ST1C2_RAT
ID ST1C2_RAT Reviewed; 296 AA.
AC Q9WUW8; F1LZL1; Q3ZAV3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Sulfotransferase 1C2;
DE Short=ST1C2;
DE Short=rSULT1C2;
DE EC=2.8.2.1 {ECO:0000269|PubMed:10872834};
DE AltName: Full=Sulfotransferase K1;
GN Name=Sult1c2; Synonyms=Sultk1;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND FUNCTION.
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 INDUCTION.
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).
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 -!- INDUCTION: Down-regulated in kidney but not in stomach following
CC feeding with 2-amino-4,5-diphenylthiazole.
CC {ECO:0000269|PubMed:12164856}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AJ238391; CAB41460.1; -; mRNA.
DR EMBL; AABR07066190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07066191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC103636; AAI03637.1; -; mRNA.
DR PIR; JC7282; JC7282.
DR RefSeq; NP_598231.3; NM_133547.4.
DR AlphaFoldDB; Q9WUW8; -.
DR SMR; Q9WUW8; -.
DR STRING; 10116.ENSRNOP00000058611; -.
DR iPTMnet; Q9WUW8; -.
DR PhosphoSitePlus; Q9WUW8; -.
DR PaxDb; Q9WUW8; -.
DR PRIDE; Q9WUW8; -.
DR GeneID; 171072; -.
DR KEGG; rno:171072; -.
DR UCSC; RGD:621064; rat.
DR CTD; 6819; -.
DR RGD; 621064; Sult1c2.
DR eggNOG; KOG1584; Eukaryota.
DR InParanoid; Q9WUW8; -.
DR OMA; FQRMNQM; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9WUW8; -.
DR BRENDA; 2.8.2.1; 5301.
DR Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR PRO; PR:Q9WUW8; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000040215; Expressed in kidney and 10 other tissues.
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; IBA:GO_Central.
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_0000085135"
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"
FT CONFLICT 197
FT /note="M -> V (in Ref. 1; CAB41460)"
SQ SEQUENCE 296 AA; 34731 MW; 21F33DC241AEBFA4 CRC64;
MALAPELSRQ TKLKEVAGIP LQAPTVDNWS QIQTFKAKPD DLLICTYPKS GTTWIQEIVD
MIEQNGDVEK CQRTIIQHRH PFIEWARPPQ PSGVDKANAM PAPRILRTHL PTQLLPPSFW
TNNCKFLYVA RNAKDCMVSY YHFYRMSQVL PDPGTWNEYF ETFINGKVSW GSWFDHVKGW
WEIRDRYQIL FLFYEDMKRD PKREIQKVMQ FMGKNLDEEV VDKIVLETSF EKMKENPMTN
RSTVPKSVLD QSISPFMRKG TVGDWKNHFT VAQNDRFDEI YKQKMGGTSL NFCMEL
