ID F4NXA8_BATDJ Unreviewed; 1466 AA.
AC F4NXA8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN ORFNames=BATDEDRAFT_9648 {ECO:0000313|EMBL:EGF82642.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF82642.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF82642.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC (GroPCho). Plays an important role in membrane lipid homeostasis.
CC {ECO:0000256|RuleBase:RU362043}.
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|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU362043}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
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DR EMBL; GL882880; EGF82642.1; -; Genomic_DNA.
DR RefSeq; XP_006676537.1; XM_006676474.1.
DR STRING; 684364.F4NXA8; -.
DR GeneID; 18245074; -.
DR HOGENOM; CLU_000960_1_1_1; -.
DR InParanoid; F4NXA8; -.
DR OMA; SSGYVWR; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 3.
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; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
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; 2.
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; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362043};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362043};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362043};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362043};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362043}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 147..213
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 659..780
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 791..881
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1156..1324
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 268..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1466 AA; 162523 MW; F0514B0044BB9662 CRC64;
MVNEPLDSQS TTTVTAQPII SIGKPSDDHD TQTSALSDTA TIVALILRLI FGHTPWLVYR
FLSYTVTATI TLDLWSVLGL LSLISLVVYL LIRYRLLNTY THLKTPAPIA PRAPFDLQPD
ATLDDDTDLN KGYPDEFMNA FLSSIKVFGY LDKPVFHELA RHLQTRKLKT GEILFDEDSE
DRDFYVVVDG CVQIYLKGNS NALARHSLGS NNFEDRSDSD DPEDEFSGHH LLNEVKAGET
VSSLFTILSL FTEDFELSTL MQPHSAATNL NESHGTSFSS KHSGFPQAQS PAFSTQLDSD
ESAWLRFNHL QQDSSIDSTP TPETAHPDAK PPHGLDGSED HKHFTHPTSG NHIPKRKHRS
VHPGIITRAS SPTTLAVIPA QAFRKLTEKF PNAAAHIVQV ILTRFQRVTF LTLYRYLGLS
KELLKIERQV NQFSGYGLPT DLFPPEILHD LRLRTIRKRR GINNTFVTNE VDSSNGNEVD
RRMSEMPGSR GTYNVNDDTA SLTISMGLTH SQQRNHRRAH RNVVEINEYN NTADSSENDT
AGPAKPPRKP NAKSSYRPTR LNDEADGPIK EAVFKCIAQL IGMRPYSGPP GHSNLAPMTD
RLYYSRSRTS WKPTSSTVFS IGSARASHPK TPDETTSPSN STGNFSIDSS DQVEIDIMYF
EHGQTLVKEG ERGAGLYFVL DGVLEASMST SNSQLFPIRT GDASQNSNPS SRGKSRRNLF
LIHPGGLAGY LAALTGQTSF VTIKAKTDAH VGFMSKQVLD KYVERFPDIL LCLAKRLVNQ
LSPLVLHIDV ALEWGQVNAG QVLCRQGEPS TSIYIVLTGR LRAIVERSRN GIESLDILGE
YGQLESVGEM EVLMDAPRTA TIHAIRDTEV AIMPKTLFNA LAIGHPEITI SIARIIAARS
TQSFLGKMGP GQQPSFNMRG SPDSGNNNVN LKTVAILPVT SIVPVFEFAD HIRDALQLIG
ASVAFLNTAS VMRELGKHAF TRLGRLKLMS WLSEQEESHR LVLYVADGGV SSPWTQRCVR
QADCILLVGL GDEDPGIGEF ERLLIGMKTT ARKELVLLHN QRACIPGSTA QWLKNRVWVH
AHHHVQMNLN TPKLLNKTTQ KQLTLINLKS HFQRVYTSMY PMNSTGKKSS APNIYSGVRS
DFARLARRLL SKSIGLVLGG GGARGFAHIG VIRAFEEAGI PVDMIGGTSM GSFVGGCYAR
ENDHVSVYGR AKMLGGRLGS TWRSLIDLTY PITAIFTGKS FCHEFNRGIW KVFSDTQIED
CWISYFAVTT NLNWSRMEVH QTGYMWRYIR ASMSLSGYLP PLCDHGSMLL DGGYINNLPA
DIMHSLGAHT IIAVDVSLAD DTSPVSYGDS VSGWWMLLSK LNPFPQSYSF RPPEIADIQS
RLTYISSVKQ LEDAKRIDGC LYIHPPVAAY TAMDFKKFKE IVEVGYKFGQ TVVQEWHNNG
TLQRQLGVTL ADSVERKLRG GRRASI
//
