S1C2A_RAT
ID S1C2A_RAT Reviewed; 296 AA.
AC Q9WUW9; Q569D0; Q642G8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sulfotransferase 1C2A;
DE Short=ST1C2A;
DE Short=rSULT1C2A {ECO:0000303|PubMed:10872834};
DE EC=2.8.2.1 {ECO:0000269|PubMed:10872834};
DE AltName: Full=Sulfotransferase K2;
GN Name=Sult1c2a; Synonyms=Sultk2;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=10872834; DOI=10.1006/bbrc.2000.2744;
RA Xiangrong L., Joehnk C., Hartmann D., Schestag F., Kroemer W.,
RA Gieselmann V.;
RT "Enzymatic properties, tissue-specific expression, and lysosomal location
RT of two highly homologous rat SULT1C2 sulfotransferases.";
RL Biochem. Biophys. Res. Commun. 272:242-250(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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: 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:10872834}.
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:10872834};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O46503}.
CC Lysosome {ECO:0000269|PubMed:10872834}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and at lower levels in
CC stomach and liver. More specifically found in the epithelia of proximal
CC tubules of the kidney, of the bile duct, of the gastric mucosa, and in
CC hepatocytes. {ECO:0000269|PubMed:10872834}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AJ238392; CAB41461.1; -; mRNA.
DR EMBL; BC081691; AAH81691.1; -; mRNA.
DR EMBL; BC092564; AAH92564.1; -; mRNA.
DR PIR; JC7283; JC7283.
DR RefSeq; NP_001013195.2; NM_001013177.2.
DR AlphaFoldDB; Q9WUW9; -.
DR SMR; Q9WUW9; -.
DR STRING; 10116.ENSRNOP00000058580; -.
DR iPTMnet; Q9WUW9; -.
DR PhosphoSitePlus; Q9WUW9; -.
DR PRIDE; Q9WUW9; -.
DR Ensembl; ENSRNOT00000061861; ENSRNOP00000058577; ENSRNOG00000042111.
DR GeneID; 316153; -.
DR KEGG; rno:316153; -.
DR UCSC; RGD:1305885; rat.
DR CTD; 316153; -.
DR RGD; 1305885; Sult1c2a.
DR GeneTree; ENSGT00940000160912; -.
DR InParanoid; Q9WUW9; -.
DR OrthoDB; 780670at2759; -.
DR BRENDA; 2.8.2.1; 5301.
DR PRO; PR:Q9WUW9; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
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; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Sulfotransferase 1C2A"
FT /id="PRO_0000085136"
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 CONFLICT 22
FT /note="M -> R (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="P -> S (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="N -> D (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="V -> F (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="P -> I (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Y -> F (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="W -> C (in Ref. 1; CAB41461)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="I -> M (in Ref. 2; AAH92564)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="P -> L (in Ref. 2; AAH92564)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="M -> L (in Ref. 2; AAH92564)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34859 MW; FB14A27E39EE847F CRC64;
MALAPELSRQ TKLKEVAGIP LMDPTVNNWS QIQTFKAKPD DLLICTYPKS GTTWIQEIVN
MIEQNGDVEK CQRTIIQHRH PVIEWARPPQ PSGVDKANAM PAPRILRTHL PPQLLPPSFW
TNNCKYLYVA RNAKDCMVSY YHFYRMCQVL PNPGTWNEYF ETFINGKVSW GSWFDHVKGW
WEIRDRYQIL FLFYEDMKRD PKREIQKVMQ FMGKNLDEEV VDKIVLETSF EKMKDNPLTN
FSTIPKTIMD QSISPFMRKG IVGDWKNHFT VAQNERFDEI YEQKMDGTSL NFCMEL
