ID   PLPL7_HUMAN             Reviewed;        1317 AA.
AC   Q6ZV29; B5MDD3; Q5T364; Q658X0; Q658Y3; Q6ZTS1; Q86YU8; Q8TAY5; Q96N75;
AC   Q9H7N5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 4.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein 7;
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:A2AJ88};
DE            EC=3.1.1.5 {ECO:0000250|UniProtKB:A2AJ88};
GN   Name=PNPLA7; Synonyms=C9orf111;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1016-1268 (ISOFORM 4), AND VARIANT ASN-1050.
RC   TISSUE=Liver, Spleen, Thalamus, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 688-1317 (ISOFORM 1), AND VARIANT
RP   LEU-908.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1317 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 897-1317 (ISOFORM 3).
RC   TISSUE=Lymph node, and Stomach;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Lysophospholipase which preferentially deacylates unsaturated
CC       lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Also
CC       can deacylate, to a lesser extent, lysophosphatidylethanolamine
CC       (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid
CC       (C16:0). {ECO:0000250|UniProtKB:A2AJ88}.
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:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC         (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC         Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
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:0000250|UniProtKB:A2AJ88};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC         Evidence={ECO:0000250|UniProtKB:A2AJ88};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:A2AJ88}; Single-pass type III membrane protein
CC       {ECO:0000250|UniProtKB:A2AJ88}. Lipid droplet
CC       {ECO:0000250|UniProtKB:A2AJ88}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6ZV29-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZV29-2; Sequence=VSP_026500, VSP_026501, VSP_026502;
CC       Name=3;
CC         IsoId=Q6ZV29-3; Sequence=VSP_026503;
CC       Name=4;
CC         IsoId=Q6ZV29-4; Sequence=VSP_026504, VSP_026505;
CC       Name=5;
CC         IsoId=Q6ZV29-5; Sequence=VSP_026500;
CC   -!- DOMAIN: The 3 cNMP binding domains are required for localization to the
CC       endoplasmic reticulum. The cNMP binding domain 3 is involved in the
CC       binding to lipid droplets. {ECO:0000250|UniProtKB:A2AJ88}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71033.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK024443; BAB15733.1; -; mRNA.
DR   EMBL; AK055880; BAB71033.1; ALT_INIT; mRNA.
DR   EMBL; AK122590; BAC56931.1; -; mRNA.
DR   EMBL; AK125060; BAC86036.1; -; mRNA.
DR   EMBL; AK126267; BAC86509.1; -; mRNA.
DR   EMBL; AL365502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025663; AAH25663.1; -; mRNA.
DR   EMBL; AL832944; CAH56322.1; -; mRNA.
DR   EMBL; AL832856; CAH56483.1; -; mRNA.
DR   CCDS; CCDS48070.1; -. [Q6ZV29-5]
DR   CCDS; CCDS7045.1; -. [Q6ZV29-1]
DR   RefSeq; NP_001092007.2; NM_001098537.2. [Q6ZV29-5]
DR   RefSeq; NP_689499.4; NM_152286.4. [Q6ZV29-1]
DR   AlphaFoldDB; Q6ZV29; -.
DR   SMR; Q6ZV29; -.
DR   BioGRID; 131999; 7.
DR   STRING; 9606.ENSP00000384610; -.
DR   iPTMnet; Q6ZV29; -.
DR   PhosphoSitePlus; Q6ZV29; -.
DR   BioMuta; PNPLA7; -.
DR   DMDM; 296452996; -.
DR   EPD; Q6ZV29; -.
DR   jPOST; Q6ZV29; -.
DR   MassIVE; Q6ZV29; -.
DR   MaxQB; Q6ZV29; -.
DR   PaxDb; 9606-ENSP00000384610; -.
DR   PeptideAtlas; Q6ZV29; -.
DR   ProteomicsDB; 68378; -. [Q6ZV29-1]
DR   ProteomicsDB; 68379; -. [Q6ZV29-2]
DR   ProteomicsDB; 68380; -. [Q6ZV29-3]
DR   ProteomicsDB; 68381; -. [Q6ZV29-4]
DR   ProteomicsDB; 68382; -. [Q6ZV29-5]
DR   Antibodypedia; 2428; 10 antibodies from 8 providers.
DR   DNASU; 375775; -.
DR   Ensembl; ENST00000277531.8; ENSP00000277531.4; ENSG00000130653.16. [Q6ZV29-1]
DR   Ensembl; ENST00000406427.6; ENSP00000384610.1; ENSG00000130653.16. [Q6ZV29-5]
DR   GeneID; 375775; -.
DR   KEGG; hsa:375775; -.
DR   MANE-Select; ENST00000406427.6; ENSP00000384610.1; NM_001098537.3; NP_001092007.2. [Q6ZV29-5]
DR   UCSC; uc004cnf.3; human. [Q6ZV29-1]
DR   AGR; HGNC:24768; -.
DR   CTD; 375775; -.
DR   DisGeNET; 375775; -.
DR   GeneCards; PNPLA7; -.
DR   HGNC; HGNC:24768; PNPLA7.
DR   HPA; ENSG00000130653; Low tissue specificity.
DR   MIM; 612122; gene.
DR   neXtProt; NX_Q6ZV29; -.
DR   OpenTargets; ENSG00000130653; -.
DR   PharmGKB; PA134935962; -.
DR   VEuPathDB; HostDB:ENSG00000130653; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   GeneTree; ENSGT00940000156763; -.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   InParanoid; Q6ZV29; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   PhylomeDB; Q6ZV29; -.
DR   TreeFam; TF300519; -.
DR   PathwayCommons; Q6ZV29; -.
DR   Reactome; R-HSA-6814848; Glycerophospholipid catabolism.
DR   BioGRID-ORCS; 375775; 35 hits in 1152 CRISPR screens.
DR   ChiTaRS; PNPLA7; human.
DR   GenomeRNAi; 375775; -.
DR   Pharos; Q6ZV29; Tdark.
DR   PRO; PR:Q6ZV29; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q6ZV29; Protein.
DR   Bgee; ENSG00000130653; Expressed in left ovary and 99 other cell types or tissues.
DR   ExpressionAtlas; Q6ZV29; baseline and differential.
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:UniProtKB-SubCell.
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.
DR   Genevisible; Q6ZV29; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Hydrolase; Lipid degradation;
KW   Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1317
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   7"
FT                   /id="PRO_0000293489"
FT   TOPO_DOM        1..12
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..1317
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          928..1094
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          320..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..945
FT                   /note="Involved in the binding to lipid droplets"
FT                   /evidence="ECO:0000250|UniProtKB:A2AJ88"
FT   REGION          1271..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           932..937
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           959..963
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1081..1083
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        320..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        961
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1081
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         145..272
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT   BINDING         458..563
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT   BINDING         591..696
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1258
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2AJ88"
FT   MOD_RES         1262
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5BK26"
FT   VAR_SEQ         10
FT                   /note="Q -> QADFCLGTALHSWGLWFTEEGSPSTM (in isoform 2 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026500"
FT   VAR_SEQ         384..433
FT                   /note="GGPGSATSDLGMACDRARVFLHSDEHPGSSVASKSRKSVMVAEIPSTVSQ
FT                   -> ARVLCLLPQCLGGLPPTDTSVYSSASSDCCGCSMPVLCIMGHKPHVTVDT (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026501"
FT   VAR_SEQ         434..1317
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026502"
FT   VAR_SEQ         1191..1255
FT                   /note="EVGYQHGRTVFDIWGRSGVLEKMLRDQQGPSKKPASAVLTCPNASFTDLAEI
FT                   VSRIEPAKPAMVD -> VP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_026503"
FT   VAR_SEQ         1256..1268
FT                   /note="DESDYQTEYEEEL -> GEWRRKTKPWRRA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026504"
FT   VAR_SEQ         1269..1317
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_026505"
FT   VARIANT         236
FT                   /note="R -> H (in dbSNP:rs12788)"
FT                   /id="VAR_061139"
FT   VARIANT         286
FT                   /note="G -> S (in dbSNP:rs2298171)"
FT                   /id="VAR_055696"
FT   VARIANT         323
FT                   /note="R -> Q (in dbSNP:rs11137410)"
FT                   /id="VAR_033060"
FT   VARIANT         364
FT                   /note="Q -> E (in dbSNP:rs3750378)"
FT                   /id="VAR_033061"
FT   VARIANT         368
FT                   /note="E -> D (in dbSNP:rs3750379)"
FT                   /id="VAR_033062"
FT   VARIANT         387
FT                   /note="G -> S (in dbSNP:rs11791683)"
FT                   /id="VAR_060409"
FT   VARIANT         803
FT                   /note="A -> V (in dbSNP:rs1891630)"
FT                   /id="VAR_033063"
FT   VARIANT         824
FT                   /note="V -> M (in dbSNP:rs34938599)"
FT                   /id="VAR_033064"
FT   VARIANT         908
FT                   /note="P -> L (in dbSNP:rs3812499)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_033065"
FT   VARIANT         993
FT                   /note="L -> M (in dbSNP:rs35177111)"
FT                   /id="VAR_033066"
FT   VARIANT         1050
FT                   /note="D -> N (in dbSNP:rs4962237)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_055697"
FT   CONFLICT        173
FT                   /note="F -> L (in Ref. 1; BAC86509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="K -> M (in Ref. 1; BAC86036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384..399
FT                   /note="Missing (in Ref. 1; BAC86509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403..473
FT                   /note="FLHSDEHPGSSVASKSRKSVMVAEIPSTVSQHSESHTDETLASRKSDAIFRA
FT                   AKKDLLTLMKLEDSSLLDG -> LCLLPQCLGGLPPTDTSVYSSASSDCCGCSMPVLCI
FT                   MGHKPHVTVDT (in Ref. 1; BAC86509)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        409
FT                   /note="H -> D (in Ref. 1; BAC86036)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        874
FT                   /note="W -> S (in Ref. 1; BAB71033)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        892..896
FT                   /note="SLPKL -> RLLPQ (in Ref. 1; BAC56931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1016..1027
FT                   /note="SIFSVFKDQQIE -> WERAHLSPVRPQ (in Ref. 1; BAB15733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1027
FT                   /note="E -> EQ (in Ref. 4; CAH56483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1055
FT                   /note="W -> R (in Ref. 1;
FT                   BAB15733/BAB71033/BAC56931/BAC86036, 3; AAH25663 and 4;
FT                   CAH56322/CAH56483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1140
FT                   /note="V -> VV (in Ref. 4; CAH56483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1317 AA;  145705 MW;  3C0DFC7DE916F349 CRC64;
     MEEEKDDSPQ LTGIAVGALL ALALVGVLIL FMFRRLRQFR QAQPTPQYRF RKRDKVMFYG
     RKIMRKVTTL PNTLVENTAL PRQRARKRTK VLSLAKRILR FKKEYPALQP KEPPPSLLEA
     DLTEFDVKNS HLPSEVLYML KNVRVLGHFE KPLFLELCKH IVFVQLQEGE HVFQPREPDP
     SICVVQDGRL EVCIQDTDGT EVVVKEVLAG DSVHSLLSIL DIITGHAAPY KTVSVRAAIP
     STILRLPAAA FHGVFEKYPE TLVRVVQIIM VRLQRVTFLA LHNYLGLTTE LFNAESQAIP
     LVSVASVAAG KAKKQVFYGE EERLKKPPRL QESCDSDHGG GRPAAAGPLL KRSHSVPAPS
     IRKQILEELE KPGAGDPDPS APQGGPGSAT SDLGMACDRA RVFLHSDEHP GSSVASKSRK
     SVMVAEIPST VSQHSESHTD ETLASRKSDA IFRAAKKDLL TLMKLEDSSL LDGRVALLHV
     PAGTVVSRQG DQDASILFVV SGLLHVYQRK IGSQEDTCLF LTRPGEMVGQ LAVLTGEPLI
     FTVKANRDCS FLSISKAHFY EIMRKQPTVV LGVAHTVVKR MSSFVRQIDF ALDWVEVEAG
     RAIYRQGDKS DCTYIMLSGR LRSVIRKDDG KKRLAGEYGR GDLVGVVETL THQARATTVH
     AVRDSELAKL PAGALTSIKR RYPQVVTRLI HLLGEKILGS LQQGPVTGHQ LGLPTEGSKW
     DLGNPAVNLS TVAVMPVSEE VPLTAFALEL EHALSAIGPT LLLTSDNIKR RLGSAALDSV
     HEYRLSSWLG QQEDTHRIVL YQADGTLTPW TQRCVRQADC ILIVGLGDQE PTVGELERML
     ESTAVRAQKQ LILLHREEGP APARTVEWLN MRSWCSGHLH LCCPRRVFSR RSLPKLVEMY
     KHVFQRPPDR HSDFSRLARV LTGNAIALVL GGGGARGCAQ VGVLKALAEC GIPVDMVGGT
     SIGAFVGALY SEERNYSQMR IRAKQWAEGM TSLMKAALDL TYPITSMFSG AGFNSSIFSV
     FKDQQIEDLW IPYFAITTDI TASAMRVHTD GSLWWYVRAS MSLSGYMPPL CDPKDGHLLM
     DGGYINNLPA DVARSMGAKV VIAIDVGSRD ETDLTNYGDA LSGWWLLWKR WNPLATKVKV
     LNMAEIQTRL AYVCCVRQLE VVKSSDYCEY LRPPIDSYST LDFGKFNEIC EVGYQHGRTV
     FDIWGRSGVL EKMLRDQQGP SKKPASAVLT CPNASFTDLA EIVSRIEPAK PAMVDDESDY
     QTEYEEELLD VPRDAYADFQ STSAQQGSDL EDESSLRHRH PSLAFPKLSE GSSDQDG
//