ID A0A094CF11_9PEZI Unreviewed; 1523 AA.
AC A0A094CF11;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=V491_03108 {ECO:0000313|EMBL:KFY21162.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY21162.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY21162.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY21162.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 Responsible for the rapid PC turnover in response to inositol, elevated
CC temperatures, or when choline is present in the growth medium.
CC {ECO:0000256|ARBA:ARBA00024965}.
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:ARBA00000960,
CC ECO:0000256|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
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:KFY21162.1}.
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DR EMBL; JPJT01001769; KFY21162.1; -; Genomic_DNA.
DR HOGENOM; CLU_000960_1_1_1; -.
DR Proteomes; UP000029338; 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 GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
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; 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; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
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:UP000029338};
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 89..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 687..745
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 839..943
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1220..1384
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 212..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..774
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 168033 MW; 66A5C937ECD1002E CRC64;
MSTLEALSAS ALTTSTGIAS SIPRLAATAG SKLSTDMSSP PPSSWLGLLV RLVVSTVKVI
PVILYWVITF TTLTLPSWLF TLFSTSLTFT LNATTVMLII LALVSTLSWF VRYRYLNMYA
RLPPEPQRKE PKVDLFPDTQ EEGTKSGLSS YLDEFLSAIK VFGYLERPVF HELTRSMQTR
KLIAGETLNL EEEKGFCLVV DGLVEIFVKS PTKDNNADSD GSHNGTEVFY SDSDEERQDG
GGHQGYQLLT EVKNGAPMSS LFSILSLFTE DIKLRHTEDD EMDANQSAGR GAHHRSASDV
EHNRGSPPSL AGSPQGERTK ASRRGSIRRD FQDPVQSDSS GLPNIPPMSL DPSNTPRPER
PKPRRAKSNS VHPDIIARAR VDTTIAIIPA SAFRRLTRVY PKATSHIVQV ILTRLQRVTL
ATGHSYLGLT AEVLRTERHM NKYTTYELPN FLRGSALARL KEKFIRERER IGPEDSRKGI
ALHNASAGRR RRSSTSLRKE ATIHALSAKT VATPPTQAPN VDEIASPSPG DLLTNIHFSR
TGGRRHYHVM SPRSPFEQST PNAHSSEDIL SPLTEKTFNP FASPVVHPQL HRQESIDEDG
IFRGSILECI FKAIGLTTTQ SALRMADSVE ASPYLHSTDQ RRPRPAFSNA FGFIDPYEGS
GDGDTESMAS SSTSNFVTVS SQGLATELRD EVEIVYFPKG SVLVEQGERN PGLYYVIDGF
LDVGIPNDDS DDSEFLGRTT KSSSFTSQKS SQFRGSSRGP KSHSRTKRPD SRRRKSSGRT
TLSLIKPGGI AGYIGTISSY RSFIDVTAKT DVYVGFLPRS SLERIVEKYP VVLLTMAKRL
TSLLPKLILH IDFALEWVQV NAGQVIYHQG DESDAIYIVL NGRLRAVLNN EDDDSEMKVV
GEYGQGESVG ELEVMTETCR SATLHAIRDT ELAKFPKTLF NSLAKEHAGI TIKISKIIAS
RMRALIEDPV FLSGNEKATA ATNVKVSSTG NLRTVAIVPI TGGVPVVEFG SRLMNALTQI
GAPNGVTSLN QAAILNHLGR HAFSRMGKLK LSQYLADLEE KYGLVLYIAD TNVNSPWTQT
CISQADCILL VGIADWSPAI GEYERFMLGM KTTARKELVL LHADKFLASG LTRSWLRNRD
WINGGHHHVQ MAFSTDTVPV HPQTRRFGSA LKHRVQIIQA EIQKYTSRKV RQTPLYSADT
PFKGDFHRVA RRLCGKSVGL VLGGGGARGI AHVGIIRALE EAGIPIDIIG GTSIGSFIGA
LYARDADVVP MYGRAKKFAG RMASMWRFAL DLTYPSASYT TGHEFNRGIF KTFGNSQIED
FWLEFYCNTT NISKSRSEIH TSGYAWRYVR ASMSLAGLLP PLCDEGSLLL DGGYVDNLTV
SHMKSLGADV IFAVDVGALD DDTPQNFGDS LSGFWAIANR WNPFSAYSNP PTLSEIQARL
AYVSSVDALE RAKTTPGCLY MRPPIDAYGT LEFQKFDEIY EVGYKFGQEY LADMREKGIL
PLMDETEEKK ALRRTMAPRR ASI
//
