NAPEP_BOVIN
ID NAPEP_BOVIN Reviewed; 392 AA.
AC Q58CN9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D;
DE Short=N-acyl phosphatidylethanolamine phospholipase D;
DE Short=NAPE-PLD;
DE Short=NAPE-hydrolyzing phospholipase D;
DE EC=3.1.4.54 {ECO:0000250|UniProtKB:Q6IQ20, ECO:0000250|UniProtKB:Q8BH82};
GN Name=NAPEPLD;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: D-type phospholipase that hydrolyzes N-acyl-
CC phosphatidylethanolamines (NAPEs) to produce bioactive N-
CC acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic
CC acid (By similarity). Cleaves the terminal phosphodiester bond of
CC diacyl- and alkenylacyl-NAPEs, primarily playing a role in the
CC generation of long-chain saturated and monounsaturated NAEs in the
CC brain (By similarity). May control NAPE homeostasis in dopaminergic
CC neuron membranes and regulate neuron survival, partly through RAC1
CC activation (By similarity). As a regulator of lipid metabolism in the
CC adipose tissue, mediates the crosstalk between adipocytes, gut
CC microbiota and immune cells to control body temperature and weight. In
CC particular, regulates energy homeostasis by promoting cold-induced
CC brown or beige adipocyte differentiation program to generate heat from
CC fatty acids and glucose. Has limited D-type phospholipase activity
CC toward N-acyl lyso-NAPEs (By similarity).
CC {ECO:0000250|UniProtKB:Q6IQ20, ECO:0000250|UniProtKB:Q8BH82}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC 1,2-diacyl-sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC Xref=Rhea:RHEA:33159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52640, ChEBI:CHEBI:58608, ChEBI:CHEBI:62537; EC=3.1.4.54;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20,
CC ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-butanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-butanoyl
CC ethanolamine; Xref=Rhea:RHEA:45620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85298,
CC ChEBI:CHEBI:85304; Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45621;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-hexanoyl
CC ethanolamine; Xref=Rhea:RHEA:45616, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85297,
CC ChEBI:CHEBI:85303; Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45617;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-octanoyl
CC ethanolamine; Xref=Rhea:RHEA:45612, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85296,
CC ChEBI:CHEBI:85302; Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45613;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-decanoyl-1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-decanoyl
CC ethanolamine; Xref=Rhea:RHEA:45608, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72860, ChEBI:CHEBI:85295,
CC ChEBI:CHEBI:85301; Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45609;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-dodecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-dodecanoylethanolamine; Xref=Rhea:RHEA:45556,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85263, ChEBI:CHEBI:85294;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45557;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-tetradecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-tetradecanoylethanolamine; Xref=Rhea:RHEA:45552,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85262, ChEBI:CHEBI:85293;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45553;
CC Evidence={ECO:0000250|UniProtKB:Q769K2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:45540,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45541;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:45596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:72860,
CC ChEBI:CHEBI:85334; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45597;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-octadecanoyl ethanolamine; Xref=Rhea:RHEA:45536,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85292, ChEBI:CHEBI:85299;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45537;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1,2-tri-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate
CC + H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:45532,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:85291;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45533;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-diacyl-sn-
CC glycero-3-phosphoethanolamine = a 1,2-diacyl-sn-glycero-3-phosphate +
CC H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC Xref=Rhea:RHEA:56548, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58608, ChEBI:CHEBI:140532;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56549;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-ethanolamine; Xref=Rhea:RHEA:45528,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:74546, ChEBI:CHEBI:85277;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45529;
CC Evidence={ECO:0000250|UniProtKB:Q769K2,
CC ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(1Z-octadecenoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC N-hexadecanoyl-ethanolamine + H2O = 1-O-(1Z-octadecenoyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:56464, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:71464, ChEBI:CHEBI:138663,
CC ChEBI:CHEBI:140452; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56465;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-diacyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-
CC sn-glycero-3-phosphate + an N-acylethanolamine + H(+);
CC Xref=Rhea:RHEA:53164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52640, ChEBI:CHEBI:57970, ChEBI:CHEBI:85216;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53165;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:45592, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:85335; Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC Xref=Rhea:RHEA:45544, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74544, ChEBI:CHEBI:85223;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC Evidence={ECO:0000250|UniProtKB:Q8BH82};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q6IQ20};
CC Note=Binds 2 zinc divalent cations per subunit.
CC {ECO:0000250|UniProtKB:Q6IQ20};
CC -!- ACTIVITY REGULATION: Activated by divalent cations. Activated by bile
CC acids. {ECO:0000250|UniProtKB:Q6IQ20}.
CC -!- SUBUNIT: Homodimer. Bile acids promote the assembly of inactive
CC monomers into an active dimer and enable catalysis.
CC {ECO:0000250|UniProtKB:Q6IQ20}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the
CC cellular membranes likely through interaction with membrane
CC phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
CC kidney and testis (at protein level). Expressed in adipose tissue (at
CC protein level). {ECO:0000250|UniProtKB:Q8BH82}.
CC -!- SIMILARITY: Belongs to the NAPE-PLD family. {ECO:0000305}.
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DR EMBL; BT021908; AAX46755.1; -; mRNA.
DR RefSeq; NP_001015680.1; NM_001015680.1.
DR RefSeq; XP_010802479.1; XM_010804177.1.
DR AlphaFoldDB; Q58CN9; -.
DR SMR; Q58CN9; -.
DR STRING; 9913.ENSBTAP00000018833; -.
DR PaxDb; Q58CN9; -.
DR PRIDE; Q58CN9; -.
DR Ensembl; ENSBTAT00000018833; ENSBTAP00000018833; ENSBTAG00000014171.
DR Ensembl; ENSBTAT00000086672; ENSBTAP00000067871; ENSBTAG00000014171.
DR GeneID; 541291; -.
DR KEGG; bta:541291; -.
DR CTD; 222236; -.
DR VEuPathDB; HostDB:ENSBTAG00000014171; -.
DR VGNC; VGNC:31883; NAPEPLD.
DR eggNOG; KOG3798; Eukaryota.
DR GeneTree; ENSGT00390000017990; -.
DR HOGENOM; CLU_020884_2_1_1; -.
DR InParanoid; Q58CN9; -.
DR OMA; QHWTRRT; -.
DR OrthoDB; 1194556at2759; -.
DR TreeFam; TF313520; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000014171; Expressed in oocyte and 109 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0032052; F:bile acid binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0102200; F:N-acetylphosphatidylethanolamine-hydrolysing phospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0048874; P:host-mediated regulation of intestinal microbiota composition; ISS:UniProtKB.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IBA:GO_Central.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR024884; NAPE-PLD.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF12706; Lactamase_B_2; 1.
DR PIRSF; PIRSF038896; NAPE-PLD; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endosome; Golgi apparatus; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Nucleus;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Zinc.
FT CHAIN 1..392
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D"
FT /id="PRO_0000318158"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 186
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 254
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 258
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 319
FT /ligand="N-acyl-1,2-diacyl-sn-glycero-3-
FT phosphoethanolamine"
FT /ligand_id="ChEBI:CHEBI:62537"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 346
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
SQ SEQUENCE 392 AA; 45341 MW; 3697EDDF04DBD97E CRC64;
MDENETNQLL MTSNQYPKEA VRKRQNSRNS GGSDSSRFSR KSFKLDYRLE EDVTKSKKGK
DGRFVNPWPT WKNPSIPSLL RWVITERDHS SVPCSKELDK ELPVLKPYFI DDPEEAGVRG
AGLRVTWLGH ATVMVEMDEL ILLTDPIFSA RASPSQRMGP KRFRRAPCTV EELPRIDAVL
VSHNHYDHLD CNSVIALNER FGNELRWFVP LGLLDWMQKC GCENVIELDW WEENCVPGHD
KVTFVFTPSQ HWCKRTLMDD NKVLWGSWSV LGPWNRFFFA GDTGYCSAFE EIGKRFGPFD
LAAIPIGAYE PRWFMKYQHV DPEEAVKIHI DVQAKKSVAI HWGTFALANE HYLEPPAKLC
EALEKYRLKT EDFLVLKHGE SRYLNTDDED VE
