TPST2_MACFA
ID TPST2_MACFA Reviewed; 377 AA.
AC Q4R863;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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; ORFNames=QtsA-13311;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB168595; BAE00709.1; -; mRNA.
DR RefSeq; XP_005567783.1; XM_005567726.2.
DR RefSeq; XP_015312847.1; XM_015457361.1.
DR AlphaFoldDB; Q4R863; -.
DR SMR; Q4R863; -.
DR STRING; 9541.XP_005567776.1; -.
DR GeneID; 101865653; -.
DR KEGG; mcf:101865653; -.
DR CTD; 8459; -.
DR VEuPathDB; HostDB:ENSMFAG00000000373; -.
DR eggNOG; KOG3988; Eukaryota.
DR OMA; DSNHVEY; -.
DR Proteomes; UP000233100; Chromosome 10.
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:0008476; F:protein-tyrosine sulfotransferase activity; ISS:UniProtKB.
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 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..377
FT /note="Protein-tyrosine sulfotransferase 2"
FT /id="PRO_0000253724"
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..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 101..105
FT /note="Interaction with peptide substrate"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT ACT_SITE 99
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 78..82
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 183
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 191
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 195
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 238
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 285..294
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT BINDING 300
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 158
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT SITE 285
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..156
FT /evidence="ECO:0000250|UniProtKB:O60704"
FT DISULFID 225..233
FT /evidence="ECO:0000250|UniProtKB:O60704"
SQ SEQUENCE 377 AA; 41850 MW; 6448F4D989145582 CRC64;
MRLSVRRVLL AAGCALVLVL AVQLGQQVLE CRAVLAGLRS PRGAMRPEQE ELVMVGTNHV
EYRYGKAMPL IFVGGVPRSG TTLMRAMLDA HPEVRCGEET RIIPRVLAMR QAWSKSGREK
LRLDEAGVTD EVLDAAMQAF ILEVIAKHGE PARVLCNKDP FTLKSSVYLS RLFPNSKFLL
MVRDGRASVH SMITRKVTIA GFDLSSYRDC LTKWNKAIEV MYAQCMEVGK DKCLPVYYEQ
LVLHPRRSLK LILDFLGIAW SDAVLHHEDL IGKPGGVSLS KIERSTDQVI KPVNLEALSK
WTGHIPGDVV RDMAQIAPML AQLGYDPYAN PPNYGNPDPI VVNNTQRVLK GDYKTPANLK
GYFQVNQNST SSHLGSS
