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Database: UniProt
Entry: W1QK61_OGAPD
LinkDB: W1QK61_OGAPD
Original site: W1QK61_OGAPD 
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
//
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