ID K9IUQ6_DESRO Unreviewed; 1268 AA.
AC K9IUQ6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative patatin-like phospholipase domain-containing protein 7 {ECO:0000313|EMBL:JAA53173.1};
DE Flags: Fragment;
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA53173.1};
RN [1] {ECO:0000313|EMBL:JAA53173.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA53173.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-
CC octadecenoate + H(+) + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40807, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:28610, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000256|ARBA:ARBA00024569};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC Evidence={ECO:0000256|ARBA:ARBA00024569};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57597;
CC Evidence={ECO:0000256|ARBA:ARBA00000355};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC Evidence={ECO:0000256|ARBA:ARBA00000355};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000256|ARBA:ARBA00000597};
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:ARBA00000150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000256|ARBA:ARBA00000150};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004643}. Membrane
CC {ECO:0000256|ARBA:ARBA00004183}; Single-pass type III membrane protein
CC {ECO:0000256|ARBA:ARBA00004183}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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DR EMBL; GABZ01000352; JAA53173.1; -; mRNA.
DR AlphaFoldDB; K9IUQ6; -.
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 CDD; cd00038; CAP_ED; 3.
DR CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
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; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF23; PATATIN-LIKE PHOSPHOLIPASE DOMAIN-CONTAINING PROTEIN 7; 1.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}.
FT DOMAIN 105..232
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 421..509
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 537..642
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 874..1040
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 273..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAA53173.1"
SQ SEQUENCE 1268 AA; 139476 MW; EF0E63AD46787CA9 CRC64;
QVQPTPQYRF RKRDKVMFYG RKIMRKVSTL PNTLVGNTAA PRQRVRKRTK VLSLAKRILR
FKKEYPTLQP KEPPPSLLEA DLTEFDVKNS HLPLEVLYML KNVRVLGHFE KPLFLELCKH
MVFVQLPEGA HVFRPGEPDT SIYVVQDGRL EVCVQDADGT EVVVKEVLAG DSVHSLLSIL
DVITGHTAPY KTVSARAAAP STVLRLPVVA FQGVFEKYPE TLVRVVQIIM VRLQRVTFLA
LHSYLGLTTE LFNPESQAIP LVSVASVAAG KAKRQASYGP EEPGDPADRG GSRAAASGLL
LKRSHSVPLP SVHETSDELG KAQAGDQAPA APPGAASDPR TACDRARVPL HAEERPGSVV
AGKPKKSVVV AETPSAIFHY SDGNSDEPVA SSKTDAIFRA AKKDLLTLMK LDDPSLLDGR
VTFLHVPGGT VVSRQGDQDV NIVFVVSGLL HVYQRKIDSE EDSCLFVARP GELVGQLAVL
TGEPLIFTVR ANRDCSFLCI SKAHFYEIMR KQPNVVLGVA HTVVKRVSSF VRQIDFALDW
MEVEAGRAVY RQGDKSDCTY IVLSGRLRSV IRQDDLKKRL AGEYGRGDLI GVVETLTHQP
RATTVHAVRD SELAKVPSGA LTSIKRRYPQ VVTRLIHLLG EKILGSLQQG TAPGHQFGLH
SAGSKWDSGN PASNLSTVAV LPASEDVPLT AFALELRHAL SAIGPVLLLT SDNIKQRLGS
AALDSIHEYR LSSWLGQQED IHRIVLYQAD STLTPWTQRC IRQADCILIV GLGEQEPTVG
ELERMLESAA VRAQKQLVLL HREDGPAPAR TVEWLNMRSW CSGHLHLRCP RRVFSRRSLP
KLVELYERLF QKPPDRHSDF SRLARVLTGN AIALVLGGGG ARGCAQVGVI RALTECGIPV
DMVGGTSIGA FMGALYAEER NYSQIRIRAK QWAEDMTSMV KTVLDLTYPI TSMFSGAGFN
SSICSVFKDR QIEDLWLPYF TITTDISASA MRVHTDGSLW RYVRASMSLS GYMPPLCDPK
DGHLLMDGGY INNLPADVAR SMGAKVVIAI DVGSRDETDL TNYGDALSGW WLLWKRWNPL
ATKVKVLNMA EIQSRLAYVC CVRQLELVRS SDYCEYLRPP IDGYGTLDFG KFTEICEVGY
QHGRTVFGIW TRGGVLEKML QDRQGTSKMK AGDVLTCPNA SFTDLAEIVS RIEPAKVAVV
DDESDSLTEC EEGLPDGSQD AYADFQSAPA DAGSDSEDEP SLHHQHARLD PPRPPQDSSA
PWRSDPDG
//
