PTER_RAT
ID PTER_RAT Reviewed; 349 AA.
AC Q63530; Q6AYY7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
DE AltName: Full=Resiniferotoxin-binding phosphotriesterase-related protein;
GN Name=Pter; Synonyms=Rpr-1;
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 [GENOMIC DNA].
RX PubMed=9237666; DOI=10.1016/s0014-5793(97)00614-5;
RA Davies J.A., Buchman V., Krylova O., Ninkina N.N.;
RT "Molecular cloning and expression pattern of rpr-1, a resiniferatoxin-
RT binding, phosphotriesterase-related protein, expressed in rat kidney
RT tubules.";
RL FEBS Lett. 410:378-382(1997).
RN [2]
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).
CC -!- FUNCTION: Binds resiniferotoxin, a vanilloid that desensitizes
CC nociceptive neurons.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- TISSUE SPECIFICITY: Expressed primarily in proximal tubules of the
CC kidney.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; X99477; CAA67840.1; -; Genomic_DNA.
DR EMBL; BC078833; AAH78833.1; -; mRNA.
DR RefSeq; NP_071560.2; NM_022224.2.
DR RefSeq; XP_006254353.1; XM_006254291.3.
DR AlphaFoldDB; Q63530; -.
DR SMR; Q63530; -.
DR STRING; 10116.ENSRNOP00000023446; -.
DR iPTMnet; Q63530; -.
DR PhosphoSitePlus; Q63530; -.
DR PaxDb; Q63530; -.
DR PRIDE; Q63530; -.
DR Ensembl; ENSRNOT00000023446; ENSRNOP00000023446; ENSRNOG00000017328.
DR GeneID; 63852; -.
DR KEGG; rno:63852; -.
DR CTD; 9317; -.
DR RGD; 61313; Pter.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR GeneTree; ENSGT00390000006960; -.
DR HOGENOM; CLU_054760_0_1_1; -.
DR InParanoid; Q63530; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; Q63530; -.
DR TreeFam; TF323205; -.
DR PRO; PR:Q63530; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017328; Expressed in kidney and 19 other tissues.
DR Genevisible; Q63530; RN.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR CDD; cd00530; PTE; 1.
DR InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR PIRSF; PIRSF016839; PhP; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..349
FT /note="Phosphotriesterase-related protein"
FT /id="PRO_0000205366"
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 28
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 298
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT CONFLICT 134
FT /note="S -> F (in Ref. 1; CAA67840)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="M -> L (in Ref. 1; CAA67840)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..280
FT /note="RIRR -> GLGG (in Ref. 1; CAA67840)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="G -> V (in Ref. 1; CAA67840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39145 MW; FAC9749B900D89B4 CRC64;
MSSLSGKVQT VLGPVEPSQL GRTLTHEHLT MAFDSFYCPP PPCQEAASRE PIMMKNLFWI
QKNPYSHQEN LQLNQEVEAV REELLYFKAK GGGAVVENTT TGLSRDVRTL KWLAEQTGVH
IIAGAGFYVD ATHSAATRAM SVEQLTDVLI SEILHGADGT SIKCGVIGEI GCSWPLTDSE
RKVLQATAHA QAQLGCPVII HPGRNPGAPF QIIRVLQEAG ADISKTVMSH LDRSIFDKKE
LLEFAQLGCY LEYDLFGTEL LNYQLSPDID MPDDNKRIRR VRFLVNEGYE DRILMAHDIH
TKHRLMKYGG HGYSHILTNV VPKMLLRGLT ERVLDKILRE NPKQWLTFK
