ST1C1_RAT
ID ST1C1_RAT Reviewed; 304 AA.
AC P50237; Q5M8B5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sulfotransferase 1C1;
DE Short=ST1C1;
DE EC=2.8.2.-;
DE AltName: Full=HAST-I;
DE AltName: Full=N-hydroxyarylamine sulfotransferase;
GN Name=Sult1c1; Synonyms=St1c1;
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], PROTEIN SEQUENCE OF 10-20 AND 28-38, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8227031; DOI=10.1016/s0021-9258(19)74524-4;
RA Nagata K., Ozawa S., Miyata M., Shimada M., Gong D.-W., Yamazoe Y.,
RA Kato R.;
RT "Isolation and expression of a cDNA encoding a male-specific rat
RT sulfotransferase that catalyzes activation of N-hydroxy-2-
RT acetylaminofluorene.";
RL J. Biol. Chem. 268:24720-24725(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8033246; DOI=10.1016/0009-2797(94)90057-4;
RA Yamazoe Y., Nagata K., Ozawa S., Kato R.;
RT "Structural similarity and diversity of sulfotransferases.";
RL Chem. Biol. Interact. 92:107-117(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs,
CC xenobiotic compounds, hormones, and neurotransmitters. May be involved
CC in the activation of carcinogenic hydroxylamines (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Liver. Male >> Female.
CC {ECO:0000269|PubMed:8227031}.
CC -!- DEVELOPMENTAL STAGE: Male specific. Maximum at 9 weeks and maintained
CC in 9-month-old rats. Can be detected at low level in females up to 9-
CC weeK-old rats but then decreases to undetectable level.
CC {ECO:0000269|PubMed:8227031}.
CC -!- INDUCTION: Induced by estrogens and suppressed by androgens.
CC {ECO:0000269|PubMed:8227031}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; L22339; AAA42181.1; -; mRNA.
DR EMBL; BC088125; AAH88125.1; -; mRNA.
DR PIR; A49098; A49098.
DR RefSeq; NP_113920.2; NM_031732.2.
DR AlphaFoldDB; P50237; -.
DR SMR; P50237; -.
DR STRING; 10116.ENSRNOP00000015189; -.
DR iPTMnet; P50237; -.
DR PhosphoSitePlus; P50237; -.
DR PaxDb; P50237; -.
DR PRIDE; P50237; -.
DR GeneID; 65185; -.
DR KEGG; rno:65185; -.
DR UCSC; RGD:3768; rat.
DR CTD; 442038; -.
DR RGD; 3768; Sult1c1.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; P50237; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P50237; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 5301.
DR PRO; PR:P50237; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; NAS:RGD.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISO:RGD.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; ISO:RGD.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:RGD.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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; Direct protein sequencing; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="Sulfotransferase 1C1"
FT /id="PRO_0000085138"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 56..61
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 115..117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 236..241
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 264..268
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CONFLICT 96
FT /note="S -> P (in Ref. 3; AAH88125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 35764 MW; C772B2EA7BD74198 CRC64;
MSLEKMKDLH LGEQDLQPET REVNGILMSK LMSDNWDKIW NFQAKPDDLL IATYAKAGTT
WTQEIVDMIQ NDGDVQKCQR ANTYDRHPFI EWTLPSPLNS GLDLANKMPS PRTLKTHLPV
HMLPPSFWKE NSKIIYVARN AKDCLVSYYY FSRMNKMLPD PGTLGEYIEQ FKAGKVLWGS
WYDHVKGWWD VKDQHRILYL FYEDMKEDPK REIKKIAKFL EKDISEEVLN KIIYHTSFDV
MKENPMANYT TLPSSIMDHS ISPFMRKGMP GDWKNYFTVA QSEDFDEDYR RKMAGSNITF
RTEI
