TPST2_MOUSE
ID TPST2_MOUSE Reviewed; 376 AA.
AC O88856; Q8CBA8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein-tyrosine sulfotransferase 2;
DE EC=2.8.2.20 {ECO:0000269|PubMed:9733778};
DE AltName: Full=Tyrosylprotein sulfotransferase 2;
DE Short=TPST-2;
GN Name=Tpst2; Synonyms=D5ucla3;
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], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=9733778; DOI=10.1074/jbc.273.38.24770;
RA Ouyang Y.-B., Moore K.L.;
RT "Molecular cloning and expression of human and mouse tyrosylprotein
RT sulfotransferase-2 and a tyrosylprotein sulfotransferase homologue in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 273:24770-24774(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; 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).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
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:9733778}.
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:9733778};
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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9733778}.
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; AF049890; AAC36060.1; -; mRNA.
DR EMBL; AK036436; BAC29428.1; -; mRNA.
DR EMBL; AK075672; BAC35887.1; -; mRNA.
DR EMBL; BC003721; AAH03721.1; -; mRNA.
DR RefSeq; NP_001313519.1; NM_001326590.1.
DR RefSeq; NP_033445.2; NM_009419.4.
DR AlphaFoldDB; O88856; -.
DR SMR; O88856; -.
DR STRING; 10090.ENSMUSP00000031287; -.
DR GlyGen; O88856; 2 sites.
DR iPTMnet; O88856; -.
DR PhosphoSitePlus; O88856; -.
DR MaxQB; O88856; -.
DR PaxDb; O88856; -.
DR PeptideAtlas; O88856; -.
DR PRIDE; O88856; -.
DR ProteomicsDB; 259172; -.
DR Antibodypedia; 10022; 202 antibodies from 27 providers.
DR DNASU; 22022; -.
DR Ensembl; ENSMUST00000031287; ENSMUSP00000031287; ENSMUSG00000029344.
DR Ensembl; ENSMUST00000071455; ENSMUSP00000071399; ENSMUSG00000029344.
DR GeneID; 22022; -.
DR KEGG; mmu:22022; -.
DR CTD; 8459; -.
DR MGI; MGI:1309516; Tpst2.
DR VEuPathDB; HostDB:ENSMUSG00000029344; -.
DR eggNOG; KOG3988; Eukaryota.
DR InParanoid; O88856; -.
DR OrthoDB; 671992at2759; -.
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; 22022; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tpst2; mouse.
DR PRO; PR:O88856; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O88856; protein.
DR Bgee; ENSMUSG00000029344; Expressed in adrenal gland and 245 other tissues.
DR ExpressionAtlas; O88856; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:MGI.
DR GO; GO:0008476; F:protein-tyrosine sulfotransferase activity; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0006478; P:peptidyl-tyrosine sulfation; IMP:MGI.
DR GO; GO:0060468; P:prevention of polyspermy; IMP:MGI.
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..376
FT /note="Protein-tyrosine sulfotransferase 2"
FT /id="PRO_0000189830"
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:0000269|PubMed:19349973"
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"
FT CONFLICT 89
FT /note="A -> S (in Ref. 2; BAC29428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42067 MW; E714C7DE3D8718D0 CRC64;
MRLSVRKVLL AAGCALALVL AVQLGQQVLE CRAVLGGTRN PRRMRPEQEE LVMLGADHVE
YRYGKAMPLI 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
