ID A0A091UA59_PHORB Unreviewed; 1204 AA.
AC A0A091UA59;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Patatin-like phospholipase domain-containing protein 7 {ECO:0000313|EMBL:KFQ87574.1};
DE Flags: Fragment;
GN ORFNames=N337_03934 {ECO:0000313|EMBL:KFQ87574.1};
OS Phoenicopterus ruber ruber.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC Phoenicopterus.
OX NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ87574.1, ECO:0000313|Proteomes:UP000053700};
RN [1] {ECO:0000313|EMBL:KFQ87574.1, ECO:0000313|Proteomes:UP000053700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ87574.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000256|ARBA:ARBA00024569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000256|ARBA:ARBA00024569};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC Evidence={ECO:0000256|ARBA:ARBA00000355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000256|ARBA:ARBA00000355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|ARBA:ARBA00000150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000256|ARBA:ARBA00000150};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004643}. Membrane
CC {ECO:0000256|ARBA:ARBA00004183}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004183}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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DR EMBL; KK425176; KFQ87574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UA59; -.
DR Proteomes; UP000053700; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00038; CAP_ED; 3.
DR CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF23; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 7; 1.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..264
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 460..541
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 569..674
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 903..1069
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ87574.1"
FT NON_TER 1204
FT /evidence="ECO:0000313|EMBL:KFQ87574.1"
SQ SEQUENCE 1204 AA; 134671 MW; 473DC01588B3B632 CRC64;
SQLTGIAIGA AVALLLIAVV VFVVYRRVKQ SKQLQPHVPQ YRFRKRDKVM FYGRKIMRKV
TTLPNSLVGN TVPRQRMRKR AKVLSLAKRI LRIKKECPTL QPKEPPPSLL EADLTEFDVK
NSHLPSEVLY MLKNVRVLGH FEKPLFLELC KHMFFVQLHE GEYIFRPGQL DNSIYVVQDG
KLEVCIQESD GTEVVVKEVL AGDSVHSLLS ILDVITGHPA PYKTVSARAA IPSTILRLPA
SAFQDVFQKY PETLVRVVQI IMVRLQRVTF LALHNYLGLT TELFICQSQA IPLISVASVT
SGGSSSKAVK RQVSNVSEED RGEKFEKAGE ALEIEPILFL SSNLYLKKQK YEKNVVTEGK
RRNSSGAKSD MDMAYERARV HFGSEDTASS PVVGKSILKK TVTVTETPSA VFHYSAVQDS
CNSKHIEAIV EAAKKDLSTL MKLDDPSLLN GKVTLHQVTA GTVLSRQGDQ DVNVCFVVSG
MLHVYQRKID SEEDTCLFIT HPGELVGQLA VLTGEPLIFT IKANRDCSFL SISKSHFYEI
MREQPSVVLG VAHTVVKRMS PFVRQIDFAL DWMEVEAGRA VYRQGDKSDC TYIVLNGRLR
SVIRMDDGKK HLTGEYGRGD LIGVVEALTH QPRATTVHAV RDSELAKLPE GALTSIKRKF
PQVVTRLIHL LGEKILGSLQ QGGHPLGLHS SSSKWDAGNP ASNLSTVAIM PVSEEVPLMA
FTLELKHALS AVGPALLLTS DNIKQRLGSA ALDSIHEYRL TSWLGQQEDI HRIVLYQADS
TLTPWTQRCI RQADCILIVG LGDQEPTVGE LERMLENTAV RAQKQLVLLH KEDGPLPSRT
VEWLNMRSWC SAHLHLHCPR RVFSKRSLPK LIEMYERVFQ KPPDRHSDFS RLARVLTGNA
IALVLGGGGA RGCSQVGVIR ALIEAGIPVD MIGGTSIGAF MSALYAEERS YNQMRIKARQ
WAMVMNSVFK TILDLTYPIT SMFSGAAFNN TINNIFKDKQ IEDLWIPYFT ITTDITASAM
RVHTDGSLWR YVRASMSLSG YMPPLCDPKD GHLLMDGGYI NNLPADVAKS MGAKVVIAID
VGSRDETDLT NYGDCLSGWW LLWKRWNPLA EKVKVLNMAE IQTRLAYVCC VRQLEMVKNS
DYCEYIRPPI DRYRTLDFGK FDEICEVGYQ HGKTVFNVWC RSGVLDKMLR DRQETCKSKT
DVSV
//
