TPSTA_CAEEL
ID TPSTA_CAEEL Reviewed; 380 AA.
AC O77081; Q9NEW9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein-tyrosine sulfotransferase A;
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60704};
DE AltName: Full=Tyrosylprotein sulfotransferase A;
DE Short=TPST-A;
GN Name=tpst-1; ORFNames=Y111B2A.15;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=9733778; DOI=10.1074/jbc.273.38.24770;
RA Ouyang Y.-B., Moore K.L.;
RT "Molecular cloning and expression of human and mouse tyrosylprotein
RT sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 273:24770-24774(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
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:O60704}.
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:O60704};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O60704}.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; AF049709; AAC36062.1; -; mRNA.
DR EMBL; BX284603; CAC35844.1; -; Genomic_DNA.
DR PIR; T42755; T42755.
DR RefSeq; NP_499646.3; NM_067245.3.
DR AlphaFoldDB; O77081; -.
DR SMR; O77081; -.
DR BioGRID; 41862; 1.
DR STRING; 6239.Y111B2A.15; -.
DR iPTMnet; O77081; -.
DR EPD; O77081; -.
DR PaxDb; O77081; -.
DR PeptideAtlas; O77081; -.
DR EnsemblMetazoa; Y111B2A.15.1; Y111B2A.15.1; WBGene00013737.
DR GeneID; 176684; -.
DR KEGG; cel:CELE_Y111B2A.15; -.
DR CTD; 176684; -.
DR WormBase; Y111B2A.15; CE26632; WBGene00013737; tpst-1.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_0_1; -.
DR InParanoid; O77081; -.
DR OMA; LNDFRQC; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; O77081; -.
DR PRO; PR:O77081; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00013737; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0005802; C:trans-Golgi network; IDA:WormBase.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IDA:WormBase.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0032963; P:collagen metabolic process; IMP:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IDA:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0061062; P:regulation of nematode larval development; IMP:WormBase.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="Protein-tyrosine sulfotransferase A"
FT /id="PRO_0000189831"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..380
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 102..106
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT ACT_SITE 100
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 79..83
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 192
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 196
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 284..293
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 299
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 284
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 97..157
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 226..234
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 380 AA; 43314 MW; FF709BF00F1EDC95 CRC64;
MRKNRELLLV LFLVVFILFY FITARTADDP YYSNHREKFN GAAADDGDES LPFHQLTSVR
SDDGYNRTSP FIFIGGVPRS GTTLMRAMLD AHPEVRCGEE TRVIPRILNL RSQWKKSEKE
WNRLQQAGVT GEVINNAISS FIMEIMVGHG DRAPRLCNKD PFTMKSAVYL KELFPNAKYL
LMIRDGRATV NSIISRKVTI TGFDLNDFRQ CMTKWNAAIQ IMVDQCESVG EKNCLKVYYE
QLVLHPEAQM RRITEFLDIP WDDKVLHHEQ LIGKDISLSN VERSSDQVVK PVNLDALIKW
VGTIPEDVVA DMDSVAPMLR RLGYDPNANP PNYGKPDELV AKKTEDVHKN GAEWYKKAVQ
VVNDPGRVDK PIVDNEVSKL
