TPST1_DANRE
ID TPST1_DANRE Reviewed; 355 AA.
AC Q9PTE6; Q804S9;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein-tyrosine sulfotransferase 1;
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60507};
DE AltName: Full=Tyrosylprotein sulfotransferase 1;
DE Short=TPST-1;
GN Name=tpst1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Moore K.L., Dudley A.A.;
RT "Tyrosylprotein sulfotransferase-1 from Danio rerio.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-256.
RA Kim C.H.;
RT "Isolation of zebrafish tyrosylprotein sulfotransferase 1 cDNA.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic
CC motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as
CC cosubstrate. {ECO:0000250|UniProtKB:O60507}.
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 Evidence={ECO:0000250|UniProtKB:O60507};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O60507}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O60507}.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AF510736; AAO42986.1; -; mRNA.
DR EMBL; BC056786; AAH56786.1; -; mRNA.
DR EMBL; AF204241; AAF18448.1; -; mRNA.
DR RefSeq; NP_571478.1; NM_131403.1.
DR AlphaFoldDB; Q9PTE6; -.
DR SMR; Q9PTE6; -.
DR STRING; 7955.ENSDARP00000101352; -.
DR PaxDb; Q9PTE6; -.
DR Ensembl; ENSDART00000114464; ENSDARP00000101352; ENSDARG00000073872.
DR Ensembl; ENSDART00000181936; ENSDARP00000154770; ENSDARG00000073872.
DR Ensembl; ENSDART00000187438; ENSDARP00000147623; ENSDARG00000073872.
DR GeneID; 30677; -.
DR KEGG; dre:30677; -.
DR CTD; 8460; -.
DR ZFIN; ZDB-GENE-000210-10; tpst1.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_1_1; -.
DR InParanoid; Q9PTE6; -.
DR OMA; LNDFRQC; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; Q9PTE6; -.
DR Reactome; R-DRE-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR PRO; PR:Q9PTE6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000073872; Expressed in granulocyte and 38 other tissues.
DR ExpressionAtlas; Q9PTE6; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; ISS:UniProtKB.
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 Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="Protein-tyrosine sulfotransferase 1"
FT /id="PRO_0000189828"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..355
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 99..103
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 76..80
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 181
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 189
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 235
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 282..291
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 297
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT SITE 156
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 282
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 94..154
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 223..230
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CONFLICT 211
FT /note="K -> R (in Ref. 3; AAF18448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40198 MW; 02F45B99C9C7E502 CRC64;
MIGKLKQNLL VACLVISSVT VFYLCRHAMD CHHRIEERSQ PLLSSLHATL RTGQNLSTPF
IYNKDMPLIF IGGVPRSGTT LMRAMLDAHP DVRCGEETRV IPRILAMKQM WSRSGREKMR
LDEAGVTDEV LDSAMQAFLL EIIVKHGEPA NYLCNKDPFA LKSLTYLAKI FPHAKFILMV
RDGRASVHSM ISRKVTIAGF DLSSYRDCLT KWNRAIETMY TQCLEAADKC LPVHYEQLVL
HPEKWMRTLL RFLNIPWNDA VLHHEELIGK AGGVSLSKVE RSTDQVIKPV NVEALSKWVG
KIPLDVQRDM AVIAPMLARL GYDPHANPPN YGRPDPLVLD NTRRLQKSPE KPNPS
