NAPEP_PONAB
ID NAPEP_PONAB Reviewed; 393 AA.
AC Q5RCU3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858175; CAH90414.1; -; mRNA.
DR RefSeq; NP_001125208.1; NM_001131736.1.
DR AlphaFoldDB; Q5RCU3; -.
DR SMR; Q5RCU3; -.
DR STRING; 9601.ENSPPYP00000020040; -.
DR GeneID; 100172099; -.
DR KEGG; pon:100172099; -.
DR CTD; 222236; -.
DR eggNOG; KOG3798; Eukaryota.
DR InParanoid; Q5RCU3; -.
DR OrthoDB; 1194556at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005769; C:early endosome; ISS: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:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
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: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..393
FT /note="N-acyl-phosphatidylethanolamine-hydrolyzing
FT phospholipase D"
FT /id="PRO_0000318161"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 188
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 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 256
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 260
FT /ligand="deoxycholate"
FT /ligand_id="ChEBI:CHEBI:23614"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 321
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 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ20"
FT BINDING 348
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 393 AA; 45644 MW; 9D6E4989DD5DF309 CRC64;
MDENESNQSL MTSSQYPKEA VRKRQNSARN SGGSDSSRFS RKSFKLDYRL EEDVTKSKKG
KDGRFVNPWP TWKNHSIPHV LRWLIMEKDH SSVPSSKEEL DKELPVLKPY FITNPEEAGV
RETGLRVTWL GHATVMVEMD ELIFLTDPIF SSRASPSQYM GPKRFRRSPC TISELPPIDA
VLISHNHYDH LDYNSVIALN ERFGNELRWF VPLGLLDWMQ KCGCENVIEL DWWEENCVPG
HDKVTFVFTP SQHWCKRTLM DDNKVLWGSW SVLGPWNRFF FAGDTGYCPA FEEIGKRFGP
FDLAAIPIGA YEPRRFMKYQ HVDPEEAVRI HIDVQTKKSM AIHWGTFALA NEHYLEPPVK
LNEALERYGL NAEDFFVLKH GESRYLNTDD ENF
