ID M3CDX0_SPHMS Unreviewed; 1520 AA.
AC M3CDX0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=SEPMUDRAFT_150206 {ECO:0000313|EMBL:EMF11221.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF11221.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF11221.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF11221.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB456266; EMF11221.1; -; Genomic_DNA.
DR RefSeq; XP_016759342.1; XM_016906020.1.
DR STRING; 692275.M3CDX0; -.
DR GeneID; 27903157; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR OMA; SSGYVWR; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000016931; 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:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
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; 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; 1.
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.
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:UP000016931};
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..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 679..762
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 835..937
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1216..1380
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 209..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 168226 MW; 9DDCF4B11C4023D8 CRC64;
MDGSVTPSGS ASLSAATQQL AAQVSLHAPD SSVTPDSARS TLSMLGGLTL GIFTVVPSIL
YWTITFVTYT LPTWLFSFLS TSMTFTMNMT TLLLVLVVMA STVSWFVRYR FLNMYSRLPP
EPQRKEPQIE IFPGSEENDS KPGLGNYFDE FLSAIKVFGY LERPVFHELT RTMQTRKLIA
GETLLLEEEK GFCLVVDGLV QIFFKSNRDQ DSDSANENGA DEDHVEDRGS GHGSYQLLTE
VKNGAPMSSL FSILALFTEN VKLRFDEDEH LNTSGSSGNL KHQFRMPPHA ENGTPELGTD
GGRHWVGGSR PASRQRTSSN AHNGGYPYSS REPPPLTLDG SASTDDGIQH QHSRRPSYAR
ADSTRTRKRK QASAHPDIVA RATVDTTIAI IPASAFHRIT RMYPKATAHI VQVILTRLQR
VTLATASSYL GLTSDVLRTE RLMDRYTSYD LPDFLRGEAM SRLKDKFRKD LERVEPEELT
KGIALHNPRI AQRRRTSSTL QRDVAMRARM SAANSIEVGR ERGGMSAGDL LTNIHAQRDS
GRVRGERGSF SHPYSTPRIN GEDIDLTSRR DGREHFSPRM NPRATLHRQE SIDEDAIFRE
SIMDCMAKAI GLTNSRDGGR MPESVAQSPR LVSYDRRSQS AVFNNAAFGF MDSFDGSQDD
GDSVASASAF SVGGSANIME DLKNEIEIVY FPKDSVLVEE GERNPGIYYV IDGFLDVSAS
MEQEAHSNVL GTLARPGGAE SADLFGPKSL PSDDKRSSSV GASEHHKRKK SGRIPKSLHL
IKPGGLAGYL GTVSSYRSLI NVSAKTDVYV GFLPRMAIEK IVERHPVVLL TMAKRITSLL
PRLILHIDFA LEWVQVNAGQ AIYNQNEESD AIYIVLNGRL RAIQENEDNK MKVIGEYGQG
DSVGELEVLT ESTRPGTLHA IRDTELAKFP KTLFNSLAQE HPGITIKVSK IIASRMRALI
ENPMNEHESY NKLKVQRPKV TTTSNLRTVA VIPCTAGVPV VEFSNKLQAA LNQIGTPNGV
CVLNQSSILN HLGRHAFSKM GKLKLTQYLA DLEEKYGIVI YVADTSVKSP WTQTCISQAD
CIYLVGLAEG SPAVGEYERF LLTTKTTARK ELILLHSERY CPSGTTRSWL RNRSWISGSH
HHVQMAYRAT PEPVHPHTAG KRLGNAIKQR VQVIQAEIHK YTSRRVRQTP LFSAETPFKG
DFHRLARRLC GKSVGLVLGG GGARGLAHVG VIRALEEAGL PIDIIGGTSI GAFVGAVYAQ
DADVVPMYGR VKKFAGRMGS MWRFALDVTY PSASYTTGHE FNRGIFKTFG DSQIEDFWLE
YYCNSTNISK SRPEVHTSGY VWRYIRASMS LAGLLPPMCD EGSMLLDGGY TDNLTVSHMK
ALGADQIFAV DVGSLDDDTP QAYGDSLSGF WASINRWNPF SSYPNPPTLS EIQARLAYVS
SVDNLERAKN IPGCRYMRPP IESYGTLDFG KFDEIYQVGY QYGKKFLADL RDEGVLPGLE
AVSEEERNLR RTMAPRRASI
//
