ST1C2_RABIT
ID ST1C2_RABIT Reviewed; 296 AA.
AC O46503;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sulfotransferase 1C2;
DE Short=ST1C2;
DE Short=rabSULT1C2;
DE EC=2.8.2.1 {ECO:0000269|PubMed:10481272};
DE AltName: Full=Sulfotransferase 1C1;
GN Name=SULT1C2; Synonyms=SULT1C1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ALTERNATIVE
RP SPLICING, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RC TISSUE=Stomach;
RX PubMed=10481272; DOI=10.1016/s1357-2725(99)00038-2;
RA Hehonah N., Zhu X., Brix L., Bolton-Grob R., Barnett A., Windmill K.,
RA McManus M.;
RT "Molecular cloning, expression, localisation and functional
RT characterisation of a rabbit SULT1C2 sulfotransferase.";
RL Int. J. Biochem. Cell Biol. 31:869-882(1999).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation.
CC Sulfonates p-nitrophenol, a small phenolic compond. Does not sulfonate
CC steroids, dopamine, acetaminophen, or alpha-naphthol.
CC {ECO:0000269|PubMed:10481272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:10481272};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 mM for p-nitrophenol {ECO:0000269|PubMed:10481272};
CC Vmax=0.39 nmol/min/mg enzyme with p-nitrophenol as substrate
CC {ECO:0000269|PubMed:10481272};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10481272}. Lysosome
CC {ECO:0000250|UniProtKB:Q9WUW8}.
CC -!- TISSUE SPECIFICITY: Found in gastrointestinal tract tissues, liver and
CC kidney. {ECO:0000269|PubMed:10481272}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF026304; AAC00410.1; -; mRNA.
DR RefSeq; NP_001076180.1; NM_001082711.1.
DR AlphaFoldDB; O46503; -.
DR SMR; O46503; -.
DR STRING; 9986.ENSOCUP00000014015; -.
DR PRIDE; O46503; -.
DR GeneID; 100009458; -.
DR KEGG; ocu:100009458; -.
DR CTD; 6819; -.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; O46503; -.
DR OMA; FQRMNQM; -.
DR OrthoDB; 780670at2759; -.
DR BRENDA; 2.8.2.1; 1749.
DR Proteomes; UP000001811; Unplaced.
DR ExpressionAtlas; O46503; baseline.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0051923; P:sulfation; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lysosome; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1C2"
FT /id="PRO_0000085134"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49..54
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT BINDING 194
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT BINDING 228..233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT BINDING 256..260
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:O00338"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D939"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D939"
SQ SEQUENCE 296 AA; 34572 MW; 4A1089D0F8D4F295 CRC64;
MALATGPGKQ TQLREVEGVP LQAAIVDNWG QIQSFEAKPD DLLICTYPKS GTTWIQEIVD
MIEQNGDVEK CQRALIQHRH PFIEWARPPQ PSGVEKAQAM PSPRILRTHL PTRLLPPSFW
ENNCKFLYVA RNVKDCMVSY YHFQRMNQVL PDPGTWEEYF ETFINGKVAW GSWFEHVKGW
WEVKGRYQIL FLFYEDIKKD PKCEIRKVAQ FMGKHLDETV LDKIVQETSF EKMKDNPMIN
RSTVPKSIMD QSISPFMRKG TVGDWKNHFT VAQSHRLDEL YRKKMEGVSI DFCLEL
