TPST1_RAT
ID TPST1_RAT Reviewed; 370 AA.
AC Q3KR92;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein-tyrosine sulfotransferase 1;
DE EC=2.8.2.20 {ECO:0000269|PubMed:9501187};
DE AltName: Full=Tyrosylprotein sulfotransferase 1;
DE Short=TPST-1;
GN Name=Tpst1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC
RP ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9501187; DOI=10.1073/pnas.95.6.2896;
RA Ouyang Y.-B., Lane W.S., Moore K.L.;
RT "Tyrosylprotein sulfotransferase: purification and molecular cloning of an
RT enzyme that catalyzes tyrosine O-sulfation, a common posttranslational
RT modification of eukaryotic proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2896-2901(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:0000269|PubMed:9501187}.
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:0000269|PubMed:9501187};
CC -!- SUBUNIT: Homodimer. Can also form heterodimers with TPST2.
CC {ECO:0000250|UniProtKB:O60507}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:9501187}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:9501187}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60507}.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; BC105826; AAI05827.1; -; mRNA.
DR RefSeq; NP_001011903.2; NM_001011903.2.
DR RefSeq; XP_008767355.1; XM_008769133.2.
DR AlphaFoldDB; Q3KR92; -.
DR SMR; Q3KR92; -.
DR IntAct; Q3KR92; 1.
DR STRING; 10116.ENSRNOP00000060104; -.
DR GlyGen; Q3KR92; 2 sites.
DR PaxDb; Q3KR92; -.
DR Ensembl; ENSRNOT00000001200; ENSRNOP00000001200; ENSRNOG00000000900.
DR GeneID; 288617; -.
DR KEGG; rno:288617; -.
DR CTD; 8460; -.
DR RGD; 1308473; Tpst1.
DR eggNOG; KOG3988; Eukaryota.
DR InParanoid; Q3KR92; -.
DR OMA; LNDFRQC; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; Q3KR92; -.
DR TreeFam; TF312910; -.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-RNO-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR PRO; PR:Q3KR92; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000900; Expressed in liver and 20 other tissues.
DR ExpressionAtlas; Q3KR92; baseline and differential.
DR Genevisible; Q3KR92; RN.
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:0042803; F:protein homodimerization activity; ISO:RGD.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Protein-tyrosine sulfotransferase 1"
FT /id="PRO_0000253722"
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..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 102..106
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60507"
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:O60507"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 192
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 196
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 239
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 286..295
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT BINDING 301
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60507"
FT SITE 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 286
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..157
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 226..234
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 370 AA; 42135 MW; A14A57DD5E62ED2E CRC64;
MVGKLKQNLL LACLVISSVT VFYLGQHAME CHHRIEERSQ PARLENPKAT VRTGLDIKAN
KTFTYHKNMP LIFIGGVPRS GTTLMRAMLD AHPDIRCGEE TRVIPRILAL KQMWSRSSKE
KIRLDEAGVT DEVLDSAMQA FLLEVIVKHG EPAPYLCNKD PFALKSLTYL ARLFPNAKFL
LMVRDGRASV HSMISRKVTI AGFDLNSYRD CLTKWNRAIE TMYNQCMEVG YKKCMLVHYE
QLVLHPERWM RTLLKFLHIP WNHSVLHHEE MIGKAGGVSL SKVERSTDQV IKPVNVGALS
KWVGKIPPDV LQDMAVIAPM LAKLGYDPYA NPPNYGKPDP KILENTRRVH KGEFQLPDFL
KEKPQTEQVE
