TPSTB_CAEBR
ID TPSTB_CAEBR Reviewed; 280 AA.
AC A8XLL3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Putative protein-tyrosine sulfotransferase {ECO:0000250|UniProtKB:Q20351};
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60704};
DE AltName: Full=Tyrosylprotein sulfotransferase {ECO:0000250|UniProtKB:Q20351};
DE Short=TPST {ECO:0000250|UniProtKB:Q20351};
GN Name=tpst-2 {ECO:0000312|EMBL:CAP33517.2}; ORFNames=CBG15241;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP33517.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP33517.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE601055; CAP33517.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XLL3; -.
DR SMR; A8XLL3; -.
DR STRING; 6238.CBG15241; -.
DR EnsemblMetazoa; CBG15241.1; CBG15241.1; WBGene00035555.
DR WormBase; CBG15241; CBP27629; WBGene00035555; Cbr-tpst-2.
DR eggNOG; KOG3988; Eukaryota.
DR HOGENOM; CLU_046916_0_0_1; -.
DR InParanoid; A8XLL3; -.
DR OMA; WTHHISG; -.
DR OrthoDB; 671992at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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..280
FT /note="Putative protein-tyrosine sulfotransferase"
FT /id="PRO_0000370219"
FT ACT_SITE 37
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 16..20
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 116
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 124
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 128
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 170
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 215..224
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 91
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..89
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 158..165
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 280 AA; 32285 MW; AD0FE2427BBB7D34 CRC64;
MLSNFEQLIF VGGVPRSGTT LMRAILDAHP DVRCGGETML LPSFLTWQAG WRTDWVNNSG
ITQEVFDDAV SAFITEIIAK HGELAPRLCN KDPYTALWLP TIQRLYPNSK FILMIRDARA
VIHSMIERKV PVAGYNTSDE QSMFVKWNQE IRKMLFQCNN APGQCIKVYY ERLIQKPEEE
IQRITNFLDL QYSQQMLHHH ELIGAEVDLN DQEFSASQVK NSINTKALTS WFDCFSEDTL
RKLDDVAPFL SVLGYDTSSS KPDYSMFADD DFYQFRNFYS
