ID A0A1E3Q5H6_LIPST Unreviewed; 1456 AA.
AC A0A1E3Q5H6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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};
GN ORFNames=LIPSTDRAFT_71208 {ECO:0000313|EMBL:ODQ72933.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ72933.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ72933.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ72933.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454294; ODQ72933.1; -; Genomic_DNA.
DR STRING; 675824.A0A1E3Q5H6; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000094385; 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; 3.
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; 2.
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:UP000094385};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362043}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1456
FT /note="Lysophospholipase NTE1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009134104"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 675..767
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 795..881
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1153..1317
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 261..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 161119 MW; A323E30AC8371232 CRC64;
MPAVPLLLLS FLVERTVSQE ISSNTSGDQI LLTNASMHSA GVTDPNSSGI LSKLIWLGPR
IFVRLLTVCA YYVPAQVLAL LGTSFSITLS FSSLLLIMAA FGAVVWAVVR YKYLNVYSRL
PTEPHRQEPK LDMMFYPNAL QRQYEKPGFA SYLDEFFTGI KVFGYLEKPV FNELTRHVQT
KKLIAGDTML LEEEKGFCIV VDGDVQIYAR THDAEHTHHD DVDGDAEGGY QLLTEVKNGA
PMSSLFTILS LFTEDIKVNT TRSPTSSATH DSLSEETLPI PSDPLISNVG SPKLLPIPNI
PPLSEKVTST VGPDESNTNS SVRQEGTRTT HSTAPGIIAR ASVDSTIAII PAEAFRRLTR
KYPKSAAHIV QVILARFQRV TFQTGHNYLG LTSEILKTEV AFNDLSRYEL PNYLGEDAVA
RIKAQVEARR LSSEQDDEAA VESDSKVERT RNIGELKVSK NPSRRRGSAY VASSLQNRHD
RASQLERGGD FNRVLPGDLV SNTSFSYRGS TSPSSSVLSP SPLLTSASPP ARPAVHTQIS
TASLRSYGGL QFSDFNEPRE QDKIDAVTKD DGEDIDNLKL AILECIFKAL GVSSESVEGK
SPISTSADTS PRLSVYENRR AQQRSNFNFR ATGLGNLGPL AFDGINAGFV DDESVTSSFA
QQSGSMQSYA SIKKELLKDI EILHFTAGSR IVKQGEPNLG LYYVIDGFLD VRTQDRPGEY
KTIYTIKPGG IGGYLGSISG YSSFVDILAT TDVYIGFLAK EAMERLVDRQ PVILLTMAKR
LISILSRLIL YLDFALEWVQ VEAGEVLYRQ GDEADSIYIV LNGRMRAIKE SKGELVLVGE
YGQGESVGEL EVLTSSKRPS TLHAVRDTEV VRFPRMLFES LSMRHPAITI QISRIIASRV
NCLVNNEVMN PLEVPSTTPK SGNFRTVAVV PVTSGLPVKE FGERLAKAFT LLGQTNVTLD
QAAILKHLGR HSFNKFGKLK LSGYLTDLEE RYQMVLYVAD TGISSPWTVT CISQADCILL
LANANADPSI GEYERMLIGM KTTARKELVL LHPDRYVPAG QTQSWLKSRI WIHSHHHVQM
QFRNTVPRTT TAYFGSRFRD LKNKVQTTLQ TELQKYRHTS RLSPASPVYT SNQTHKNDFA
RLARLLSGKA VGLVLGGGGA RGLSHLGVIR ALEEAGIPID IVGGTSIGSF VGGLYARDAD
IVPIFGRLKK FSGRIGSLWR MFFDLTYPAT SYTTGHEFNR GIWKAFGDAR IEDFWLQYYN
NTTNITHSRM EIHSAGYAWR YIRASMSLAG LLPPITDNGS MLLDGGYVDN LPVSHMKLLG
TEVVFAVDVG SIDDTTPMTW GDSLSGFWVL FNRWNIFSRH PNVPSMAEIQ ARLAYVSSVG
ALEKAKSSPG CIYLRPPIDH YATLDFGKFE EIYRVGYDFA KEFLNNMQRD GKFPKIAGMS
HFDGTSRRII QRRNSI
//
