ID A0A096NEP3_PAPAN Unreviewed; 500 AA.
AC A0A096NEP3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Peptidase M20 domain containing 1 {ECO:0000313|Ensembl:ENSPANP00000011370.2};
GN Name=PM20D1 {ECO:0000313|Ensembl:ENSPANP00000011370.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000011370.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000011370.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000011370.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00034626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51313;
CC Evidence={ECO:0000256|ARBA:ARBA00034626};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51314;
CC Evidence={ECO:0000256|ARBA:ARBA00034626};
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:0000256|ARBA:ARBA00034630};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51301;
CC Evidence={ECO:0000256|ARBA:ARBA00034630};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51302;
CC Evidence={ECO:0000256|ARBA:ARBA00034630};
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:0000256|ARBA:ARBA00034640};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51318;
CC Evidence={ECO:0000256|ARBA:ARBA00034640};
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:0000256|ARBA:ARBA00034635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64133;
CC Evidence={ECO:0000256|ARBA:ARBA00034635};
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:0000256|ARBA:ARBA00034637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64109;
CC Evidence={ECO:0000256|ARBA:ARBA00034637};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64110;
CC Evidence={ECO:0000256|ARBA:ARBA00034637};
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:0000256|ARBA:ARBA00034616};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64117;
CC Evidence={ECO:0000256|ARBA:ARBA00034616};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64118;
CC Evidence={ECO:0000256|ARBA:ARBA00034616};
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:0000256|ARBA:ARBA00034627};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64137;
CC Evidence={ECO:0000256|ARBA:ARBA00034627};
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:0000256|ARBA:ARBA00034643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51357;
CC Evidence={ECO:0000256|ARBA:ARBA00034643};
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:0000256|ARBA:ARBA00034652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51361;
CC Evidence={ECO:0000256|ARBA:ARBA00034652};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:51362;
CC Evidence={ECO:0000256|ARBA:ARBA00034652};
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:0000256|ARBA:ARBA00034633};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64193;
CC Evidence={ECO:0000256|ARBA:ARBA00034633};
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:0000256|ARBA:ARBA00034645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64145;
CC Evidence={ECO:0000256|ARBA:ARBA00034645};
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:0000256|ARBA:ARBA00034646};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51353;
CC Evidence={ECO:0000256|ARBA:ARBA00034646};
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:0000256|ARBA:ARBA00034619};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64177;
CC Evidence={ECO:0000256|ARBA:ARBA00034619};
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:0000256|ARBA:ARBA00034625};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64185;
CC Evidence={ECO:0000256|ARBA:ARBA00034625};
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:0000256|ARBA:ARBA00034620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64125;
CC Evidence={ECO:0000256|ARBA:ARBA00034620};
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:0000256|ARBA:ARBA00034641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64129;
CC Evidence={ECO:0000256|ARBA:ARBA00034641};
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:0000256|ARBA:ARBA00034644};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC Evidence={ECO:0000256|ARBA:ARBA00034644};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15567;
CC Evidence={ECO:0000256|ARBA:ARBA00034644};
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:0000256|ARBA:ARBA00034622};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54185;
CC Evidence={ECO:0000256|ARBA:ARBA00034622};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54186;
CC Evidence={ECO:0000256|ARBA:ARBA00034622};
CC -!- PATHWAY: Amino-acid metabolism. {ECO:0000256|ARBA:ARBA00034698}.
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR AlphaFoldDB; A0A096NEP3; -.
DR STRING; 9555.ENSPANP00000011370; -.
DR Ensembl; ENSPANT00000019490.3; ENSPANP00000011370.2; ENSPANG00000011481.3.
DR eggNOG; KOG2275; Eukaryota.
DR GeneTree; ENSGT00940000156659; -.
DR HOGENOM; CLU_021802_11_1_1; -.
DR OMA; NYGDHSG; -.
DR OrthoDB; 3672990at2759; -.
DR Proteomes; UP000028761; Chromosome 1.
DR Bgee; ENSPANG00000011481; Expressed in urinary bladder and 23 other cell types or tissues.
DR ExpressionAtlas; A0A096NEP3; baseline.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:Ensembl.
DR GO; GO:0043605; P:amide catabolic process; IEA:Ensembl.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:Ensembl.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035236873"
FT DOMAIN 240..383
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 500 AA; 55574 MW; 41BEAB4A8B536B33 CRC64;
MAQRCLCVLA LAAMLLLVFA TVSRSMGLRS DEHQRASRIP AEFSKEERVA MKEALKGAIQ
IPTVTFSYEK ANTTALVEFG KYIYKVFPTV LSTSFIQHEV VEEYSHLFTI KGSDPSLQPY
LLMAHFDVVP APEEGWEVPP FSGLERDGAI YGRGTLDDKN SVMALLQALE LLLIRKYIPR
RSFFISLGHD EESSGTGAQK VSALLQSRGV QLAFVVDEGG FILDDFIPDF KKPIALIGVS
EKGSMNLLLQ VNMSSGHSSA PPKETSIGIL AAAVSRLEQT PMPIIFGSGT LVTVLRQMAD
EFPFPVDKIL SNPRLFEPLI TRFMEKNPLT NAIIRTTTAL TIFEAGIKVN VIPSVAKATV
NFRIHSGQTV QEVLELTKNI VADNRVQFHV MTAFDPLPIS PYDDNAMGYQ LLRQTIQSVF
PEVNITIPGT SLGNTDSRFF TNLTTGIYRF NPIYPEDLKR FHGVNEKISV QGYENQVKFI
FELIQNADTD QEPVSHLHKL
//