P20D1_XENTR
ID P20D1_XENTR Reviewed; 512 AA.
AC Q08BT9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=N-fatty-acyl-amino acid synthase/hydrolase PM20D1 {ECO:0000305};
DE EC=3.5.1.114 {ECO:0000250|UniProtKB:Q8C165};
DE EC=3.5.1.14 {ECO:0000250|UniProtKB:Q8C165};
DE AltName: Full=Peptidase M20 domain-containing protein 1 {ECO:0000250|UniProtKB:Q8C165};
DE Flags: Precursor;
GN Name=pm20d1 {ECO:0000250|UniProtKB:Q8C165};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Secreted enzyme that regulates the endogenous N-fatty acyl
CC amino acid (NAAs) tissue and circulating levels by functioning as a
CC bidirectional NAA synthase/hydrolase. It condenses free fatty acids and
CC free amino acids to generate NAAs and bidirectionally catalyzes the
CC reverse hydrolysis reaction. Some of these NAAs stimulate oxidative
CC metabolism via mitochondrial uncoupling, increasing energy expenditure
CC in a UPC1-independent manner. Thereby, this secreted protein may
CC indirectly regulate whole body energy expenditure. PM20D1 circulates in
CC tight association with both low- and high-density (LDL and
CC HDL,respectively) lipoprotein particles.
CC {ECO:0000250|UniProtKB:Q8C165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate +
CC an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824,
CC ChEBI:CHEBI:138093; EC=3.5.1.114;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine; Xref=Rhea:RHEA:64108,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:59002; Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-
CC phenylalanine; Xref=Rhea:RHEA:64124, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:149699;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine +
CC octadecanoate; Xref=Rhea:RHEA:64128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:58095, ChEBI:CHEBI:149700;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-
CC phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-
CC phenylalanine; Xref=Rhea:RHEA:64132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58095, ChEBI:CHEBI:77016, ChEBI:CHEBI:149701;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate +
CC L-asparagine; Xref=Rhea:RHEA:64136, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58048, ChEBI:CHEBI:149730;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + glycine = H2O + N-(9Z-
CC octadecenoyl)glycine; Xref=Rhea:RHEA:51316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57305, ChEBI:CHEBI:133992;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-
CC lysine; Xref=Rhea:RHEA:64192, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:32551, ChEBI:CHEBI:149731;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate +
CC L-methionine; Xref=Rhea:RHEA:64144, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57844, ChEBI:CHEBI:149732;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-
CC serine; Xref=Rhea:RHEA:51352, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:134031;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate +
CC L-tryptophan; Xref=Rhea:RHEA:64176, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57912, ChEBI:CHEBI:149733;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-
CC tyrosine; Xref=Rhea:RHEA:64184, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:58315, ChEBI:CHEBI:149734;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate +
CC L-glutamine; Xref=Rhea:RHEA:51356, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58359, ChEBI:CHEBI:134033;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine; Xref=Rhea:RHEA:64116,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:149697; Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine;
CC Xref=Rhea:RHEA:51312, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:58095, ChEBI:CHEBI:134022;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-
CC leucine; Xref=Rhea:RHEA:51360, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:134035;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-
CC octadecenoyl)-L-phenylalanine; Xref=Rhea:RHEA:51300,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:134020; Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302;
CC Evidence={ECO:0000250|UniProtKB:Q8C165};
CC -!- ACTIVITY REGULATION: Lipoproteins are powerful coactivators of PM20D1
CC activity in vitro and NAA biosynthesis in vivo.
CC {ECO:0000250|UniProtKB:Q8C165}.
CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000250|UniProtKB:Q8C165}.
CC -!- PATHWAY: Energy metabolism; electron transfer.
CC {ECO:0000250|UniProtKB:Q8C165}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000250|UniProtKB:Q8C165}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8C165}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; BC124564; AAI24565.1; -; mRNA.
DR RefSeq; NP_001120523.1; NM_001127051.1.
DR AlphaFoldDB; Q08BT9; -.
DR SMR; Q08BT9; -.
DR STRING; 8364.ENSXETP00000013076; -.
DR PaxDb; Q08BT9; -.
DR DNASU; 100145660; -.
DR GeneID; 100145660; -.
DR KEGG; xtr:100145660; -.
DR CTD; 148811; -.
DR Xenbase; XB-GENE-996553; pm20d1.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_1_1; -.
DR InParanoid; Q08BT9; -.
DR OrthoDB; 1432382at2759; -.
DR PhylomeDB; Q08BT9; -.
DR Reactome; R-XTR-9673163; Oleoyl-phe metabolism.
DR UniPathway; UPA00092; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000005950; Expressed in liver and 8 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:1990845; P:adaptive thermogenesis; ISS:UniProtKB.
DR GO; GO:0043604; P:amide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043605; P:cellular amide catabolic process; ISS:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR GO; GO:0044255; P:cellular lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:2000275; P:regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Lipid metabolism; Lyase; Metal-binding; Protease;
KW Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..512
FT /note="N-fatty-acyl-amino acid synthase/hydrolase PM20D1"
FT /id="PRO_0000321932"
FT ACT_SITE 136
FT /evidence="ECO:0000250"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 512 AA; 56710 MW; 3CB9E96706E05B70 CRC64;
MAVSRWKAVG STLLAAFLVG LVVLIAVLLI RTYTLPTAVR KWNRNESLIT ELAEKERKQL
VEALKGAIRI PTVSFSEEEQ NTTALREFGE YIQKVFPQVF SSSLIQHEVL GGYSHLFKVQ
GSDHNLLPYM LLAHIDVVPA PPESWEVPPF SGEERDGYIY GRGTLDDKNC VIGILQSLEF
LLKRGHKPRR SFYIGLGHDE EISGHKGAQK IVEKLQSQGV KLAFVLDEGL AVLDGVIQGI
SQPVALVGTT EKGSVTLDLT VNRLPGHSSM PPSETSIGIL AAAVSRLEQN MMPNMFGNGP
EQDMFEHLST KFDFPLNIIM ANLWLFSPIL SRILELSPST NAIVRTTTAL TIFKAGIKSN
VIPPTATATV NFRLHPAQTV QEVLDIVQNT IKDERVELSV LNSFDPLPVS PNDMSLGYHI
LQRTIHDVFS GPPVAPGVCV GNTDSRHFVN LTNSIYRFSP VVLKKEDVDR IHGLNERISK
EAIELLVQFY IQLIQNSDTD NIPPPHLDTH EL
