ID A0A1C7N5X1_9FUNG Unreviewed; 1303 AA.
AC A0A1C7N5X1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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};
DE Flags: Fragment;
GN Name=nte1 {ECO:0000313|EMBL:OBZ84427.1};
GN ORFNames=A0J61_07523 {ECO:0000313|EMBL:OBZ84427.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ84427.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ84427.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ84427.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-2016) 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}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000256|ARBA:ARBA00008045}.
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:OBZ84427.1}.
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DR EMBL; LUGH01000512; OBZ84427.1; -; Genomic_DNA.
DR STRING; 101091.A0A1C7N5X1; -.
DR InParanoid; A0A1C7N5X1; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000093000; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.370; -; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR009053; Prefoldin.
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; 1.
DR Pfam; PF01734; Patatin; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF46579; Prefoldin; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51635; PNPLA; 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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000093000};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 480..574
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 887..1051
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OBZ84427.1"
SQ SEQUENCE 1303 AA; 144002 MW; C5B79CEA7080C3EA CRC64;
FPKAAAHIVQ VIVTRFQRVT LMTSHRYLGL TKELLRLEKL VNESAINLNE LPPNFFAPGG
MDRLRRKFND EETSSQEDNG SLSPAEISRS ESSGIIRAIG IIDIPGTPSL HINSPANNSS
TNVNESPTSA GKAGSPNLRR QKLNRRGEYS MEDDEHLRTS VMQCLANALG IKVKPNNDTP
HDMQSPHSLT MSPRNPRRFP QYPMDLFSHA GTVDTSNSPS LDALDSAYDD DMDVRSTTSS
VHSSNTNSDI FSNKHHKASE SISADDVQIL YFPKDAVLVR EGVHNSGLFF VIDGLLEASM
TPATGEDVLN DVTSSDSKGK KSKSRAQGAY RRKPRIIDPD LTLSPSSSTS SASAQQPASR
ADDNGVKYIK YNASNGKEDK VVASKAPAGR SKETDDNKDD PEKVKKPVYI IKPGGLTGYL
DALTGFPSFV EIKAKTDTYV GYVSKKRLDR IMDKNPAVML KLANELVGHV SPLILHIDLA
LEWMQVNAGQ IIRKEGEPSN DLYMVLHGRL RTIHEKKDGQ IEIIGEFGHG DSVGELEVLT
GIPTAATLHA IRDTELARMP KTLFNALAMR HPEITLQISR MVAFRSLQLV THNNSTHGSG
QGPKVLQLKP TADASAAISS ITDAAPNRYP ELYGRNNVNL KTVGIIPVNS SVPVTEFAES
LKTELLHSVG ATCALLNSAT VTTMMGKYAF SRLGKLKMAS WLAEQEEKYR IVLYLADSGV
TSQWTRTCIR QSDCILLVGL GDGDPSVGEY ERFLINMKTT ARKELVLLHG ERSCTSGTTQ
NWLKNRLWIQ AHHHIYMPMK QHATLTANER FRPPWLAEQG RKMTAGSINM LANVKDQIKE
YYSAVPNFGR LLDVKKSTTN SLNTMHSPSR NDFARLARRL CGKSVALVLG GGGARGIGHV
GVIQAIEEAG IPIDIIGGTS IGSFVGGLYA KNMDLVSVIA RSKMFAGRVS SIWRQLMDLT
YPVTAWFTGH EFNRAVWKCV GDSQIEDYWL PYFAVTTNIT FSRMEVHTTG YAWRYIRASM
SLSGYMPPIC DNGNMLVDGG YMDNLPVSVA KSMGADIIIA VDVASEDDTS PVHYGDSISG
WWALLHGFNP FRTYNVPSIA DIQSRLAYVS SVAKLEEAKI TDGTMYLKLP VQQWGTLEFA
KYNDIFQTGY EVGREVVSRW RKAGYASGRI NDSVADSKSI GKEVKGKRGR RNSVFVELQS
KYVHSQQQAN TTKAQIATKQ RERKLAELTR RELDGLDDET KTYKPIGKMF IQSPLKDMKQ
QYVDAVTKAD EDIKGLEKSQ KYWERAAYDA QANLKDILQG PRT
//
