ID A0A2B4RUQ7_STYPI Unreviewed; 1139 AA.
AC A0A2B4RUQ7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Putative carboxypeptidase PM20D1.2 {ECO:0000313|EMBL:PFX21331.1};
GN Name=pm20d1.2 {ECO:0000313|EMBL:PFX21331.1};
GN ORFNames=AWC38_SpisGene14176 {ECO:0000313|EMBL:PFX21331.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX21331.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
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 G-protein coupled receptor 1 family.
CC {ECO:0000256|RuleBase:RU000688}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX21331.1}.
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DR EMBL; LSMT01000281; PFX21331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4RUQ7; -.
DR STRING; 50429.A0A2B4RUQ7; -.
DR EnsemblMetazoa; XM_022941754.1; XP_022797489.1; LOC111335758.
DR EnsemblMetazoa; XM_022941770.1; XP_022797505.1; LOC111335773.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00637; 7tm_classA_rhodopsin-like; 1.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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; PF00001; 7tm_1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:PFX21331.1};
KW G-protein coupled receptor {ECO:0000256|RuleBase:RU000688};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Receptor {ECO:0000256|RuleBase:RU000688};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transducer {ECO:0000256|RuleBase:RU000688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000688};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..322
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 425..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 129190 MW; D29E509927CBFE33 CRC64;
MAVNLNSTED SNKETLSFKV FKITMYSLIL LLCLLGNTLV IIVICKMKRM RNPSNLLILN
LAVCDLITPL ASIPFDLALE EKGYIWPFGR ILCKTLWPLA TLSAISASLT LAIISLDRYR
VIMHPFKQRL SSKQVKCSIV IMHFVALLFV VPYIYYLNLV GEGSTKSCEE TWPAFHYRQV
YTLALFIGQY GIPLAFMSVM YTMTLSNLRS SANMFEKVQQ RPSQVNVVGN YNNRQMDFQR
KASRVTIGQR HNSLLGKANQ NIRATKMFVT VVIVFATCRL PNEIFWLWSD FGDGLNQDHS
QIVGIICRMF TYTNSIFNPV IYWIFSRDFK RGFRRILTSL CKRKQDGSFD DSVDRSELSY
LRKISSISES FSFVWRKLSR SRSDNGGPLE LKENQRLYKH SISNSPESSH RKASRKISFL
REGFANDPDK TLSGTTNRNN PGSVQLDDSF RFIKLQSQPR LEKINEEPSF KPAQEHGMVR
IRRFGIVETP NAQPLNEQLI MKTTQPATDD LSFSPNEMIG DTTESMDLVP RKNSQPTADK
VSSLEIKRSF DDIKNDGGVD CEKKAFLNHR DLTSVYFQFS PSLLNLAALK ETQSVMNFTN
FVYAVPISAT YHEKAKYNYK NETPQERLTH KVNMAGVREL SYLLVTALGT VILIVIARTV
MYSHQPTAAY PCRPSDLDYI NADEDVKRRF QTALSFQTVS WNVGNYNREE LYNFLQFILK
EFSDVFSHPL VEPRVIGNYS LLISIKGSNT SLKPYLIAGH FDVVPATNES WDVPPFEGRV
QDGYFWGRGT LDHKNGVMGS LEALNFLLKQ GHQPQRSFFL AFGHDEEVLG IDGAKQIAVY
LRSQGVKLEF LVDEGTVIVK DALPGLKMPY ALIGVAEKGY IMAELSVQTS AGHSSMPPRQ
TSIGILSNAV VKLEACPMPA VFDSSGPVRE MFENFTPQVP VYLRPIIANL WLFSPIVVRI
LEKKPATNAF LRTTTAVTQF NAGVKANVIP SSARVTVNHR IHPSNTIEEV LEHDRRCIND
DRVNIRVVQS EKPSPLSSWD KHSFGFQVIS QSVRQVFPEV GVSPGLMIAN TDTKYYLDLT
DAVYRFMPSV LTPEDTKRIH GFNERIGVKN YEKTINYFYH VMINADAARL DTDTQHTEL
//
