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Database: UniProt
Entry: F6QBQ3_HORSE
LinkDB: F6QBQ3_HORSE
Original site: F6QBQ3_HORSE 
ID   F6QBQ3_HORSE            Unreviewed;      1285 AA.
AC   F6QBQ3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Patatin like phospholipase domain containing 7 {ECO:0000313|Ensembl:ENSECAP00000015750.3};
GN   Name=PNPLA7 {ECO:0000313|Ensembl:ENSECAP00000015750.3,
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:ENSECAP00000015750.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000015750.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015750.3,
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:ENSECAP00000015750.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015750.3};
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   Ensembl; ENSECAT00000019256.3; ENSECAP00000015750.3; ENSECAG00000017449.4.
DR   VGNC; VGNC:21637; PNPLA7.
DR   GeneTree; ENSGT00940000156763; -.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   TreeFam; TF300519; -.
DR   Proteomes; UP000002281; Chromosome 25.
DR   Bgee; ENSECAG00000017449; Expressed in gluteus medius and 21 other cell types or tissues.
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; 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        33..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          169..296
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          503..587
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          615..720
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          891..1057
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REGION          342..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  141462 MW;  8573EC3DB0B0D05D CRC64;
     MEQEDTSPEA GFCLGATLRS WVLQLMEQPS QAAMLMGIAI GALLALALVG VTVFFMYRKF
     SQFGQVQPTP QYRFRKRDKV MFYGRKIMRK VTTLPNTLVG NTAAPRQRVR KRTKVLSLAK
     RILRFKKEYP TLQPKEPPPS LLEADLTEFD VKNSHLPSEV LYMLKNVRVL GHFEKPLFLE
     LCKHMVFVQL LEGEHVFRPG EPDTSIYVVQ DGRLEVCIQD TDGTEVAVKE VLAGDSVHSL
     LSILDVITGH TAPYKTVSAR AAAASTVLRL PAAAFQGVFE KYPETLVRVV QIIMVRLQRV
     TFLALHNYLG LTTELFNPES QAIPLVSVAS LAVGKTKRQV SCSPEERLEK SLRPQESCDP
     DHGGSRAAAS GPLLKRSHSV PLPSVHKEIS DELGKAQAGD KAPSAPPGSV AGAPSDLRMA
     CDRARVVLQA EERPASAVAS KSKKSVVVAE TPSAVFHYED STSDETAASR KTDAIFRAAK
     KDLLTLMKLD DPSLLDGRVT LLHVPGGTVV SRQGDQDVNI LFVVSGLLHV YQRKIDSEED
     TCLFVTRPGE MVGQLAVLTG EPLIFTIKAN RDCSFLSISK AHFYEIMRKQ PTVVLGVAHT
     LVKRMSSFVR QIDFALDWME VEAGRAIYRQ GDKSDCTYIV LSGRLRSVIR KDDGKKRLAG
     EYGRGDLIGV VETLTHQARA TTVHAVRDSE LAKLPAGALT SIKRRYPQVV TRLIHLLGEK
     ILGSLQQGTA TGHQFGLHAA GGKWDSGNPP SNLSTVAVMP VSEDVPLTTF ALELKHALSA
     IGPVLLLTSD NIKQRLGSAA LDSIHEYRLS SWLGQQEDIH RIVLYQADST LTPWTQRCIR
     QADCILIVGL GEQEPTVGEV EMYERVFQRP PDRHSDFSRL ARVLTGNAIA LVLGGGGARG
     CAQVGIIRAL VECGIPVDMV GGTSIGAFMG ALYSEERSCS QMRIRAKQWA EGMTSVVRTM
     LDLTYPITSM FSGAGFNNSI CSVFKDRQIE DLWIPYFTIT TDITASAMRV HTDGSLWRYV
     RASMSLSGYM PPLCDPKDGH LLMDGGYINN LPADVARSMG AKVVIAIDVG SQDEVDLTNY
     GDALSGWWLL WKRWNPLATK VKVLNMAEIQ TRLAYVCCVR QLEMVKSSDY CECLRPPIDR
     YRTLDFGKFD EICEVGYQHG RTVFDIWGRS GVLEKMLQDR QGTSRMKACD ALTCPNASFT
     DLAEIVSRIE PAKVAAVDDE SDYQTEYEEE LLEGPQDAYA DFQCAPADSG SDSEDEPSLQ
     HQDPSLASAK LSRDSSSLCL SDQDG
//
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