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Database: UniProt
Entry: A0A3Q2I1N1_HORSE
LinkDB: A0A3Q2I1N1_HORSE
Original site: A0A3Q2I1N1_HORSE 
ID   A0A3Q2I1N1_HORSE        Unreviewed;      1404 AA.
AC   A0A3Q2I1N1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Patatin like phospholipase domain containing 7 {ECO:0000313|Ensembl:ENSECAP00000040937.2};
GN   Name=PNPLA7 {ECO:0000313|Ensembl:ENSECAP00000040937.2,
GN   ECO:0000313|VGNC:VGNC:21637};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000040937.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000040937.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040937.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000040937.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040937.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   STRING; 9796.ENSECAP00000040937; -.
DR   PaxDb; 9796-ENSECAP00000040937; -.
DR   Ensembl; ENSECAT00000031343.2; ENSECAP00000040937.2; ENSECAG00000017449.4.
DR   VGNC; VGNC:21637; PNPLA7.
DR   GeneTree; ENSGT00940000156763; -.
DR   InParanoid; A0A3Q2I1N1; -.
DR   OMA; SSGYVWR; -.
DR   Proteomes; UP000002281; Chromosome 25.
DR   Bgee; ENSECAG00000017449; Expressed in gluteus medius and 21 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 3.
DR   CDD; cd07225; Pat_PNPLA6_PNPLA7; 1.
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; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        93..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          227..354
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          561..645
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          673..778
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          1010..1176
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          402..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1357..1404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1379..1404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1404 AA;  154652 MW;  E47F0AC5546681F1 CRC64;
     MPVLTLPDCG VFLQAGFCLG ATLRSWVLQL MEQPSQAAMV TTSCSWETGR SQVLRPVSPL
     AAPALLCPAC GQGWEGLHSG LANRCSVYDL AQLMGIAIGA LLALALVGVT VFFMYRKFSQ
     FGQVQPTPQY RFRKRDKVMF YGRKIMRKVT TLPNTLVGNT AAPRQRVRKR TKVLSLAKRI
     LRFKKEYPTL QPKEPPPSLL EADLTEFDVK NSHLPSEVLY MLKNVRVLGH FEKPLFLELC
     KHMVFVQLLE GEHVFRPGEP DTSIYVVQDG RLEVCIQDTD GTEVAVKEVL AGDSVHSLLS
     ILDVITGHTA PYKTVSARAA AASTVLRLPA AAFQGVFEKY PETLVRVVQI IMVRLQRVTF
     LALHNYLGLT TELFNPESQA IPLVSVASLA VGKTKRQVSC SPEERLEKSL RPQESCDPDH
     GGSRAAASGP LLKRSHSVPL PSVHKEISDE LGKAQAGDKA PSAPPGSVAG APSDLRMACD
     RARVVLQAEE RPASAVASKS KKSVVVAETP SAVFHYEDST SDETAASRKT DAIFRAAKKD
     LLTLMKLDDP SLLDGRVTLL HVPGGTVVSR QGDQDVNILF VVSGLLHVYQ RKIDSEEDTC
     LFVTRPGEMV GQLAVLTGEP LIFTIKANRD CSFLSISKAH FYEIMRKQPT VVLGVAHTLV
     KRMSSFVRQI DFALDWMEVE AGRAIYRQGD KSDCTYIVLS GRLRSVIRKD DGKKRLAGEY
     GRGDLIGVVE TLTHQARATT VHAVRDSELA KLPAGALTSI KRRYPQVVTR LIHLLGEKIL
     GSLQQGTATG HQFGLHAAGG KWDSGNPPSN LSTVAVMPVS EDVPLTTFAL ELKHALSAIG
     PVLLLTSDNI KQRLGSAALD SIHEYRLSSW LGQQEDIHRI VLYQADSTLT PWTQRCIRQA
     DCILIVGLGE QEPTVGELER MLESTAVRAQ KQLILLHREE GPAPSRTVEW LNMRSWCSGH
     LHLCCPRRVF SRRSMPKLVE MYERVFQRPP DRHSDFSRLA RVLTGNAIAL VLGGGGARGC
     AQVGIIRALV ECGIPVDMVG GTSIGAFMGA LYSEERSCSQ MRIRAKQWAE GMTSVVRTML
     DLTYPITSMF SGAGFNNSIC SVFKDRQIED LWIPYFTITT DITASAMRVH TDGSLWRYVR
     ASMSLSGYMP PLCDPKDGHL LMDGGYINNL PADVARSMGA KVVIAIDVGS QDEVDLTNYG
     DALSGWWLLW KRWNPLATKV KVLNMAEIQT RLAYVCCVRQ LEMVKSSDYC ECLRPPIDRY
     RTLDFGKFDE ICEVGYQHGR TVFDIWGRSG VLEKMLQDRQ GTSRMKACDA LTCPNASFTD
     LAEIVSRIEP AKVAAVDDES DYQTEYEEEL LEGPQDAYAD FQCAPADSGS DSEDEPSLQH
     QDPSLASAKL SRDSSSLCLS DQDG
//
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