ID W1QK61_OGAPD Unreviewed; 1394 AA.
AC W1QK61;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=HPODL_04993 {ECO:0000313|EMBL:ESX02242.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX02242.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESX02242.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) 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 -!- 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:ESX02242.1}.
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DR EMBL; AEOI02000004; ESX02242.1; -; Genomic_DNA.
DR RefSeq; XP_013936828.1; XM_014081353.1.
DR STRING; 871575.W1QK61; -.
DR GeneID; 25774416; -.
DR KEGG; opa:HPODL_04993; -.
DR eggNOG; KOG2968; Eukaryota.
DR HOGENOM; CLU_000960_1_1_1; -.
DR OMA; SSGYVWR; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000008673; Chromosome II.
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|PROSITE-
KW ProRule:PRU01161};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|PROSITE-
KW ProRule:PRU01161};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|PROSITE-
KW ProRule:PRU01161}; Membrane {ECO:0000256|RuleBase:RU362043};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Transmembrane {ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362043}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 586..681
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 710..817
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1092..1256
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 358..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1096..1101
FT /note="GXGXXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 1123..1127
FT /note="GXSXG"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT MOTIF 1243..1245
FT /note="DGA/G"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1125
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 1394 AA; 155098 MW; 9B16490480D6992D CRC64;
MSQWLLALPQ KLVSGFINLL ATSLYLFSAF LYSIATYLAQ VALSFSTVLL IAIVVSLATY
AYIHYRYLTV YSRLPEDPKR QEPSMDTFLE TSGRERKARQ NYLDEFLSAI KIFGYLESQV
FNELTKSMQT QKLDSGEIVF LDENSGFMIC VEGEIEVFCK IGSSNDENAV FTNESSTNYV
IVDDIKYRLL NNVKSGAPLS SLTSVLNLLT ASDLNIPDRQ ASGILPVPSD FDLDNKVFAD
SPVPQPPCLN ETPTLIAIPK NNCTISIIPK DSFTRLAYKY PKATCHIVQM ILTKLYRVTF
QTAHDYLGLT ADIMRTEINL NKQCSNVLPS YLSNNVVEHF MPRLSSYSTL NESHSLLKRS
QSSKLMRSEP IRLDPSSRSV SPGGPISIHT APTSFMATLS SDADESNQSD DMLAMPRSRI
KARRPRSEVP GARNSSRHFS LAARNSTNPG DLVSNVPVSH LDKMASIEKT DKGHRHDRIV
NGENEEPAEM AVRVAIAESI CESIGVDRGS LQVSSPSRMS FSPSVVSSPM VAGITEMNPK
PKGLGIGTRS KVRTFSSHNL GTPNDDEDGT TGSQKSFMDF ENIKSDLANS INLKHVSAGT
KLIEANEHTP GIYYVIDGVL KVTYMNENTD GDPTEEFVYE VKQGGIAGYL GTLIGSKSFV
NVVAAVDCYV AFLPREVFEI LNERFPYLQL AIAKNLLRIL DKRLLLADYA MEWVHISAGD
SLYTQGDPAN GIYIVLNGRF RSMRTPEGKD VQPVIVSEHG QGESLGEVEV LTKTKRDLTL
VAIRDSELAR IPRSLFEMIA LSNPSIMVKV TRIVANRFIH SKEHDGNFEL TTPTAPIKDD
NFSKNFNNYR TITILPITYG LPVVEFGERL TTALENVSKT AKMLTQSTAL SRLGKHAFDH
LAKLKQSGYF SELEDKYDIV IYVADTPVNS SWTKTCIQQG DCILLLADSQ QPPNIGEYER
LLVKNNTTAR TELILLHPER YVEPGSTNNW LKNRIWVHSH HHVQLSFDTN SMPAEVDFGP
ISKSANTSKL LTATTAKLSA NLRNMLSNNE FLQMIKQTRE AFKSKRYYRP MQEHKDDFMR
LARILTGQAV GLVLGGGGAR GISHIGVIAA LEEKGIPVDF VGGTSIGAFV GALYAREYDL
VPVYGRAKTF SGRMGSIWRS LLDLTIPLTS YTTGHEFNRG IWKALGDSRI EDFWIKFYCN
STNITESVME IHTSGYAWRY VRASMSLAAL LPPLTDNGNM LLDGGYIDNL TVEEMKRRGA
HAIIACDVGS EDDRSKMHYG ESLSGLWVLL NRINPFSAHP NVPTMTDIQI RLAYVASVIA
LEKSKNSKDC VYLRPPIEGY ATLDFSKFDE IYGVGSKYAA EVLNKLQSKG ELPSFKTRRR
ELSKHPTLQR RNSI
//