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PLPL6_HUMAN
ID   PLPL6_HUMAN             Reviewed;        1375 AA.
AC   Q8IY17; A6NGQ0; B4DFB9; B7Z7T2; F5H5K9; J3KQS3; O60859; Q86W58; Q9UG58;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 3.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein 6 {ECO:0000305};
DE            EC=3.1.1.5 {ECO:0000269|PubMed:15044461};
DE   AltName: Full=Neuropathy target esterase {ECO:0000303|PubMed:9576844};
GN   Name=PNPLA6 {ECO:0000312|HGNC:HGNC:16268}; Synonyms=NTE;
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 [MRNA] (ISOFORM 2), GLYCOSYLATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=9576844; DOI=10.1042/bj3320001;
RA   Lush M.J., Li Y., Read D.J., Willis A.C., Glynn P.;
RT   "Neuropathy target esterase and a homologous Drosophila neurodegeneration-
RT   associated mutant protein contain a novel domain conserved from bacteria to
RT   man.";
RL   Biochem. J. 332:1-4(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP   PRO-412.
RC   TISSUE=Cerebellum;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 43-1375 (ISOFORM 3), AND VARIANTS PRO-412 AND
RP   ARG-1033.
RC   TISSUE=Brain, Duodenum, and Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 994-1375 (ISOFORMS 2/3/4/5).
RC   TISSUE=Brain;
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   [7]
RP   REVIEW ON ACTIVITY REGULATION.
RX   PubMed=1666291; DOI=10.3109/10408449209089884;
RA   Lotti M.;
RT   "The pathogenesis of organophosphate polyneuropathy.";
RL   Crit. Rev. Toxicol. 21:465-487(1991).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11927584; DOI=10.1074/jbc.m200330200;
RA   van Tienhoven M., Atkins J., Li Y., Glynn P.;
RT   "Human neuropathy target esterase catalyzes hydrolysis of membrane
RT   lipids.";
RL   J. Biol. Chem. 277:20942-20948(2002).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15044461; DOI=10.1074/jbc.m400830200;
RA   Zaccheo O., Dinsdale D., Meacock P.A., Glynn P.;
RT   "Neuropathy target esterase and its yeast homologue degrade
RT   phosphatidylcholine to glycerophosphocholine in living cells.";
RL   J. Biol. Chem. 279:24024-24033(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354; THR-361 AND SER-362, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354; SER-362; SER-372 AND
RP   SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   INVOLVEMENT IN BNHS, AND VARIANTS BNHS CYS-1147; CYS-1175 AND TRP-1359.
RX   PubMed=25033069; DOI=10.1210/jc.2014-1836;
RA   Topaloglu A.K., Lomniczi A., Kretzschmar D., Dissen G.A., Kotan L.D.,
RA   McArdle C.A., Koc A.F., Hamel B.C., Guclu M., Papatya E.D., Eren E.,
RA   Mengen E., Gurbuz F., Cook M., Castellano J.M., Kekil M.B., Mungan N.O.,
RA   Yuksel B., Ojeda S.R.;
RT   "Loss-of-function mutations in PNPLA6 encoding neuropathy target esterase
RT   underlie pubertal failure and neurological deficits in Gordon Holmes
RT   syndrome.";
RL   J. Clin. Endocrinol. Metab. 99:E2067-E2075(2014).
RN   [16]
RP   INVOLVEMENT IN SPG39, AND VARIANTS SPG39 HIS-938 AND VAL-1060.
RX   PubMed=18313024; DOI=10.1016/j.ajhg.2007.12.018;
RA   Rainier S., Bui M., Mark E., Thomas D., Tokarz D., Ming L., Delaney C.,
RA   Richardson R.J., Albers J.W., Matsunami N., Stevens J., Coon H.,
RA   Leppert M., Fink J.K.;
RT   "Neuropathy target esterase gene mutations cause motor neuron disease.";
RL   Am. J. Hum. Genet. 82:780-785(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND THR-464, AND
RP   IDENTIFICATION BY 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).
RN   [18]
RP   TISSUE SPECIFICITY, INVOLVEMENT IN LNMS, INVOLVEMENT IN OMCS, VARIANT LNMS
RP   ARG-726, AND VARIANTS OMCS GLN-1099; ARG-1129; SER-1176 AND ALA-1215.
RX   PubMed=25480986; DOI=10.1136/jmedgenet-2014-102856;
RA   Hufnagel R.B., Arno G., Hein N.D., Hersheson J., Prasad M., Anderson Y.,
RA   Krueger L.A., Gregory L.C., Stoetzel C., Jaworek T.J., Hull S., Li A.,
RA   Plagnol V., Willen C.M., Morgan T.M., Prows C.A., Hegde R.S., Riazuddin S.,
RA   Grabowski G.A., Richardson R.J., Dieterich K., Huang T., Revesz T.,
RA   Martinez-Barbera J.P., Sisk R.A., Jefferies C., Houlden H., Dattani M.T.,
RA   Fink J.K., Dollfus H., Moore A.T., Ahmed Z.M.;
RT   "Neuropathy target esterase impairments cause Oliver-McFarlane and
RT   Laurence-Moon syndromes.";
RL   J. Med. Genet. 52:85-94(2015).
RN   [19]
RP   VARIANTS SPG39 ILE-263 AND GLU-840, VARIANTS BNHS TRP-578; LEU-1045;
RP   ILE-1058; SER-1066; MET-1110 AND LEU-1122, AND VARIANTS GLY-1100 AND
RP   GLY-1362.
RX   PubMed=24355708; DOI=10.1093/brain/awt326;
RA   Synofzik M., Gonzalez M.A., Lourenco C.M., Coutelier M., Haack T.B.,
RA   Rebelo A., Hannequin D., Strom T.M., Prokisch H., Kernstock C., Durr A.,
RA   Schols L., Lima-Martinez M.M., Farooq A., Schule R., Stevanin G.,
RA   Marques W. Jr., Zuchner S.;
RT   "PNPLA6 mutations cause Boucher-Neuhauser and Gordon Holmes syndromes as
RT   part of a broad neurodegenerative spectrum.";
RL   Brain 137:69-77(2014).
CC   -!- FUNCTION: Phospholipase B that deacylates intracellular
CC       phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC       (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of
CC       PtdCho. Catalyzes the hydrolysis of several naturally occurring
CC       membrane-associated lipids (PubMed:11927584). Hydrolyzes
CC       lysophospholipids and monoacylglycerols, preferring the 1-acyl to the
CC       2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols
CC       or fatty acid amides (PubMed:11927584). {ECO:0000269|PubMed:11927584,
CC       ECO:0000269|PubMed:15044461}.
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:0000269|PubMed:15044461};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000269|PubMed:15044461};
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:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40808;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC         hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC         glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC         Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC         Evidence={ECO:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC         Evidence={ECO:0000305|PubMed:11927584};
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:Q3TRM4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093;
CC         Evidence={ECO:0000250|UniProtKB:Q3TRM4};
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:0000269|PubMed:11927584};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000305|PubMed:11927584};
CC   -!- ACTIVITY REGULATION: Inhibited by a series a OPs such as mipafox (MPX),
CC       phenyl saligenin phosphate (PSP), phenyl dipentyl phosphinate (PDPP),
CC       diisopropyl fluorophosphate and paraoxon. {ECO:0000269|PubMed:15044461,
CC       ECO:0000305|PubMed:1666291}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.05 mM for 1-palmitoyl-lysophosphatidylcholine
CC         {ECO:0000269|PubMed:11927584};
CC         KM=0.4 mM for 1-palmitoylglycerol {ECO:0000269|PubMed:11927584};
CC         Vmax=20 umol/min/mg enzyme towards 1-palmitoyl-
CC         lysophosphatidylcholine {ECO:0000269|PubMed:11927584};
CC         Vmax=1 umol/min/mg enzyme towards 1-palmitoylglycerol
CC         {ECO:0000269|PubMed:11927584};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15044461}; Single-pass type III membrane protein
CC       {ECO:0000269|PubMed:15044461}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=4;
CC         IsoId=Q8IY17-4; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IY17-2; Sequence=VSP_059668;
CC       Name=3;
CC         IsoId=Q8IY17-3; Sequence=VSP_059670;
CC       Name=5;
CC         IsoId=Q8IY17-5; Sequence=VSP_059668, VSP_059669, VSP_059670;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, placenta, kidney, neuron and
CC       skeletal muscle. Expressed in the developing eye, pituitary and brain.
CC       {ECO:0000269|PubMed:25480986, ECO:0000269|PubMed:9576844}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:9576844}.
CC   -!- DISEASE: Spastic paraplegia 39, autosomal recessive (SPG39)
CC       [MIM:612020]: A form of spastic paraplegia, a neurodegenerative
CC       disorder characterized by a slow, gradual, progressive weakness and
CC       spasticity of the lower limbs. Rate of progression and the severity of
CC       symptoms are quite variable. Initial symptoms may include difficulty
CC       with balance, weakness and stiffness in the legs, muscle spasms, and
CC       dragging the toes when walking. In some forms of the disorder, bladder
CC       symptoms (such as incontinence) may appear, or the weakness and
CC       stiffness may spread to other parts of the body. SPG39 is associated
CC       with a motor axonopathy affecting upper and lower limbs and resulting
CC       in progressive wasting of distal upper and lower extremity muscles.
CC       {ECO:0000269|PubMed:18313024, ECO:0000269|PubMed:24355708}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Boucher-Neuhauser syndrome (BNHS) [MIM:215470]: An autosomal
CC       recessive disorder characterized by spinocerebellar ataxia,
CC       hypogonadotropic hypogonadism, and visual impairment due to
CC       chorioretinal dystrophy. The age at onset is variable, but most
CC       patients develop 1 or more symptoms in the first decade of life.
CC       Chorioretinal dystrophy may not always be present.
CC       {ECO:0000269|PubMed:24355708, ECO:0000269|PubMed:25033069}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Laurence-Moon syndrome (LNMS) [MIM:245800]: An autosomal
CC       recessive syndrome characterized by progressive spinocerebellar
CC       degeneration, spastic paraplegia, intellectual disability,
CC       hypogonadism, dwarfism, and chorioretinopathy. Trichomegaly is absent.
CC       {ECO:0000269|PubMed:25480986}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Oliver-McFarlane syndrome (OMCS) [MIM:275400]: A rare
CC       autosomal recessive, congenital syndrome characterized by trichomegaly,
CC       severe chorioretinal atrophy and multiple pituitary hormone
CC       deficiencies. It results in intellectual impairment and dwarfism, if
CC       untreated. Clinical features include hypogonadotropic hypogonadism
CC       during puberty, pigmentary retinal degeneration, ataxia, spastic
CC       paraplegia, and peripheral neuropathy. {ECO:0000269|PubMed:25480986}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- MISCELLANEOUS: Its specific chemical modification by certain
CC       organophosphorus (OP) compounds leads to distal axonopathy.
CC       {ECO:0000303|PubMed:1666291}.
CC   -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
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DR   EMBL; AJ004832; CAA06164.1; -; mRNA.
DR   EMBL; AK294021; BAG57380.1; -; mRNA.
DR   EMBL; AK302462; BAH13718.1; -; mRNA.
DR   EMBL; AC008878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC009003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471139; EAW69029.1; -; Genomic_DNA.
DR   EMBL; BC038229; AAH38229.1; -; mRNA.
DR   EMBL; BC050553; AAH50553.1; -; mRNA.
DR   EMBL; BC051768; AAH51768.1; -; mRNA.
DR   EMBL; AL050362; CAB43674.1; -; mRNA.
DR   CCDS; CCDS32891.1; -. [Q8IY17-2]
DR   CCDS; CCDS54206.1; -. [Q8IY17-4]
DR   CCDS; CCDS54207.1; -. [Q8IY17-5]
DR   RefSeq; NP_001159583.1; NM_001166111.1. [Q8IY17-4]
DR   RefSeq; NP_001159584.1; NM_001166112.1. [Q8IY17-5]
DR   RefSeq; NP_001159585.1; NM_001166113.1. [Q8IY17-2]
DR   RefSeq; NP_001159586.1; NM_001166114.1.
DR   RefSeq; NP_006693.3; NM_006702.4. [Q8IY17-2]
DR   AlphaFoldDB; Q8IY17; -.
DR   SMR; Q8IY17; -.
DR   BioGRID; 116114; 98.
DR   IntAct; Q8IY17; 40.
DR   MINT; Q8IY17; -.
DR   STRING; 9606.ENSP00000407509; -.
DR   ChEMBL; CHEMBL2189129; -.
DR   SwissLipids; SLP:000000615; -.
DR   GlyGen; Q8IY17; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IY17; -.
DR   PhosphoSitePlus; Q8IY17; -.
DR   BioMuta; PNPLA6; -.
DR   DMDM; 150403921; -.
DR   EPD; Q8IY17; -.
DR   jPOST; Q8IY17; -.
DR   MassIVE; Q8IY17; -.
DR   MaxQB; Q8IY17; -.
DR   PaxDb; Q8IY17; -.
DR   PeptideAtlas; Q8IY17; -.
DR   PRIDE; Q8IY17; -.
DR   ProteomicsDB; 26908; -.
DR   ProteomicsDB; 71085; -. [Q8IY17-2]
DR   ProteomicsDB; 71086; -. [Q8IY17-3]
DR   Antibodypedia; 2222; 247 antibodies from 30 providers.
DR   DNASU; 10908; -.
DR   Ensembl; ENST00000221249.10; ENSP00000221249.5; ENSG00000032444.17. [Q8IY17-2]
DR   Ensembl; ENST00000414982.7; ENSP00000407509.2; ENSG00000032444.17. [Q8IY17-4]
DR   Ensembl; ENST00000450331.7; ENSP00000394348.2; ENSG00000032444.17. [Q8IY17-2]
DR   Ensembl; ENST00000545201.6; ENSP00000443323.1; ENSG00000032444.17. [Q8IY17-5]
DR   GeneID; 10908; -.
DR   KEGG; hsa:10908; -.
DR   UCSC; uc002mgq.3; human. [Q8IY17-4]
DR   CTD; 10908; -.
DR   DisGeNET; 10908; -.
DR   GeneCards; PNPLA6; -.
DR   GeneReviews; PNPLA6; -.
DR   HGNC; HGNC:16268; PNPLA6.
DR   HPA; ENSG00000032444; Low tissue specificity.
DR   MalaCards; PNPLA6; -.
DR   MIM; 215470; phenotype.
DR   MIM; 245800; phenotype.
DR   MIM; 275400; phenotype.
DR   MIM; 603197; gene.
DR   MIM; 612020; phenotype.
DR   neXtProt; NX_Q8IY17; -.
DR   OpenTargets; ENSG00000032444; -.
DR   Orphanet; 1180; Ataxia-hypogonadism-choroidal dystrophy syndrome.
DR   Orphanet; 139480; Autosomal recessive spastic paraplegia type 39.
DR   Orphanet; 1173; Cerebellar ataxia-hypogonadism syndrome.
DR   Orphanet; 2377; Laurence-Moon syndrome.
DR   Orphanet; 3363; Trichomegaly-retina pigmentary degeneration-dwarfism syndrome.
DR   PharmGKB; PA145148268; -.
DR   VEuPathDB; HostDB:ENSG00000032444; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   GeneTree; ENSGT00940000159130; -.
DR   HOGENOM; CLU_000960_1_0_1; -.
DR   InParanoid; Q8IY17; -.
DR   OMA; FMYFKRL; -.
DR   OrthoDB; 253518at2759; -.
DR   PhylomeDB; Q8IY17; -.
DR   TreeFam; TF300519; -.
DR   PathwayCommons; Q8IY17; -.
DR   Reactome; R-HSA-6814848; Glycerophospholipid catabolism.
DR   SignaLink; Q8IY17; -.
DR   SIGNOR; Q8IY17; -.
DR   BioGRID-ORCS; 10908; 19 hits in 1078 CRISPR screens.
DR   ChiTaRS; PNPLA6; human.
DR   GeneWiki; Neuropathy_target_esterase; -.
DR   GenomeRNAi; 10908; -.
DR   Pharos; Q8IY17; Tbio.
DR   PRO; PR:Q8IY17; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q8IY17; protein.
DR   Bgee; ENSG00000032444; Expressed in granulocyte and 186 other tissues.
DR   ExpressionAtlas; Q8IY17; baseline and differential.
DR   Genevisible; Q8IY17; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; EXP:Reactome.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0046475; P:glycerophospholipid catabolic process; TAS:Reactome.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 3.
DR   Gene3D; 2.60.120.10; -; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 3.
DR   SUPFAM; SSF51206; SSF51206; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 3.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Dwarfism; Endoplasmic reticulum;
KW   Glycoprotein; Hereditary spastic paraplegia; Hydrolase;
KW   Hypogonadotropic hypogonadism; Intellectual disability; Lipid degradation;
KW   Lipid metabolism; Membrane; Neurodegeneration; Phosphoprotein;
KW   Reference proteome; Repeat; Retinitis pigmentosa; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1375
FT                   /note="Patatin-like phospholipase domain-containing protein
FT                   6"
FT                   /id="PRO_0000292199"
FT   TOPO_DOM        1..59
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..1375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          981..1147
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1306..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           985..990
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1012..1016
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1134..1136
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        365..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..400
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1014
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         195..322
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         511..633
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
FT   BINDING         629..749
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="3"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         361
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         464
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         10..57
FT                   /note="Missing (in isoform 2 and isoform 5)"
FT                   /id="VSP_059668"
FT   VAR_SEQ         521..546
FT                   /note="Missing (in isoform 5)"
FT                   /id="VSP_059669"
FT   VAR_SEQ         763
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /id="VSP_059670"
FT   VARIANT         263
FT                   /note="V -> I (in SPG39; dbSNP:rs587777184)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071091"
FT   VARIANT         412
FT                   /note="A -> P (in dbSNP:rs17854645)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032949"
FT   VARIANT         578
FT                   /note="G -> W (in BNHS; dbSNP:rs587777615)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071092"
FT   VARIANT         726
FT                   /note="G -> R (in LNMS)"
FT                   /evidence="ECO:0000269|PubMed:25480986"
FT                   /id="VAR_073409"
FT   VARIANT         840
FT                   /note="G -> E (in SPG39; dbSNP:rs587777185)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071093"
FT   VARIANT         938
FT                   /note="R -> H (in SPG39; dbSNP:rs121434416)"
FT                   /evidence="ECO:0000269|PubMed:18313024"
FT                   /id="VAR_044409"
FT   VARIANT         1033
FT                   /note="K -> R (in dbSNP:rs17854647)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_032950"
FT   VARIANT         1045
FT                   /note="S -> L (in BNHS; dbSNP:rs541098659)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071094"
FT   VARIANT         1058
FT                   /note="T -> I (in BNHS; dbSNP:rs587777181)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071095"
FT   VARIANT         1060
FT                   /note="M -> V (in SPG39; dbSNP:rs121434415)"
FT                   /evidence="ECO:0000269|PubMed:18313024"
FT                   /id="VAR_044410"
FT   VARIANT         1066
FT                   /note="F -> S (in BNHS; dbSNP:rs587777183)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071096"
FT   VARIANT         1099
FT                   /note="R -> Q (in OMCS; dbSNP:rs786201037)"
FT                   /evidence="ECO:0000269|PubMed:25480986"
FT                   /id="VAR_073410"
FT   VARIANT         1100
FT                   /note="V -> G (found in a patient with sporadic ataxia and
FT                   BNHS; unknown pathological significance;
FT                   dbSNP:rs754429587)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071097"
FT   VARIANT         1110
FT                   /note="V -> M (in BNHS; dbSNP:rs587777182)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071098"
FT   VARIANT         1122
FT                   /note="P -> L (in BNHS; dbSNP:rs748506175)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071099"
FT   VARIANT         1129
FT                   /note="G -> R (in OMCS; dbSNP:rs773955314)"
FT                   /evidence="ECO:0000269|PubMed:25480986"
FT                   /id="VAR_073411"
FT   VARIANT         1147
FT                   /note="R -> C (in BNHS; dbSNP:rs587777854)"
FT                   /evidence="ECO:0000269|PubMed:25033069"
FT                   /id="VAR_073412"
FT   VARIANT         1175
FT                   /note="S -> C (in BNHS; dbSNP:rs1555751592)"
FT                   /evidence="ECO:0000269|PubMed:25033069"
FT                   /id="VAR_073413"
FT   VARIANT         1176
FT                   /note="G -> S (in OMCS; dbSNP:rs142422525)"
FT                   /evidence="ECO:0000269|PubMed:25480986"
FT                   /id="VAR_073414"
FT   VARIANT         1215
FT                   /note="V -> A (in OMCS; dbSNP:rs1211079280)"
FT                   /evidence="ECO:0000269|PubMed:25480986"
FT                   /id="VAR_073415"
FT   VARIANT         1359
FT                   /note="R -> W (in BNHS; dbSNP:rs374434303)"
FT                   /evidence="ECO:0000269|PubMed:25033069"
FT                   /id="VAR_073416"
FT   VARIANT         1362
FT                   /note="R -> G (found in a patient with Gordon-Holmes
FT                   syndrome; unknown pathological significance;
FT                   dbSNP:rs1204274988)"
FT                   /evidence="ECO:0000269|PubMed:24355708"
FT                   /id="VAR_071100"
FT   CONFLICT        43..46
FT                   /note="AGRI -> TRPV (in Ref. 5; AAH38229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        648
FT                   /note="T -> A (in Ref. 2; BAG57380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        714
FT                   /note="A -> T (in Ref. 5; AAH38229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        994
FT                   /note="I -> W (in Ref. 6; CAB43674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1178
FT                   /note="W -> V (in Ref. 6; CAB43674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1296
FT                   /note="E -> G (in Ref. 6; CAB43674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1302
FT                   /note="E -> K (in Ref. 2; BAH13718)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1375 AA;  150954 MW;  1C9F2797FB6D8612 CRC64;
     MEAPLQTGMM GTSSHGLATN SSGAKVAERD GFQDVLAPGE GSAGRICGAQ PVPFVPQVLG
     VMIGAGVAVV VTAVLILLVV RRLRVPKTPA PDGPRYRFRK RDKVLFYGRK IMRKVSQSTS
     SLVDTSVSAT SRPRMRKKLK MLNIAKKILR IQKETPTLQR KEPPPAVLEA DLTEGDLANS
     HLPSEVLYML KNVRVLGHFE KPLFLELCRH MVFQRLGQGD YVFRPGQPDA SIYVVQDGLL
     ELCLPGPDGK ECVVKEVVPG DSVNSLLSIL DVITGHQHPQ RTVSARAARD STVLRLPVEA
     FSAVFTKYPE SLVRVVQIIM VRLQRVTFLA LHNYLGLTNE LFSHEIQPLR LFPSPGLPTR
     TSPVRGSKRM VSTSATDEPR ETPGRPPDPT GAPLPGPTGD PVKPTSLETP SAPLLSRCVS
     MPGDISGLQG GPRSDFDMAY ERGRISVSLQ EEASGGSLAA PARTPTQEPR EQPAGACEYS
     YCEDESATGG CPFGPYQGRQ TSSIFEAAKQ ELAKLMRIED PSLLNSRVLL HHAKAGTIIA
     RQGDQDVSLH FVLWGCLHVY QRMIDKAEDV CLFVAQPGEL VGQLAVLTGE PLIFTLRAQR
     DCTFLRISKS DFYEIMRAQP SVVLSAAHTV AARMSPFVRQ MDFAIDWTAV EAGRALYRQG
     DRSDCTYIVL NGRLRSVIQR GSGKKELVGE YGRGDLIGVV EALTRQPRAT TVHAVRDTEL
     AKLPEGTLGH IKRRYPQVVT RLIHLLSQKI LGNLQQLQGP FPAGSGLGVP PHSELTNPAS
     NLATVAILPV CAEVPMVAFT LELQHALQAI GPTLLLNSDI IRARLGASAL DSIQEFRLSG
     WLAQQEDAHR IVLYQTDASL TPWTVRCLRQ ADCILIVGLG DQEPTLGQLE QMLENTAVRA
     LKQLVLLHRE EGAGPTRTVE WLNMRSWCSG HLHLRCPRRL FSRRSPAKLH ELYEKVFSRR
     ADRHSDFSRL ARVLTGNTIA LVLGGGGARG CSHIGVLKAL EEAGVPVDLV GGTSIGSFIG
     ALYAEERSAS RTKQRAREWA KSMTSVLEPV LDLTYPVTSM FTGSAFNRSI HRVFQDKQIE
     DLWLPYFNVT TDITASAMRV HKDGSLWRYV RASMTLSGYL PPLCDPKDGH LLMDGGYINN
     LPADIARSMG AKTVIAIDVG SQDETDLSTY GDSLSGWWLL WKRLNPWADK VKVPDMAEIQ
     SRLAYVSCVR QLEVVKSSSY CEYLRPPIDC FKTMDFGKFD QIYDVGYQYG KAVFGGWSRG
     NVIEKMLTDR RSTDLNESRR ADVLAFPSSG FTDLAEIVSR IEPPTSYVSD GCADGEESDC
     LTEYEEDAGP DCSRDEGGSP EGASPSTASE MEEEKSILRQ RRCLPQEPPG SATDA
 
 
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