SSU1_CAEEL
ID SSU1_CAEEL Reviewed; 412 AA.
AC Q9U2Z2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Sulfotransferase ssu-1 {ECO:0000305};
DE EC=2.8.2.1 {ECO:0000269|PubMed:16567400, ECO:0000269|PubMed:16973616};
DE AltName: Full=Suppressor of stomatin uncoordination protein 1 {ECO:0000303|PubMed:16973616};
GN Name=ssu-1 {ECO:0000312|WormBase:Y113G7A.11};
GN Synonyms=ST1 {ECO:0000303|PubMed:16567400};
GN ORFNames=Y113G7A.11 {ECO:0000312|WormBase:Y113G7A.11};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16567400; DOI=10.1093/jb/mvj041;
RA Hattori K., Inoue M., Inoue T., Arai H., Tamura H.O.;
RT "A novel sulfotransferase abundantly expressed in the dauer larvae of
RT Caenorhabditis elegans.";
RL J. Biochem. 139:355-362(2006).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 284-TRP--GLU-412.
RX PubMed=16973616; DOI=10.1074/jbc.m606086200;
RA Carroll B.T., Dubyak G.R., Sedensky M.M., Morgan P.G.;
RT "Sulfated signal from ASJ sensory neurons modulates stomatin-dependent
RT coordination in Caenorhabditis elegans.";
RL J. Biol. Chem. 281:35989-35996(2006).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 47-ARG--GLU-412; 108-GLN--GLU-412;
RP 195-TRP--GLU-412 AND 284-TRP--GLU-412.
RX PubMed=30514845; DOI=10.1038/s41467-018-07640-w;
RA Burton N.O., Dwivedi V.K., Burkhart K.B., Kaplan R.E.W., Baugh L.R.,
RA Horvitz H.R.;
RT "Neurohormonal signaling via a sulfotransferase antagonizes insulin-like
RT signaling to regulate a Caenorhabditis elegans stress response.";
RL Nat. Commun. 9:5152-5152(2018).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfonation of xenobiotics
CC that contain phenol functional groups (PubMed:16567400,
CC PubMed:16973616). Acts in ASJ sensory neurons to modulate developmental
CC arrest, perhaps by modifying endocrine signaling via the orphan nuclear
CC receptor nhr-1 (PubMed:30514845). {ECO:0000269|PubMed:16567400,
CC ECO:0000269|PubMed:16973616, ECO:0000269|PubMed:30514845}.
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:16567400, ECO:0000269|PubMed:16973616};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + bisphenol A = adenosine 3',5'-
CC bisphosphate + bisphenyl A sulfate + H(+); Xref=Rhea:RHEA:66580,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33216, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:167171;
CC Evidence={ECO:0000269|PubMed:16567400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-naphthol + 3'-phosphoadenylyl sulfate = 2-naphthyl sulfate +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:66572,
CC ChEBI:CHEBI:10432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:167170;
CC Evidence={ECO:0000269|PubMed:16567400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-isopropylphenol = 4-
CC isopropylphenyl sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:66576, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:167172, ChEBI:CHEBI:167173;
CC Evidence={ECO:0000269|PubMed:16567400};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 4-nitrophenol = 4-nitrophenyl
CC sulfate + adenosine 3',5'-bisphosphate; Xref=Rhea:RHEA:66548,
CC ChEBI:CHEBI:57917, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:140994; Evidence={ECO:0000269|PubMed:16567400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.55 uM for bisphenol A (at 25 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:16567400};
CC KM=4.31 uM for 3'-phosphoadenylyl sulfate (PAPS) (at 25 degrees
CC Celsius and pH 6.8 with 4-hydroxyphenylacetamide as cosubstrate)
CC {ECO:0000269|PubMed:16567400};
CC KM=8.1 uM for 2-naphthol (at 25 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:16567400};
CC KM=25.3 uM for 4-isopropylphenol (at 25 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:16567400};
CC KM=11.9 uM for 4-nitrophenol (at 25 degrees Celsius and pH 6.8)
CC {ECO:0000269|PubMed:16567400};
CC Note=kcat is 0.283 sec(-1) with bisphenol A as substrate (at 25
CC degrees Celsius and pH 6.8) (PubMed:16567400). kcat is 0.909 sec(-1)
CC with 3'-phosphoadenylyl sulfate (PAPS) as substrate (at 25 degrees
CC Celsius and pH 6.8, and with 4-hydroxyphenylacetamide as cosubstrate)
CC (PubMed:16567400). kcat is 0.533 sec(-1) with 2-naphthol as substrate
CC (at 25 degrees Celsius and pH 6.8) (PubMed:16567400). kcat is 1.32
CC sec(-1) with 4-isopropylphenol as substrate (at 25 degrees Celsius
CC and pH 6.8) (PubMed:16567400). kcat is 0.397 sec(-1) with 4-
CC nitrophenol (at 25 degrees Celsius and pH 6.8) (PubMed:16567400).
CC {ECO:0000269|PubMed:16567400};
CC pH dependence:
CC Optimum pH is 6.4-6.8 with 4-hydroxyphenylacetamide as substrate.
CC {ECO:0000269|PubMed:16567400};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius with 4-
CC hydroxyphenylacetamide as substrate. {ECO:0000269|PubMed:16567400};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16567400}.
CC Membrane {ECO:0000269|PubMed:16567400}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16567400}.
CC -!- TISSUE SPECIFICITY: Expressed in ASJ amphid sensory neurons.
CC {ECO:0000269|PubMed:16973616}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, but higher
CC expression in both embryo and adult stages (at protein level)
CC (PubMed:16567400). Expression increases at the dauer larval stage,
CC compared to the level in the embryo (PubMed:16567400).
CC {ECO:0000269|PubMed:16567400}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; BX284605; CAB60475.1; -; Genomic_DNA.
DR RefSeq; NP_507880.1; NM_075479.1.
DR AlphaFoldDB; Q9U2Z2; -.
DR SMR; Q9U2Z2; -.
DR STRING; 6239.Y113G7A.11; -.
DR PaxDb; Q9U2Z2; -.
DR EnsemblMetazoa; Y113G7A.11.1; Y113G7A.11.1; WBGene00013748.
DR GeneID; 190959; -.
DR KEGG; cel:CELE_Y113G7A.11; -.
DR UCSC; Y113G7A.11; c. elegans.
DR CTD; 190959; -.
DR WormBase; Y113G7A.11; CE23282; WBGene00013748; ssu-1.
DR eggNOG; KOG1584; Eukaryota.
DR HOGENOM; CLU_667705_0_0_1; -.
DR InParanoid; Q9U2Z2; -.
DR OMA; FCFRKGP; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q9U2Z2; -.
DR Reactome; R-CEL-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-CEL-9753281; Paracetamol ADME.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00013748; Expressed in multicellular organism and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034930; F:1-hydroxypyrene sulfotransferase activity; IDA:WormBase.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:WormBase.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0051923; P:sulfation; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:WormBase.
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; Membrane; Reference proteome; Transferase.
FT CHAIN 1..412
FT /note="Sulfotransferase ssu-1"
FT /id="PRO_0000452493"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 96..101
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 169
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 177
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 233
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 272..277
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT BINDING 297..299
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q06520"
FT MUTAGEN 47..412
FT /note="Missing: In gk747222; defects in developmental
FT arrest in response to osmotic stress."
FT /evidence="ECO:0000269|PubMed:30514845"
FT MUTAGEN 108..412
FT /note="Missing: In gk319712; defects in developmental
FT arrest in response to osmotic stress."
FT /evidence="ECO:0000269|PubMed:30514845"
FT MUTAGEN 195..412
FT /note="Missing: In gk876992; defects in developmental
FT arrest in response to osmotic stress."
FT /evidence="ECO:0000269|PubMed:30514845"
FT MUTAGEN 284..412
FT /note="Missing: In fc73, gk266317 and n5888; defects in
FT developmental arrest in response to osmotic stress.
FT Suppresses volatile anesthetic sensitivity and
FT uncoordinated locomotion phenotype on stomatin-like unc-1
FT mutant background."
FT /evidence="ECO:0000269|PubMed:16973616,
FT ECO:0000269|PubMed:30514845"
SQ SEQUENCE 412 AA; 47252 MW; 2D3062EDB9911DC4 CRC64;
MTPKTPKTPK PPQTPRPMLT VGSPPCTPCS PFVLNATSFC FRKGPARSVV YQPNGHPKQV
VIDGEIWPPI FKPKNVRTAK SMQFGETDVV IATYPKCGTT WLQHITSQLI KGHDYKAGKG
NELCVQSPMI ERMGAAFADN IKGPRVLKTH FHHYNIPKYP DTKYIYCVRN PKDCLTSYFH
HNRNFKIYNW ANGTWDVFLD LFASGQLAFG DYFEHLLSWL PCLKDDNVLF LKYEDMFQDL
ENAVYKIGQF LGGEAAHRVE NPEILREIVD NSTIDAMKKD QKRWFPESQL HKVEFIRKGG
SRDWKNYFTR EQSDRIDSIF AAKFAGTPAE HWWKYEMAWE EKPLSIENLS MEEEEEEQSQ
KLFALPPLPP QRRFSRTSLL SAGYGSVWSL SSQNANMSAS SSVNKDLSTF AE
