ID A0A120E9L6_9BASI Unreviewed; 1449 AA.
AC A0A120E9L6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
DE Flags: Fragment;
GN ORFNames=RHOSPDRAFT_14195 {ECO:0000313|EMBL:KWU47420.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47420.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU47420.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU47420.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; KQ954464; KWU47420.1; -; Genomic_DNA.
DR STRING; 1305733.A0A120E9L6; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000062823; 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; 4.
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:UP000062823};
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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 633..752
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 765..867
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1144..1308
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 149..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KWU47420.1"
SQ SEQUENCE 1449 AA; 158530 MW; 9BE59DF1FAC52B10 CRC64;
TLSLPSLAFS ALHYSASLTF HLTFLKIVAF LLIVTTIASY VWKVRYLNRY TELRDLPGGN
RIKGDVGFDL DPDLANDQTA SGFHNYLDEF LSAIKVFGYL EKPVFHELAR HLQTRRLVAG
DTLDLSQDKS FYIVVDGRVE VFARTPQAAT NGADDYGSDT DPSDDDAEGK GWQLLNNVES
GGTLSSLFTI LRLFTEDVKL RYEEDKDAAE ESSASDDGGA AAAFAKQHRE RDADVSTFEL
DGGAIHAARR AARPNLASRD FGSLNTAALN DTDDADVEDA ARADDTETTL ASPYEDTEAE
NETLHDRGQL DHLDSTIAPQ STGPQTIAGE STIARAATDT TLAVIPAEAF RRLTKKFPNA
AAHIVQVILT RLQRVTFLTA HKYLGLTREV VRTEKAINDL ACYPLPPAFW ESGGIQRLRA
RFVPETKLDG PYEHDAAVLA ARRYNVPLMT PYAGPKMGEV FWDEVNVEHS SDDGVRLKYR
APNSSLLGSP ASRRPLRKAG DLLTMSSVAP SQGMLPVQTP RLERTKTDRT DDGGERDFDL
REAVMECISK AIGLVQPHVT PSQSAEASPA LRPHERQTSA NGTLRDQAAF NSSFGSLSML
GLSGLNDDES SISSLSSLRN ADAGAVGSFT SMDLENEVEI LYFPQGSVLV KEGERNAGLY
FVIDGFLDVS MPETQPATGP KVTRKQTPVG SDGTASPASP SKAKSIHLFT VRPGGIAGYL
SSLSGFPSYV DITAKTECYV GFLPAKALER IMDRKPIVLL TLAKRLISLL SPLVLHIDSA
LDWMHVSAGQ VIYRQNDSAD SFYIVINGRL RSITDRQEGG IQVQAEHGQG ESVGELDCIT
STPRPTTLHA IRDTELARMP MTLFNAISVR HPLVTIQISR IIAARLRLQV TRESKLQGGL
PKELGAPGMG DNGMGKNNFN LKTVAVIPTN RHVPVSEFAS KLHAALEGIG APTSYLNQAT
VMQVLGRHAF SKMGQLKLAG WLAETEQKYR IVLYVADTAI SAPWTQTCIR QADCILVVAD
AGAEPDLGEH EKLLVSMKTT ARKELVLLHA ERNVISGSTR PWLRNRPWVH AHHHVEMLGA
TPEVNRSQVH NPTAVVALQK LAARFELEIS KYKKAAPRPV PQRAPAFSDF ARLARRLCGK
SIGIVLGGGG ARGISHVGVL RALHDRGIPI DMVGGTSIGA FVGGLYAKEG DLVSMYGRAK
RFSGRMSTLW RILTDLTYPV VAYTTGHEFN RGIYKSFYDT HIEDMWLPYF CNTTNITHSR
MDVHTSGYAW RYVRASMSLA GLLPPLCDEG DMLVDGGYVD NLPVSVMLGQ GAASVFAIDV
GSVDDTSPRN YGESVSGWYL LLQRWNPFGK QPNIPNITEI QSRLTYVSSV KMLEEAKATP
GVLYMRMPVT QFGTMEFKRF TEILDVGSEF ANSLLDEWAA DKKLPTGMEG DAVAPRKQKR
GQPIRRNSI
//
