TPST2_RAT
ID TPST2_RAT Reviewed; 376 AA.
AC Q5RJS8;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein-tyrosine sulfotransferase 2;
DE EC=2.8.2.20 {ECO:0000250|UniProtKB:O60704};
DE AltName: Full=Tyrosylprotein sulfotransferase 2;
DE Short=TPST-2;
GN Name=Tpst2;
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=Ovary;
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: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 -!- SUBUNIT: Homodimer. Can also form heterodimers with TPST1.
CC {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 -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60704}.
CC -!- MISCELLANEOUS: Substrate peptides must be flexible in order to adopt an
CC L-shaped conformation in the deep binding cleft. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein sulfotransferase family.
CC {ECO:0000305}.
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DR EMBL; BC086518; AAH86518.1; -; mRNA.
DR AlphaFoldDB; Q5RJS8; -.
DR SMR; Q5RJS8; -.
DR STRING; 10116.ENSRNOP00000000831; -.
DR GlyGen; Q5RJS8; 2 sites.
DR PhosphoSitePlus; Q5RJS8; -.
DR PaxDb; Q5RJS8; -.
DR RGD; 1305331; Tpst2.
DR VEuPathDB; HostDB:ENSRNOG00000000664; -.
DR eggNOG; KOG3988; Eukaryota.
DR HOGENOM; CLU_046916_0_1_1; -.
DR InParanoid; Q5RJS8; -.
DR OMA; DSNHVEY; -.
DR PhylomeDB; Q5RJS8; -.
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:Q5RJS8; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000664; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5RJS8; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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: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:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; ISO:RGD.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; ISS:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; ISO:RGD.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..376
FT /note="Protein-tyrosine sulfotransferase 2"
FT /id="PRO_0000253725"
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..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 100..104
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT ACT_SITE 98
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 77..81
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 182
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 190
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 237
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 157
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 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..155
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 224..232
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 376 AA; 42068 MW; C0FE61AF3B46B114 CRC64;
MRLSVRKVLL AVGCALALVL AVQLGQQVLE CRAVLGGVRS PRRMQPEQEE LVMLGADHVE
YRYGKTMPLI FVGGVPRSGT TLMRAMLDAH PEVRCGEETR IIPRVLAMRQ AWTKSGREKL
RLDEAGVTDE VLDAAMQAFI LEVIAKHGEP ARVLCNKDPF TLKSSVYLAR LFPNSKFLLM
VRDGRASVHS MITRKVTIAG FDLSSYRDCL TKWNKAIEVM YAQCMEVGRD KCLPVYYEQL
VLHPRRSLKR ILDFLGIAWS DTVLHHEDLI GKPGGVSLSK IERSTDQVIK PVNLEALSKW
TGHIPRDVVR DMAQIAPMLA RLGYDPYANP PNYGNPDPIV INNTHRVLKG DYKTPANLKG
YFQVNQNSTS PHLGSS
