ST1C1_MOUSE
ID ST1C1_MOUSE Reviewed; 304 AA.
AC Q80VR3; O70262;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sulfotransferase 1C1;
DE Short=ST1C1;
DE EC=2.8.2.-;
DE AltName: Full=Phenol sulfotransferase;
GN Name=Sult1c1 {ECO:0000312|MGI:MGI:102928};
GN Synonyms=Sult1a2 {ECO:0000312|MGI:MGI:102928};
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] {ECO:0000305, ECO:0000312|EMBL:AAC17740.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC STRAIN=ddY {ECO:0000312|EMBL:AAC17740.1};
RX PubMed=9560327; DOI=10.1042/bj3310953;
RA Tamura H.O., Harada Y., Miyawaki A., Mikoshiba K., Matsui M.;
RT "Molecular cloning and expression of a cDNA encoding an olfactory-specific
RT mouse phenol sulphotransferase.";
RL Biochem. J. 331:953-958(1998).
RN [2] {ECO:0000312|EMBL:AAH45149.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH45149.1};
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 [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8641270; DOI=10.1002/j.1460-2075.1996.tb00558.x;
RA Miyawaki A., Homma H., Tamura H., Matsui M., Mikoshiba K.;
RT "Zonal distribution of sulfotransferase for phenol in olfactory
RT sustentacular cells.";
RL EMBO J. 15:2050-2055(1996).
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. Shows activity
CC towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).
CC Also shows activity towards cinnamyl alcohol at pH 6.4 but not at pH
CC 5.5, and towards a number of phenolic odorants including eugenol,
CC guaiacol and 2-naphthol. {ECO:0000269|PubMed:9560327}.
CC -!- ACTIVITY REGULATION: Inhibited by 2,6-dichloro-4-nitrophenol but not by
CC triethylamine or tetra-n-butyl-ammonium chloride.
CC {ECO:0000269|PubMed:9560327}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.36 uM for 2-naphthol {ECO:0000269|PubMed:9560327};
CC KM=3.15 uM for guaiacol {ECO:0000269|PubMed:9560327};
CC KM=2.60 uM for N-hydroxy-2-acetylamino-fluorene
CC {ECO:0000269|PubMed:9560327};
CC Vmax=36.1 nmol/min/mg enzyme toward 2-naphthol
CC {ECO:0000269|PubMed:9560327};
CC Vmax=40.7 nmol/min/mg enzyme toward guaiacol
CC {ECO:0000269|PubMed:9560327};
CC Vmax=0.709 nmol/min/mg enzyme toward N-hydroxy-2-acetylamino-fluorene
CC {ECO:0000269|PubMed:9560327};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8641270}.
CC -!- TISSUE SPECIFICITY: Expressed only in olfactory tissue. Detected in
CC sustentacular cells in the dorso-medial portion of the nasal cavity.
CC {ECO:0000269|PubMed:8641270, ECO:0000269|PubMed:9560327}.
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; AF033653; AAC17740.1; -; mRNA.
DR EMBL; BC045149; AAH45149.1; -; mRNA.
DR CCDS; CCDS28884.1; -.
DR RefSeq; NP_061221.2; NM_018751.2.
DR AlphaFoldDB; Q80VR3; -.
DR SMR; Q80VR3; -.
DR STRING; 10090.ENSMUSP00000024738; -.
DR iPTMnet; Q80VR3; -.
DR PhosphoSitePlus; Q80VR3; -.
DR jPOST; Q80VR3; -.
DR MaxQB; Q80VR3; -.
DR PaxDb; Q80VR3; -.
DR PeptideAtlas; Q80VR3; -.
DR PRIDE; Q80VR3; -.
DR ProteomicsDB; 258631; -.
DR Antibodypedia; 54777; 63 antibodies from 11 providers.
DR DNASU; 20888; -.
DR Ensembl; ENSMUST00000024738; ENSMUSP00000024738; ENSMUSG00000023943.
DR GeneID; 20888; -.
DR KEGG; mmu:20888; -.
DR UCSC; uc008czv.1; mouse.
DR CTD; 20888; -.
DR MGI; MGI:102928; Sult1c1.
DR VEuPathDB; HostDB:ENSMUSG00000023943; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000160996; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q80VR3; -.
DR OMA; ISHFEVN; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q80VR3; -.
DR TreeFam; TF321745; -.
DR BRENDA; 2.8.2.1; 3474.
DR SABIO-RK; Q80VR3; -.
DR BioGRID-ORCS; 20888; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Sult1c2; mouse.
DR PRO; PR:Q80VR3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80VR3; protein.
DR Bgee; ENSMUSG00000023943; Expressed in olfactory epithelium and 18 other tissues.
DR Genevisible; Q80VR3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; ISO:MGI.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; ISO:MGI.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:MGI.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; ISO:MGI.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:MGI.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IEA:Ensembl.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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; Reference proteome; Transferase.
FT CHAIN 1..304
FT /note="Sulfotransferase 1C1"
FT /id="PRO_0000231634"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 56..61
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
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 133
FT /note="K -> Q (in Ref. 1; AAC17740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 35797 MW; 9CF4A4B63713B977 CRC64;
MPLEKLKDLH LDEQNMQPET REVNGILMSK MMSENWDKIW NFQAKPDDLL IATYAKAGTT
WTQEIVDMIQ NDGDVQKCQR ANTYDRHPFI EWTLPPPLNS GLDLANKMPS PRTLKTHLPV
QMLPPSFWKE NSKIIYVARN AKDCLVSYYY FSRMNKMLPD PGTLGEYIET FKAGKVLWGS
WYDHVKGWWD VKDKHRILYL FYEDMKEDPK REIKKIVKFL EKDISEEVLN KIIHHTSFDV
MKQNPMANYT TLPSSIMDHS ISPFMRKGMP GDWKNYFTVA QSEDFDEDYR KKMAGSTITF
RTEI
