TPSTB_CAEEL
ID TPSTB_CAEEL Reviewed; 259 AA.
AC Q20351; Q8T8N1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative protein-tyrosine sulfotransferase;
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60704};
DE AltName: Full=Tyrosylprotein sulfotransferase;
DE Short=TPST;
GN Name=tpst-2; ORFNames=F42G9.8;
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 [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 [2]
RP IDENTIFICATION.
RX PubMed=9736702; DOI=10.1073/pnas.95.19.11134;
RA Beisswanger R., Corbeil D., Vannier C., Thiele C., Dohrmann U., Kellner R.,
RA Ashman K., Niehrs C., Huttner W.B.;
RT "Existence of distinct tyrosylprotein sulfotransferase genes: molecular
RT characterization of tyrosylprotein sulfotransferase-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11134-11139(1998).
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 -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; FO080196; CCD61891.1; -; Genomic_DNA.
DR PIR; T16350; T16350.
DR RefSeq; NP_497256.1; NM_064855.1.
DR AlphaFoldDB; Q20351; -.
DR SMR; Q20351; -.
DR BioGRID; 50441; 4.
DR IntAct; Q20351; 5.
DR STRING; 6239.F42G9.8; -.
DR PaxDb; Q20351; -.
DR EnsemblMetazoa; F42G9.8.1; F42G9.8.1; WBGene00018365.
DR EnsemblMetazoa; F42G9.8.2; F42G9.8.2; WBGene00018365.
DR GeneID; 185681; -.
DR CTD; 185681; -.
DR WormBase; F42G9.8; CE24966; WBGene00018365; tpst-2.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_0_1; -.
DR InParanoid; Q20351; -.
DR OMA; WTHHISG; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; Q20351; -.
DR PRO; PR:Q20351; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00018365; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IBA:GO_Central.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Reference proteome; Transferase.
FT CHAIN 1..259
FT /note="Putative protein-tyrosine sulfotransferase"
FT /id="PRO_0000189832"
FT ACT_SITE 16
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 95
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 103
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 107
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 149
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 194..203
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 70
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 194
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 13..68
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 137..144
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 259 AA; 29922 MW; 8773576C94130C4F CRC64;
MRAILDAHPD VRCGGETMLL PSFLTWQAGW RNDWVNNSGI TQEVFDDAVS AFITEIVAKH
SELAPRLCNK DPYTALWLPT IRRLYPNAKF ILMIRDARAV VHSMIERKVP VAGYNTSDEI
SMFVQWNQEL RKMTFQCNNA PGQCIKVYYE RLIQKPAEEI LRITNFLDLP FSQQMLRHQD
LIGDEVDLND QEFSASQVKN SINTKALTSW FDCFSEETLR KLDDVAPFLG ILGYDTSISK
PDYSTFADDD FYQFKNFYS
