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N-fatty-acyl-amino acid synthase/hydrolase PM20D1 (EC 3.5.1.-) (EC 4.3.-.-) (Peptidase M20 domain-containing protein 1)

 P20D1_HUMAN             Reviewed;         502 AA.
Q6GTS8; Q6P4E3; Q96DM4;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
28-FEB-2018, entry version 113.
RecName: Full=N-fatty-acyl-amino acid synthase/hydrolase PM20D1 {ECO:0000305|PubMed:27374330};
EC=3.5.1.- {ECO:0000269|PubMed:27374330};
EC=4.3.-.- {ECO:0000269|PubMed:27374330};
AltName: Full=Peptidase M20 domain-containing protein 1 {ECO:0000312|HGNC:HGNC:26518};
Flags: Precursor;
Name=PM20D1 {ECO:0000312|HGNC:HGNC:26518};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS VAL-149 AND TRP-153.
TISSUE=Kidney, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
TYR-33; VAL-149; TRP-153; THR-237; ARG-346 AND THR-380.
TISSUE=Pancreas, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=27374330; DOI=10.1016/j.cell.2016.05.071;
Long J.Z., Svensson K.J., Bateman L.A., Lin H., Kamenecka T.,
Lokurkar I.A., Lou J., Rao R.R., Chang M.R., Jedrychowski M.P.,
Paulo J.A., Gygi S.P., Griffin P.R., Nomura D.K., Spiegelman B.M.;
"The secreted enzyme PM20D1 regulates lipidated amino acid uncouplers
of mitochondria.";
Cell 166:424-435(2016).
-!- FUNCTION: Bidirectional N-fatty-acyl amino acid synthase/hydrolase
that regulates the production of N-fatty-acyl amino acids. These
metabolites are endogenous chemical uncouplers of mitochondrial
respiration. In an UCP1-independent manner, maybe through
interaction with mitochondrial transporters, they promote proton
leakage into the mitochondrial matrix. Thereby, this secreted
protein may indirectly regulate the bodily dissipation of chemical
energy as heat through thermogenic respiration.
{ECO:0000269|PubMed:27374330}.
-!- CATALYTIC ACTIVITY: A N-fatty-acyl-L-amino acid + H2O = a fatty
acid + an amino acid. {ECO:0000250|UniProtKB:Q8C165}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8C165}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6GTS8-1; Sequence=Displayed;
Name=2;
IsoId=Q6GTS8-2; Sequence=VSP_031826, VSP_031827;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A touch of warmth
- Issue 195 of September 2017;
URL="https://web.expasy.org/spotlight/back_issues/195/";
-----------------------------------------------------------------------
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EMBL; AK057131; BAB71368.1; -; mRNA.
EMBL; AK290786; BAF83475.1; -; mRNA.
EMBL; AC119673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039170; AAH39170.1; -; mRNA.
EMBL; BC063477; AAH63477.1; -; mRNA.
CCDS; CCDS1460.1; -. [Q6GTS8-1]
RefSeq; NP_689704.4; NM_152491.4. [Q6GTS8-1]
UniGene; Hs.177744; -.
ProteinModelPortal; Q6GTS8; -.
BioGrid; 127171; 2.
STRING; 9606.ENSP00000356104; -.
SwissLipids; SLP:000001665; -.
MEROPS; M20.011; -.
iPTMnet; Q6GTS8; -.
PhosphoSitePlus; Q6GTS8; -.
BioMuta; PM20D1; -.
DMDM; 317373406; -.
PaxDb; Q6GTS8; -.
PeptideAtlas; Q6GTS8; -.
PRIDE; Q6GTS8; -.
Ensembl; ENST00000367136; ENSP00000356104; ENSG00000162877. [Q6GTS8-1]
GeneID; 148811; -.
KEGG; hsa:148811; -.
UCSC; uc001hdj.4; human. [Q6GTS8-1]
CTD; 148811; -.
DisGeNET; 148811; -.
EuPathDB; HostDB:ENSG00000162877.12; -.
GeneCards; PM20D1; -.
HGNC; HGNC:26518; PM20D1.
MIM; 617124; gene.
neXtProt; NX_Q6GTS8; -.
OpenTargets; ENSG00000162877; -.
PharmGKB; PA162399772; -.
eggNOG; KOG2275; Eukaryota.
eggNOG; COG0624; LUCA.
GeneTree; ENSGT00880000137960; -.
HOGENOM; HOG000245216; -.
HOVERGEN; HBG059923; -.
InParanoid; Q6GTS8; -.
KO; K13049; -.
OMA; ATVNFRI; -.
OrthoDB; EOG091G0BP2; -.
PhylomeDB; Q6GTS8; -.
TreeFam; TF328688; -.
GenomeRNAi; 148811; -.
PRO; PR:Q6GTS8; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162877; -.
CleanEx; HS_PM20D1; -.
Genevisible; Q6GTS8; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:Ensembl.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
GO; GO:1990845; P:adaptive thermogenesis; IEA:Ensembl.
GO; GO:0043604; P:amide biosynthetic process; IDA:UniProtKB.
GO; GO:0043605; P:cellular amide catabolic process; IDA:UniProtKB.
GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
GO; GO:0044255; P:cellular lipid metabolic process; IDA:UniProtKB.
GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
GO; GO:2000275; P:regulation of oxidative phosphorylation uncoupler activity; IEA:Ensembl.
InterPro; IPR036264; Bact_exopeptidase_dim_dom.
InterPro; IPR002933; Peptidase_M20.
InterPro; IPR011650; Peptidase_M20_dimer.
Pfam; PF07687; M20_dimer; 1.
Pfam; PF01546; Peptidase_M20; 1.
SUPFAM; SSF55031; SSF55031; 2.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Glycoprotein; Hydrolase;
Lyase; Metal-binding; Polymorphism; Protease; Reference proteome;
Secreted; Signal; Zinc.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 502 N-fatty-acyl-amino acid
synthase/hydrolase PM20D1.
/FTId=PRO_0000321928.
ACT_SITE 127 127 {ECO:0000250}.
ACT_SITE 191 191 Proton acceptor. {ECO:0000250}.
METAL 125 125 Zinc 2. {ECO:0000250}.
METAL 157 157 Zinc 1. {ECO:0000250}.
METAL 157 157 Zinc 2. {ECO:0000250}.
METAL 192 192 Zinc 1. {ECO:0000250}.
METAL 217 217 Zinc 2. {ECO:0000250}.
METAL 464 464 Zinc 1. {ECO:0000250}.
CARBOHYD 252 252 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 302 361 FPFPVNIILSNPWLFEPLISRFMERNPLTNAIIRTTTALTI
FKAGVKFNVIPPVAQATVN -> VYGEKSLNQCNNQDHHGT
HHIQSRGQVQCHPPSGPGHSQLPDSPWTDSPRGPRTHEEHC
G (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_031826.
VAR_SEQ 362 502 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_031827.
VARIANT 33 33 H -> Y (in dbSNP:rs11540014).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_039380.
VARIANT 149 149 I -> V (in dbSNP:rs1891460).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_039381.
VARIANT 153 153 R -> W (in dbSNP:rs1104899).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_039382.
VARIANT 237 237 I -> T (in dbSNP:rs7518979).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_039383.
VARIANT 258 258 S -> C (in dbSNP:rs11581214).
/FTId=VAR_039384.
VARIANT 346 346 G -> R (in dbSNP:rs11240573).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_039385.
VARIANT 380 380 I -> T (in dbSNP:rs1361754).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_039386.
CONFLICT 84 84 H -> R (in Ref. 3; AAH39170).
{ECO:0000305}.
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


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