ID E4WSS2_OIKDI Unreviewed; 1276 AA.
AC E4WSS2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 7 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSOID_T00005815001 {ECO:0000313|EMBL:CBY06753.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY06753.1};
RN [1] {ECO:0000313|EMBL:CBY06753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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; FN653016; CBY06753.1; -; Genomic_DNA.
DR AlphaFoldDB; E4WSS2; -.
DR InParanoid; E4WSS2; -.
DR Proteomes; UP000001307; 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 Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
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:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..276
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 479..569
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 597..671
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 927..1096
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 144464 MW; 7C758852CA9D822D CRC64;
MITRILEFWA QSGWVELFIA SLIIFITTTA ILFILKNPKK HDDKNGNSDD KSGELSTPPE
SDETKNKLPR QYRRLKRQAT KKFDELRRAT HSKIISIHDK LRDGLPTGQP YFNIPKISHS
GRPLSQKERT QILLKKLLQL EKEPEHLLVK QIPEYLLKGD SDIEIDDRLP IEFMFLLKTV
RVFGHFDKPV FLSLCKHMKV QELKQDEYLF NIGDKDEWIY VVQTGQIDLF VQQGSHEKLI
AEIRPGQSIA SLLSVLDVLT GNAAPYKTVS AKARVDSTII KLPASSILQE FESFPASLVR
IVQMIMLRLQ RVTFLALHDY LGLSEELIDS QAKSSLHRTP SRNSSIKTSV SSDDALNSPN
VNSRRRTSSI TGRRPRFSEV ATVFEVATDD NVSEKTNTAT YKQGKNVNND FNSAIERAFC
RDTDDDCHSD AVGSPSTNKE TPTKTSKKTS FISFFDEELF EDSVQELADI FGLENSDAIA
DKLDMAKVEG GTVICDEGDQ DPCLYYIVSG CLVAQQRCGD RSATLYEATR GSISGQLSVL
TGEPTFFKTT ARENSILLKM QKSDFYALMR DYPRVVLNLA ATVVSRLSKF VRQIDFALDW
VQYEAGQQLF AENEPADCIY IVLSGRLRGV KAEGIVCEFG RGETVGLMDL FRSQYRTLSV
HAVRDTEVAR IPAALMEHIK RLFPSTIQNI IALMTDQVAI NQSHQIMANQ QNIFNKETYG
GLANQLANVS TVAVLTSDPD VPLEIFSIEV ANALNAHGKV QRLASDLVKR RLGERIFEVQ
NEFRLTTWLG QQEDIHRVTI YQCDEKLTGW TKRCLRQADC ILVVALGGSK SKMGSLEHEI
ENFATRALKV LVLLHNEEAE TPHKTAEWLN IRGWLTTHFH IKVPSLMMKK NASRLRKELL
EKIREKNESP FSDFSRLARF ITGRSVGIVF GGGVKMVSKC FQIAFIEQLI AKGIPIDMVG
GTSIGSLVGA LYAKYRDVDT MNVHMKDFCK RMSSLFTKIL DITYPITAMF SGRGFNREIQ
QTVMETQIED LWIPYFAIST DLTVSRMRVH TCGSLWRYVR GSMTLTGYLP PICDPRDGHY
LVDGGYINNL PVDVAKTRGA NIVLAIDVGA REDANLHNYG DYISGWYLLW QKWWPWAKTL
RIPDLNEIQS RLAYIANNHL LEEFINSDAC VYMRIENIDK FATMDFDKFD PIYDFGRENT
SKILTEEIVE NVKSTFSDQS RTLVKKKMKK SPTFVDLAAI FEKLPTPLKT SVSRAFLSEH
SENEDEERLN PGYVSG
//
