PTER_MOUSE
ID PTER_MOUSE Reviewed; 349 AA.
AC Q60866; A2AUR4; A2AUR6; Q8BTA3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
GN Name=Pter;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=8654936; DOI=10.1016/0378-1119(95)00746-6;
RA Hou X., Maser R.L., Magenheimer B.S., Calvet J.P.;
RT "A mouse kidney- and liver-expressed cDNA having homology with a
RT prokaryotic parathion hydrolase (phosphotriesterase)-encoding gene:
RT abnormal expression in injured and polycystic kidneys.";
RL Gene 168:157-163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Pancreas;
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q60866-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q60866-2; Sequence=VSP_038343, VSP_038344;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and liver.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; U28016; AAA68951.1; -; mRNA.
DR EMBL; AK012076; BAC25353.1; -; mRNA.
DR EMBL; AL929209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08046.1; -; Genomic_DNA.
DR EMBL; BC003793; AAH03793.1; -; mRNA.
DR CCDS; CCDS15691.1; -. [Q60866-1]
DR CCDS; CCDS84471.1; -. [Q60866-2]
DR RefSeq; NP_001292365.1; NM_001305436.1. [Q60866-2]
DR RefSeq; NP_001292366.1; NM_001305437.1.
DR RefSeq; NP_032987.1; NM_008961.3. [Q60866-1]
DR AlphaFoldDB; Q60866; -.
DR SMR; Q60866; -.
DR BioGRID; 202450; 1.
DR IntAct; Q60866; 1.
DR STRING; 10090.ENSMUSP00000117009; -.
DR iPTMnet; Q60866; -.
DR PhosphoSitePlus; Q60866; -.
DR SwissPalm; Q60866; -.
DR REPRODUCTION-2DPAGE; Q60866; -.
DR EPD; Q60866; -.
DR jPOST; Q60866; -.
DR MaxQB; Q60866; -.
DR PaxDb; Q60866; -.
DR PeptideAtlas; Q60866; -.
DR PRIDE; Q60866; -.
DR ProteomicsDB; 301895; -. [Q60866-1]
DR ProteomicsDB; 301896; -. [Q60866-2]
DR Antibodypedia; 25152; 110 antibodies from 26 providers.
DR DNASU; 19212; -.
DR Ensembl; ENSMUST00000028063; ENSMUSP00000028063; ENSMUSG00000026730. [Q60866-2]
DR Ensembl; ENSMUST00000134794; ENSMUSP00000117009; ENSMUSG00000026730. [Q60866-1]
DR GeneID; 19212; -.
DR KEGG; mmu:19212; -.
DR UCSC; uc008ijt.2; mouse. [Q60866-1]
DR UCSC; uc012bqx.2; mouse. [Q60866-2]
DR CTD; 9317; -.
DR MGI; MGI:107372; Pter.
DR VEuPathDB; HostDB:ENSMUSG00000026730; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR GeneTree; ENSGT00390000006960; -.
DR InParanoid; Q60866; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; Q60866; -.
DR TreeFam; TF323205; -.
DR BioGRID-ORCS; 19212; 0 hits in 57 CRISPR screens.
DR ChiTaRS; Pter; mouse.
DR PRO; PR:Q60866; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60866; protein.
DR Bgee; ENSMUSG00000026730; Expressed in right kidney and 216 other tissues.
DR ExpressionAtlas; Q60866; baseline and differential.
DR Genevisible; Q60866; MM.
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; IEA:Ensembl.
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 SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..349
FT /note="Phosphotriesterase-related protein"
FT /id="PRO_0000205365"
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 VAR_SEQ 258..260
FT /note="TEL -> SIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038343"
FT VAR_SEQ 261..349
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038344"
FT CONFLICT 197
FT /note="P -> S (in Ref. 2; BAC25353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39218 MW; FF602F1887F16B33 CRC64;
MSSLSGKVQT VLGLVEPSQL GRTLTHEHLT MTFDSFYCPP PPCHEVTSKE PIMMKNLFWI
QKNPYSHREN LQLNQEVGAI REELLYFKAK GGGALVENTT TGLSRDVHTL KWLAEQTGVH
IIAGAGFYVD ATHSAATRAM SVEQLTDVLI NEILHGADGT SIKCGVIGEI GCSWPLTDSE
RKILEATAHA QAQLGCPVII HPGRNPGAPF QIIRILQEAG ADISKTVMSH LDRTIFDKKE
LLEFAQLGCY LEYDLFGTEL LNYQLSPDID MPDDNKRIRR VHFLVDEGYE DRILMAHDIH
TKHRLMKYGG HGYSHILTNI VPKMLLRGLT ERVLDKILIE NPKQWLTFK
