYY
EQLVLHPEEW MRKILKFLDV PWNDAVLHHE EFINKPNGVP LSKVERSSDQ VIKPVNLEAM
SKWVGQIPGD VVRDMADIAP MLSVLGYDPY ANPPDYGKPD AWVQDNTSKL KANRMLWESK
AKQVLQMSSS EDDNTNTIIN NSNNKDNNNN QYTINKIIPE QHSRQRQHVQ QQHLQQQQQQ
HLQQQQHQRQ QQQQQREEES ESEREAEPDR EQQLLHQKPK DVITIKQLPL AGSNNNNINN
NINNNNNNNN IMEDPMADT
