ID A0A099YTR3_TINGU Unreviewed; 1313 AA.
AC A0A099YTR3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Patatin-like phospholipase domain-containing protein 7 {ECO:0000313|EMBL:KGL72777.1};
DE Flags: Fragment;
GN ORFNames=N309_01359 {ECO:0000313|EMBL:KGL72777.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL72777.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL72777.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL72777.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL885225; KGL72777.1; -; Genomic_DNA.
DR STRING; 94827.A0A099YTR3; -.
DR Proteomes; UP000053641; 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:UP000053641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..272
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 482..563
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 591..696
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 925..1091
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 1280..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL72777.1"
FT NON_TER 1313
FT /evidence="ECO:0000313|EMBL:KGL72777.1"
SQ SEQUENCE 1313 AA; 146235 MW; 75885FFEB5F972A2 CRC64;
FVEDRIQTTM LTGIAIGAAV AIFLIGIVVF LVYRRVKQSK QLQPHVPQYR FRKRDKVMFY
GRKIMRKVTT LPNSLVGNTV PRQRMRKRAK VLSLAKRILR IKKECPTLQP KEPPPSLLEA
DLTEFDVKNS HLPSEVLYML KNVRVLGHFE KPLFLELCKH MFFVQLHEGE YIFRPGQLDN
SIYVVQDGKL EVCIQESDGT EVVVKEVLAG DSVHSLLSIL DVITGHPAPY KTVSARAAVP
STILRLPASA FQDVFQKYPE TLVRVVQIIM VRLQRVTFLA LHNYLGLTTE LFNCQSQAIP
LISVASVTSG GKSTEQNFVT LNGRLFSKGR GSWSPASEGA GCRRFGSSST AAVCGIPARL
CSANGLASCS SFQLPSVPLS NSSGAKSDMD MAYERARVHF GSEDTGSSPA GSKSILKKTV
TVTETPSAVF HYTDRELAVQ DSSNSKPIDA IFEAAKKDLS TLMKLDDPLL LNGKVTLHQV
TAGTVVSRQG DQDVNVCFVI SGMLHVYQRK IDSEEDTCLF ITHPGELVGQ LAVLTGEPLI
FTIKANRDCS FLSISKSHFY EIMREQPSVV LGVAHTVVKR MSSFVRQIDF ALDWMEVEAG
RAVYRQGDKS DCTYIVLNGR LRSVIRMDDG KKHLTGEYGR GDLIGVVEAL THQPRATTVH
AVRDSELAKL PEGALTSIKR KFPQVVTRLI HLLGEKILGS LQQGGHPLGL HTSSSKWDAG
NPANNLSTVA IMPVSEEVPL TAFTLELKHA LSAVGPALLL TSDNIKQRLG SAALDSIHEY
RLTSWLGQQE DIHRIVLYQA DSTLTPWTQR CIRQADCILI VGLGDQEPTV GELERMLENT
AVRAQKQLVL LHKEDGPLPS RTVEWLNMRS WCSAHLHLHC PRRVFSRRSL PKLIEMYERV
FQKAPDRHSD FSRLARVLTG NAIALVLGGG GARGCSQVGV IRALIEAGIP VDMIGGTSIG
AFMSALYAEE RSYNQMRIKA RQWAMDMNSV FKTILDLTYP ITSMFSGASF NNGINNIFKD
KQIEDLWIPY FTITTDITAS TMRVHTDGSL WRYVRASMSL SGYMPPLCDP KDGHLLMDGG
YINNLPADVA RSMGAKVVIA IDVGSRDETD LTNYGDCLSG WWLLWKRWNP LVEKVKVLNM
AEIQTRLAYV CCVRQLEMVK NSDYCEYIRP PIDRYGTLDF GKFDEICEVG YQHGKTVFNV
WCRSGVLDKM LKDRQETCKS KTSDNVTCPS PSFTDLAEIV SRIEPVKAPV ADDESDYQTE
YEEEILDSQK DDYINFLSNQ VEEDSDSDED VQIRQRKNLP NSDCQANSTG EQA
//
