P20D1_HUMAN
ID P20D1_HUMAN Reviewed; 502 AA.
AC Q6GTS8; Q6P4E3; Q96DM4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=N-fatty-acyl-amino acid synthase/hydrolase PM20D1 {ECO:0000305|PubMed:27374330};
DE EC=3.5.1.114 {ECO:0000269|PubMed:27374330};
DE EC=3.5.1.14 {ECO:0000269|PubMed:27374330};
DE AltName: Full=Peptidase M20 domain-containing protein 1 {ECO:0000312|HGNC:HGNC:26518};
DE Flags: Precursor;
GN Name=PM20D1 {ECO:0000312|HGNC:HGNC:26518};
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] (ISOFORMS 1 AND 2), AND VARIANTS
RP VAL-149 AND TRP-153.
RC TISSUE=Kidney, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS TYR-33;
RP VAL-149; TRP-153; THR-237; ARG-346 AND THR-380.
RC TISSUE=Pancreas, and Skin;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=27374330; DOI=10.1016/j.cell.2016.05.071;
RA Long J.Z., Svensson K.J., Bateman L.A., Lin H., Kamenecka T.,
RA Lokurkar I.A., Lou J., Rao R.R., Chang M.R., Jedrychowski M.P., Paulo J.A.,
RA Gygi S.P., Griffin P.R., Nomura D.K., Spiegelman B.M.;
RT "The secreted enzyme PM20D1 regulates lipidated amino acid uncouplers of
RT mitochondria.";
RL Cell 166:424-435(2016).
RN [5]
RP MISCELLANEOUS.
RX PubMed=29736028; DOI=10.1038/s41591-018-0013-y;
RA Sanchez-Mut J.V., Heyn H., Silva B.A., Dixsaut L., Garcia-Esparcia P.,
RA Vidal E., Sayols S., Glauser L., Monteagudo-Sanchez A., Perez-Tur J.,
RA Ferrer I., Monk D., Schneider B., Esteller M., Graeff J.;
RT "PM20D1 is a quantitative trait locus associated with Alzheimer's
RT disease.";
RL Nat. Med. 24:598-603(2018).
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 (PubMed:27374330). It condenses
CC free fatty acids and free amino acids to generate NAAs and
CC bidirectionally catalyzes the reverse hydrolysis reaction
CC (PubMed:27374330). Some of these NAAs stimulate oxidative metabolism
CC via mitochondrial uncoupling, increasing energy expenditure in a UPC1-
CC independent manner. Thereby, this secreted protein may indirectly
CC regulate whole body energy expenditure. PM20D1 circulates in tight
CC association with both low- and high-density (LDL and HDL,respectively)
CC lipoprotein particles (By similarity). {ECO:0000250|UniProtKB:Q8C165,
CC ECO:0000269|PubMed:27374330}.
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:0000269|PubMed:27374330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000269|PubMed:27374330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567;
CC Evidence={ECO:0000269|PubMed:27374330};
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:0000269|PubMed:27374330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185;
CC Evidence={ECO:0000269|PubMed:27374330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186;
CC Evidence={ECO:0000269|PubMed:27374330};
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:0000269|PubMed:27374330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301;
CC Evidence={ECO:0000269|PubMed:27374330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302;
CC Evidence={ECO:0000269|PubMed:27374330};
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:0000269|PubMed:27374330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361;
CC Evidence={ECO:0000269|PubMed:27374330};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362;
CC Evidence={ECO:0000269|PubMed:27374330};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
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:0000269|PubMed:27374330}.
CC -!- PATHWAY: Energy metabolism. {ECO:0000269|PubMed:27374330}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:27374330}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8C165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6GTS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6GTS8-2; Sequence=VSP_031826, VSP_031827;
CC -!- MISCELLANEOUS: Genetically increasing or decreasing the expression of
CC PM20D1 reduces and aggravates Alzheimer's disease (AD) related
CC pathologies, respectively. These findings suggest that in a particular
CC genetic background, PM20D1 contributes to neuroprotection against AD.
CC {ECO:0000269|PubMed:29736028}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A touch of warmth - Issue
CC 195 of September 2017;
CC URL="https://web.expasy.org/spotlight/back_issues/195/";
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DR EMBL; AK057131; BAB71368.1; -; mRNA.
DR EMBL; AK290786; BAF83475.1; -; mRNA.
DR EMBL; AC119673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039170; AAH39170.1; -; mRNA.
DR EMBL; BC063477; AAH63477.1; -; mRNA.
DR CCDS; CCDS1460.1; -. [Q6GTS8-1]
DR RefSeq; NP_689704.4; NM_152491.4. [Q6GTS8-1]
DR AlphaFoldDB; Q6GTS8; -.
DR SMR; Q6GTS8; -.
DR BioGRID; 127171; 22.
DR IntAct; Q6GTS8; 2.
DR STRING; 9606.ENSP00000356104; -.
DR SwissLipids; SLP:000001665; -.
DR MEROPS; M20.011; -.
DR GlyGen; Q6GTS8; 3 sites.
DR iPTMnet; Q6GTS8; -.
DR PhosphoSitePlus; Q6GTS8; -.
DR BioMuta; PM20D1; -.
DR DMDM; 317373406; -.
DR MassIVE; Q6GTS8; -.
DR PaxDb; Q6GTS8; -.
DR PeptideAtlas; Q6GTS8; -.
DR PRIDE; Q6GTS8; -.
DR ProteomicsDB; 66320; -. [Q6GTS8-1]
DR ProteomicsDB; 66321; -. [Q6GTS8-2]
DR Antibodypedia; 2556; 26 antibodies from 12 providers.
DR DNASU; 148811; -.
DR Ensembl; ENST00000367136.5; ENSP00000356104.4; ENSG00000162877.13. [Q6GTS8-1]
DR GeneID; 148811; -.
DR KEGG; hsa:148811; -.
DR MANE-Select; ENST00000367136.5; ENSP00000356104.4; NM_152491.5; NP_689704.4.
DR UCSC; uc001hdj.4; human. [Q6GTS8-1]
DR CTD; 148811; -.
DR DisGeNET; 148811; -.
DR GeneCards; PM20D1; -.
DR HGNC; HGNC:26518; PM20D1.
DR HPA; ENSG00000162877; Tissue enriched (pancreas).
DR MIM; 617124; gene.
DR neXtProt; NX_Q6GTS8; -.
DR OpenTargets; ENSG00000162877; -.
DR PharmGKB; PA162399772; -.
DR VEuPathDB; HostDB:ENSG00000162877; -.
DR eggNOG; KOG2275; Eukaryota.
DR GeneTree; ENSGT00940000156659; -.
DR HOGENOM; CLU_021802_11_1_1; -.
DR InParanoid; Q6GTS8; -.
DR OMA; NYGDHSG; -.
DR OrthoDB; 1432382at2759; -.
DR PhylomeDB; Q6GTS8; -.
DR TreeFam; TF328688; -.
DR PathwayCommons; Q6GTS8; -.
DR Reactome; R-HSA-9673163; Oleoyl-phe metabolism.
DR SignaLink; Q6GTS8; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 148811; 11 hits in 1064 CRISPR screens.
DR ChiTaRS; PM20D1; human.
DR GenomeRNAi; 148811; -.
DR Pharos; Q6GTS8; Tdark.
DR PRO; PR:Q6GTS8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6GTS8; protein.
DR Bgee; ENSG00000162877; Expressed in upper leg skin and 94 other tissues.
DR Genevisible; Q6GTS8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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; EXP:Reactome.
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; TAS:Reactome.
DR GO; GO:0043604; P:amide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0043605; P:cellular amide catabolic process; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0044255; P:cellular lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
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; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Hydrolase; Lipid metabolism; Lyase;
KW Metal-binding; Protease; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..502
FT /note="N-fatty-acyl-amino acid synthase/hydrolase PM20D1"
FT /id="PRO_0000321928"
FT ACT_SITE 127
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 302..361
FT /note="FPFPVNIILSNPWLFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIP
FT PVAQATVN -> VYGEKSLNQCNNQDHHGTHHIQSRGQVQCHPPSGPGHSQLPDSPWTD
FT SPRGPRTHEEHCG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031826"
FT VAR_SEQ 362..502
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_031827"
FT VARIANT 33
FT /note="H -> Y (in dbSNP:rs11540014)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039380"
FT VARIANT 149
FT /note="I -> V (in dbSNP:rs1891460)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_039381"
FT VARIANT 153
FT /note="R -> W (in dbSNP:rs1104899)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_039382"
FT VARIANT 237
FT /note="I -> T (in dbSNP:rs7518979)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039383"
FT VARIANT 258
FT /note="S -> C (in dbSNP:rs11581214)"
FT /id="VAR_039384"
FT VARIANT 346
FT /note="G -> R (in dbSNP:rs11240573)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039385"
FT VARIANT 380
FT /note="I -> T (in dbSNP:rs1361754)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039386"
FT CONFLICT 84
FT /note="H -> R (in Ref. 3; AAH39170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 55741 MW; 0CC2C45E1A7ADEA8 CRC64;
MAQRCVCVLA LVAMLLLVFP TVSRSMGPRS GEHQRASRIP SQFSKEERVA MKEALKGAIQ
IPTVTFSSEK SNTTALAEFG KYIHKVFPTV VSTSFIQHEV VEEYSHLFTI QGSDPSLQPY
LLMAHFDVVP APEEGWEVPP FSGLERDGII YGRGTLDDKN SVMALLQALE LLLIRKYIPR
RSFFISLGHD EESSGTGAQR ISALLQSRGV QLAFIVDEGG FILDDFIPNF KKPIALIAVS
EKGSMNLMLQ VNMTSGHSSA PPKETSIGIL AAAVSRLEQT PMPIIFGSGT VVTVLQQLAN
EFPFPVNIIL SNPWLFEPLI SRFMERNPLT NAIIRTTTAL TIFKAGVKFN VIPPVAQATV
NFRIHPGQTV QEVLELTKNI VADNRVQFHV LSAFDPLPVS PSDDKALGYQ LLRQTVQSVF
PEVNITAPVT SIGNTDSRFF TNLTTGIYRF YPIYIQPEDF KRIHGVNEKI SVQAYETQVK
FIFELIQNAD TDQEPVSHLH KL
