ST1C2_MOUSE
ID ST1C2_MOUSE Reviewed; 296 AA.
AC Q9D939; Q3UNA9; Q8R210;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sulfotransferase 1C2;
DE Short=ST1C2;
DE EC=2.8.2.1 {ECO:0000269|PubMed:12164856};
GN Name=Sult1c2; Synonyms=Sult1c1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Kidney;
RX PubMed=12164856; DOI=10.1046/j.1523-1755.2002.00512.x;
RA Sugimura K., Tanaka T., Tanaka Y., Takano H., Kanagawa K., Sakamoto N.,
RA Ikemoto S., Kawashima H., Nakatani T.;
RT "Decreased sulfotransferase SULT1C2 gene expression in DPT-induced
RT polycystic kidney.";
RL Kidney Int. 62:757-762(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Gall bladder, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (PubMed:12164856).
CC Does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol
CC (PubMed:12164856). {ECO:0000269|PubMed:12164856}.
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:12164856};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for p-nitrophenol {ECO:0000269|PubMed:12164856};
CC Vmax=20 nmol/min/mg enzyme with p-nitrophenol as substrate
CC {ECO:0000269|PubMed:12164856};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O46503}.
CC Lysosome {ECO:0000250|UniProtKB:Q9WUW8}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stomach and kidney.
CC {ECO:0000269|PubMed:12164856}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AY005469; AAG00823.1; -; mRNA.
DR EMBL; AK007384; BAB25002.1; -; mRNA.
DR EMBL; AK144336; BAE25838.1; -; mRNA.
DR EMBL; BC022665; AAH22665.1; -; mRNA.
DR CCDS; CCDS28883.1; -.
DR RefSeq; NP_081211.3; NM_026935.4.
DR AlphaFoldDB; Q9D939; -.
DR SMR; Q9D939; -.
DR BioGRID; 213218; 1.
DR STRING; 10090.ENSMUSP00000023886; -.
DR iPTMnet; Q9D939; -.
DR PhosphoSitePlus; Q9D939; -.
DR jPOST; Q9D939; -.
DR MaxQB; Q9D939; -.
DR PaxDb; Q9D939; -.
DR PeptideAtlas; Q9D939; -.
DR PRIDE; Q9D939; -.
DR ProteomicsDB; 257082; -.
DR Antibodypedia; 1928; 312 antibodies from 27 providers.
DR DNASU; 69083; -.
DR Ensembl; ENSMUST00000023886; ENSMUSP00000023886; ENSMUSG00000023122.
DR GeneID; 69083; -.
DR KEGG; mmu:69083; -.
DR UCSC; uc008czu.1; mouse.
DR CTD; 6819; -.
DR MGI; MGI:1916333; Sult1c2.
DR VEuPathDB; HostDB:ENSMUSG00000023122; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000160912; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; Q9D939; -.
DR OMA; FQRMNQM; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9D939; -.
DR TreeFam; TF321745; -.
DR Reactome; R-MMU-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; Q9D939; -.
DR BioGRID-ORCS; 69083; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sult1c2; mouse.
DR PRO; PR:Q9D939; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D939; protein.
DR Bgee; ENSMUSG00000023122; Expressed in epithelium of stomach and 63 other tissues.
DR Genevisible; Q9D939; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
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_0000085133"
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:0007744|PubMed:21183079"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 95
FT /note="D -> V (in Ref. 3; AAH22665)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="K -> Q (in Ref. 2; BAE25838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34953 MW; 50B8648F2A2BEA57 CRC64;
MALTPELSRQ TKLKEVAGIP LQAPTVDNWR QIQTFEAKPD DLLICTYPKS GTTWIQEIVD
MIEQNGDVEK CRRTIIQHRH PFIEWARPPQ PSGVDKANEM PAPRILRTHL PTQLLPPSFW
TNNCKFLYVA RNAKDCMVSY YHFYRMSQVL PEPGTWDEYF ETFINGKVSW GSWFDHVKGW
WEIRDKYQIL FLFYEDMKRN PKHEIQKVMQ FMGKNLDEDV VDKIVLETSF EKMKENPMTN
RSTAPKSILD QSISPFMRKG TVGDWKNHFT VAQNERFDEI YKQKMGRTSL NFSMEL
