PTER_HUMAN
ID PTER_HUMAN Reviewed; 349 AA.
AC Q96BW5; B0YJ77; B3KTF5; D3DRU0; Q9BY46;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
DE Short=hPHRP;
GN Name=PTER;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Uterus;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 -!- INTERACTION:
CC Q96BW5; O15499: GSC2; NbExp=3; IntAct=EBI-4291023, EBI-19954058;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96BW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BW5-2; Sequence=VSP_038342;
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; AF212237; AAK14923.1; -; mRNA.
DR EMBL; AK095486; BAG53067.1; -; mRNA.
DR EMBL; AK314910; BAG37422.1; -; mRNA.
DR EMBL; EF445015; ACA06055.1; -; Genomic_DNA.
DR EMBL; EF445015; ACA06056.1; -; Genomic_DNA.
DR EMBL; EF445015; ACA06057.1; -; Genomic_DNA.
DR EMBL; AL360230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86226.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86229.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86227.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86228.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86230.1; -; Genomic_DNA.
DR EMBL; BC015092; AAH15092.1; -; mRNA.
DR EMBL; BC050411; AAH50411.1; -; mRNA.
DR CCDS; CCDS58070.1; -. [Q96BW5-2]
DR CCDS; CCDS7111.1; -. [Q96BW5-1]
DR RefSeq; NP_001001484.1; NM_001001484.2. [Q96BW5-1]
DR RefSeq; NP_001248765.1; NM_001261836.1. [Q96BW5-1]
DR RefSeq; NP_001248766.1; NM_001261837.1. [Q96BW5-2]
DR RefSeq; NP_001248767.1; NM_001261838.1.
DR RefSeq; NP_109589.2; NM_030664.4. [Q96BW5-1]
DR RefSeq; XP_016872418.1; XM_017016929.1. [Q96BW5-2]
DR RefSeq; XP_016872419.1; XM_017016930.1. [Q96BW5-2]
DR AlphaFoldDB; Q96BW5; -.
DR SMR; Q96BW5; -.
DR BioGRID; 114728; 37.
DR IntAct; Q96BW5; 10.
DR MINT; Q96BW5; -.
DR STRING; 9606.ENSP00000367239; -.
DR GlyGen; Q96BW5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96BW5; -.
DR PhosphoSitePlus; Q96BW5; -.
DR BioMuta; PTER; -.
DR DMDM; 32171701; -.
DR EPD; Q96BW5; -.
DR jPOST; Q96BW5; -.
DR MassIVE; Q96BW5; -.
DR MaxQB; Q96BW5; -.
DR PaxDb; Q96BW5; -.
DR PeptideAtlas; Q96BW5; -.
DR PRIDE; Q96BW5; -.
DR ProteomicsDB; 76122; -. [Q96BW5-1]
DR ProteomicsDB; 76123; -. [Q96BW5-2]
DR Antibodypedia; 25152; 110 antibodies from 26 providers.
DR DNASU; 9317; -.
DR Ensembl; ENST00000298942.4; ENSP00000298942.4; ENSG00000165983.15. [Q96BW5-2]
DR Ensembl; ENST00000378000.5; ENSP00000367239.1; ENSG00000165983.15. [Q96BW5-1]
DR Ensembl; ENST00000535784.7; ENSP00000439485.1; ENSG00000165983.15. [Q96BW5-1]
DR GeneID; 9317; -.
DR KEGG; hsa:9317; -.
DR MANE-Select; ENST00000535784.7; ENSP00000439485.1; NM_001261836.2; NP_001248765.1.
DR UCSC; uc001ioh.3; human. [Q96BW5-1]
DR CTD; 9317; -.
DR DisGeNET; 9317; -.
DR GeneCards; PTER; -.
DR HGNC; HGNC:9590; PTER.
DR HPA; ENSG00000165983; Tissue enhanced (kidney).
DR MIM; 604446; gene.
DR neXtProt; NX_Q96BW5; -.
DR OpenTargets; ENSG00000165983; -.
DR PharmGKB; PA33944; -.
DR VEuPathDB; HostDB:ENSG00000165983; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR GeneTree; ENSGT00390000006960; -.
DR HOGENOM; CLU_054760_0_1_1; -.
DR InParanoid; Q96BW5; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; Q96BW5; -.
DR TreeFam; TF323205; -.
DR PathwayCommons; Q96BW5; -.
DR SignaLink; Q96BW5; -.
DR BioGRID-ORCS; 9317; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; PTER; human.
DR GenomeRNAi; 9317; -.
DR Pharos; Q96BW5; Tbio.
DR PRO; PR:Q96BW5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96BW5; protein.
DR Bgee; ENSG00000165983; Expressed in anterior cingulate cortex and 176 other tissues.
DR ExpressionAtlas; Q96BW5; baseline and differential.
DR Genevisible; Q96BW5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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; IEP:UniProtKB.
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_0000205364"
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 234..280
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038342"
FT VARIANT 97
FT /note="E -> G (in dbSNP:rs36023740)"
FT /id="VAR_051610"
FT CONFLICT 234
FT /note="T -> A (in Ref. 1; AAK14923)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="E -> D (in Ref. 1; AAK14923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39018 MW; 76DCEA1E5C9FED46 CRC64;
MSSLSGKVQT VLGLVEPSKL GRTLTHEHLA MTFDCCYCPP PPCQEAISKE PIVMKNLYWI
QKNAYSHKEN LQLNQETEAI KEELLYFKAN GGGALVENTT TGISRDTQTL KRLAEETGVH
IISGAGFYVD ATHSSETRAM SVEQLTDVLM NEILHGADGT SIKCGIIGEI GCSWPLTESE
RKVLQATAHA QAQLGCPVII HPGRSSRAPF QIIRILQEAG ADISKTVMSH LDRTILDKKE
LLEFAQLGCY LEYDLFGTEL LHYQLGPDID MPDDNKRIRR VRLLVEEGCE DRILVAHDIH
TKTRLMKYGG HGYSHILTNV VPKMLLRGIT ENVLDKILIE NPKQWLTFK
