TPST1_MOUSE
ID TPST1_MOUSE Reviewed; 370 AA.
AC O70281;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
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:0000250|UniProtKB:O60507}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O60507}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, lung, liver,
CC spleen, kidney, skeletal muscle and testis.
CC {ECO:0000269|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; AF038008; AAC13551.1; -; mRNA.
DR EMBL; BC012666; AAH12666.1; -; mRNA.
DR CCDS; CCDS39293.1; -.
DR RefSeq; NP_001123948.1; NM_001130476.2.
DR RefSeq; NP_038865.1; NM_013837.2.
DR AlphaFoldDB; O70281; -.
DR SMR; O70281; -.
DR STRING; 10090.ENSMUSP00000035614; -.
DR GlyGen; O70281; 2 sites.
DR iPTMnet; O70281; -.
DR PhosphoSitePlus; O70281; -.
DR PaxDb; O70281; -.
DR PeptideAtlas; O70281; -.
DR PRIDE; O70281; -.
DR ProteomicsDB; 259291; -.
DR Antibodypedia; 35330; 160 antibodies from 18 providers.
DR DNASU; 22021; -.
DR Ensembl; ENSMUST00000040721; ENSMUSP00000035614; ENSMUSG00000034118.
DR Ensembl; ENSMUST00000118993; ENSMUSP00000112571; ENSMUSG00000034118.
DR GeneID; 22021; -.
DR KEGG; mmu:22021; -.
DR UCSC; uc008zuc.3; mouse.
DR CTD; 8460; -.
DR MGI; MGI:1298231; Tpst1.
DR VEuPathDB; HostDB:ENSMUSG00000034118; -.
DR eggNOG; KOG3988; Eukaryota.
DR GeneTree; ENSGT00390000006030; -.
DR HOGENOM; CLU_046916_0_1_1; -.
DR InParanoid; O70281; -.
DR OMA; LNDFRQC; -.
DR OrthoDB; 671992at2759; -.
DR PhylomeDB; O70281; -.
DR TreeFam; TF312910; -.
DR BRENDA; 2.8.2.20; 3474.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-MMU-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR BioGRID-ORCS; 22021; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Tpst1; mouse.
DR PRO; PR:O70281; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70281; protein.
DR Bgee; ENSMUSG00000034118; Expressed in vault of skull and 250 other tissues.
DR ExpressionAtlas; O70281; baseline and differential.
DR Genevisible; O70281; MM.
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:MGI.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IDA: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 Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Protein-tyrosine sulfotransferase 1"
FT /id="PRO_0000189827"
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; 42132 MW; 4B85624D23C7800D CRC64;
MVGKLKQNLL LACLVISSVT VFYLGQHAME CHHRIEERSQ PARLENPKAT VRAGLDIKAN
KTFTYHKDMP 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 KILENTRRVY KGEFQLPDFL
KEKPQTEQVE
