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PTER_BOVIN
ID   PTER_BOVIN              Reviewed;         349 AA.
AC   A6QLJ8;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Phosphotriesterase-related protein;
DE            EC=3.1.-.-;
DE   AltName: Full=Parathion hydrolase-related protein;
GN   Name=PTER;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR   EMBL; BC147990; AAI47991.1; -; mRNA.
DR   RefSeq; NP_001094752.1; NM_001101282.1.
DR   RefSeq; XP_005214341.1; XM_005214284.2.
DR   RefSeq; XP_005214342.1; XM_005214285.3.
DR   AlphaFoldDB; A6QLJ8; -.
DR   SMR; A6QLJ8; -.
DR   STRING; 9913.ENSBTAP00000022174; -.
DR   PaxDb; A6QLJ8; -.
DR   PRIDE; A6QLJ8; -.
DR   Ensembl; ENSBTAT00000022174; ENSBTAP00000022174; ENSBTAG00000016676.
DR   Ensembl; ENSBTAT00000075515; ENSBTAP00000061794; ENSBTAG00000016676.
DR   Ensembl; ENSBTAT00000078237; ENSBTAP00000064770; ENSBTAG00000016676.
DR   Ensembl; ENSBTAT00000078923; ENSBTAP00000059284; ENSBTAG00000016676.
DR   GeneID; 782020; -.
DR   KEGG; bta:782020; -.
DR   CTD; 9317; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016676; -.
DR   VGNC; VGNC:33497; PTER.
DR   eggNOG; ENOG502QQQR; Eukaryota.
DR   GeneTree; ENSGT00390000006960; -.
DR   HOGENOM; CLU_054760_0_1_1; -.
DR   InParanoid; A6QLJ8; -.
DR   OMA; MVKCGFI; -.
DR   OrthoDB; 972282at2759; -.
DR   TreeFam; TF323205; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000016676; Expressed in metanephros cortex and 105 other tissues.
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   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..349
FT                   /note="Phosphotriesterase-related protein"
FT                   /id="PRO_0000388665"
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"
SQ   SEQUENCE   349 AA;  39098 MW;  150B3FB4104DF0C8 CRC64;
     MSSLSGKVQT VLGLVEPGTL GRTLTHEHLT MTFDCCYYPP PPSHEAISKE PIIMKNLFWI
     QKNPYSHKEN LQLNQETEAI KEELLDFKAK GGGALVENTT TGLSRDVRTL KWLAEETGVH
     IIAGAGFYVD ATHSSETRAK SVEQLTDVLV NEILCGADGT SIKCGVIGEI GCSWPLTDSE
     RKVLQATAHA QTQLGCPVII HPGRNQSAPF QIIRVLQEAG GDISKTVMSH IDRTILDKKE
     LLEFAQFGCY LEYDLFGTEL FHYQFNPDID MPNDNKRIKR VRLLVDEGYE DRILMAHDIH
     TKNRLTKYGG HGYSHILTNI VPKMLLRGIT EGALDKILIE NPKQWLTFK
 
 
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