ENPP2_HUMAN
ID ENPP2_HUMAN Reviewed; 863 AA.
AC Q13822; A8UHA1; E9PHP7; Q13827; Q14555; Q15117; Q9UCQ8; Q9UCR0; Q9UCR1;
AC Q9UCR2; Q9UCR3; Q9UCR4;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 2;
DE Short=E-NPP 2;
DE EC=3.1.4.39 {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:26371182};
DE AltName: Full=Autotaxin {ECO:0000303|PubMed:12176993, ECO:0000303|PubMed:7982964};
DE AltName: Full=Extracellular lysophospholipase D;
DE Short=LysoPLD {ECO:0000303|PubMed:12176993};
DE Flags: Precursor;
GN Name=ENPP2;
GN Synonyms=ATX {ECO:0000303|PubMed:18175805, ECO:0000303|PubMed:26371182},
GN PDNP2 {ECO:0000303|PubMed:8586446};
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), PARTIAL PROTEIN SEQUENCE,
RP CHARACTERIZATION, AND VARIANT PRO-493.
RC TISSUE=Melanoma;
RX PubMed=7982964; DOI=10.1016/s0021-9258(18)43838-0;
RA Murata J., Lee H.Y., Clair T., Krutzsch H.C., Arestad A.A., Sobel M.E.,
RA Liotta L.A., Stracke M.L.;
RT "cDNA cloning of the human tumor motility-stimulating protein, autotaxin,
RT reveals a homology with phosphodiesterases.";
RL J. Biol. Chem. 269:30479-30484(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-45, TISSUE SPECIFICITY, AND VARIANT PRO-493.
RX PubMed=8586446; DOI=10.1006/geno.1995.0036;
RA Kawagoe H., Soma O., Goji J., Nishimura N., Narita M., Inazawa J.,
RA Nakamura H., Sano K.;
RT "Molecular cloning and chromosomal assignment of the human brain-type
RT phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2).";
RL Genomics 30:380-384(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP PRO-493.
RC TISSUE=Teratocarcinoma;
RX PubMed=8579579; DOI=10.1006/bbrc.1996.0127;
RA Lee H.Y., Murata J., Clair T., Polymeropoulos M.H., Torres R., Manrow R.E.,
RA Liotta L.A., Stracke M.L.;
RT "Cloning, chromosomal localization, and tissue expression of autotaxin from
RT human teratocarcinoma cells.";
RL Biochem. Biophys. Res. Commun. 218:714-719(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, ACTIVITY REGULATION, AND VARIANT PRO-493.
RX PubMed=15769751; DOI=10.1074/jbc.m413183200;
RA van Meeteren L.A., Ruurs P., Christodoulou E., Goding J.W., Takakusa H.,
RA Kikuchi K., Perrakis A., Nagano T., Moolenaar W.H.;
RT "Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-
RT phosphate.";
RL J. Biol. Chem. 280:21155-21161(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 36-42
RP AND 49-54, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND VARIANT PRO-493.
RC TISSUE=Brain, and Melanoma;
RX PubMed=18175805; DOI=10.1074/jbc.m708705200;
RA Giganti A., Rodriguez M., Fould B., Moulharat N., Coge F., Chomarat P.,
RA Galizzi J.-P., Valet P., Saulnier-Blache J.-S., Boutin J.A., Ferry G.;
RT "Murine and human autotaxin alpha, beta, and gamma isoforms: gene
RT organization, tissue distribution, and biochemical characterization.";
RL J. Biol. Chem. 283:7776-7789(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-493.
RC TISSUE=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 [8]
RP PROTEIN SEQUENCE OF 36-49; 318-330; 335-344; 440-450 AND 854-863, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12176993; DOI=10.1074/jbc.m205623200;
RA Tokumura A., Majima E., Kariya Y., Tominaga K., Kogure K., Yasuda K.,
RA Fukuzawa K.;
RT "Identification of human plasma lysophospholipase D, a lysophosphatidic
RT acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase.";
RL J. Biol. Chem. 277:39436-39442(2002).
RN [9]
RP PROTEIN SEQUENCE OF 256-266; 370-392; 457-463; 481-496; 501-510; 545-554;
RP 639-643; 706-710 AND 829-840, FUNCTION, SUBCELLULAR LOCATION, AND VARIANT
RP PRO-493.
RC TISSUE=Melanoma;
RX PubMed=1733949; DOI=10.1016/s0021-9258(18)45911-x;
RA Stracke M.L., Krutzsch H.C., Unsworth E.J., Aarestad A., Cioce V.,
RA Schiffmann E., Liotta L.A.;
RT "Identification, purification, and partial sequence analysis of autotaxin,
RT a novel motility-stimulating protein.";
RL J. Biol. Chem. 267:2524-2529(1992).
RN [10]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=11559573;
RA Nam S.W., Clair T., Kim Y.S., McMarlin A., Schiffmann E., Liotta L.A.,
RA Stracke M.L.;
RT "Autotaxin (NPP-2), a metastasis-enhancing mitogen, is an angiogenic
RT factor.";
RL Cancer Res. 61:6938-6944(2001).
RN [11]
RP FUNCTION.
RX PubMed=12354767; DOI=10.1074/jbc.m206812200;
RA Aoki J., Taira A., Takanezawa Y., Kishi Y., Hama K., Kishimoto T.,
RA Mizuno K., Saku K., Taguchi R., Arai H.;
RT "Serum lysophosphatidic acid is produced through diverse phospholipase
RT pathways.";
RL J. Biol. Chem. 277:48737-48744(2002).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF THR-210; HIS-316 AND HIS-360.
RX PubMed=14500380;
RA Clair T., Aoki J., Koh E., Bandle R.W., Nam S.W., Ptaszynska M.M.,
RA Mills G.B., Schiffmann E., Liotta L.A., Stracke M.L.;
RT "Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator
RT of migration, sphingosine-1-phosphate.";
RL Cancer Res. 63:5446-5453(2003).
RN [13]
RP INDUCTION, AND POSSIBLE FUNCTION IN OBESITY.
RX PubMed=15700135; DOI=10.1007/s00125-004-1660-8;
RA Boucher J., Quilliot D., Pradere J.P., Simon M.F., Gres S., Guigne C.,
RA Prevot D., Ferry G., Boutin J.A., Carpene C., Valet P.,
RA Saulnier-Blache J.S.;
RT "Potential involvement of adipocyte insulin resistance in obesity-
RT associated up-regulation of adipocyte lysophospholipase D/autotaxin
RT expression.";
RL Diabetologia 48:569-577(2005).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21393252; DOI=10.1194/jlr.m013326;
RA Bolen A.L., Naren A.P., Yarlagadda S., Beranova-Giorgianni S., Chen L.,
RA Norman D., Baker D.L., Rowland M.M., Best M.D., Sano T., Tsukahara T.,
RA Liliom K., Igarashi Y., Tigyi G.;
RT "The phospholipase A1 activity of lysophospholipase A-I links platelet
RT activation to LPA production during blood coagulation.";
RL J. Lipid Res. 52:958-970(2011).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP THR-210; PHE-211; ALA-218; ASN-231 AND TYR-307.
RX PubMed=21240271; DOI=10.1038/nsmb.1980;
RA Hausmann J., Kamtekar S., Christodoulou E., Day J.E., Wu T., Fulkerson Z.,
RA Albers H.M., van Meeteren L.A., Houben A.J., van Zeijl L., Jansen S.,
RA Andries M., Hall T., Pegg L.E., Benson T.E., Kasiem M., Harlos K.,
RA Kooi C.W., Smyth S.S., Ovaa H., Bollen M., Morris A.J., Moolenaar W.H.,
RA Perrakis A.;
RT "Structural basis of substrate discrimination and integrin binding by
RT autotaxin.";
RL Nat. Struct. Mol. Biol. 18:198-204(2011).
RN [16] {ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 55-860 IN COMPLEX WITH SYNTHETIC
RP INHIBITOR; CALCIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-525, AND
RP DISULFIDE BONDS.
RX PubMed=26371182; DOI=10.1124/mol.115.100404;
RA Stein A.J., Bain G., Prodanovich P., Santini A.M., Darlington J.,
RA Stelzer N.M., Sidhu R.S., Schaub J., Goulet L., Lonergan D., Calderon I.,
RA Evans J.F., Hutchinson J.H.;
RT "Structural Basis for Inhibition of Human Autotaxin by Four Potent
RT Compounds with Distinct Modes of Binding.";
RL Mol. Pharmacol. 88:982-992(2015).
RN [17] {ECO:0007744|PDB:5MHP}
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR;
RP CALCIUM AND ZINC, COFACTOR, AND DISULFIDE BONDS.
RX PubMed=28414242; DOI=10.1021/acs.jmedchem.7b00032;
RA Desroy N., Housseman C., Bock X., Joncour A., Bienvenu N., Cherel L.,
RA Labeguere V., Rondet E., Peixoto C., Grassot J.M., Picolet O., Annoot D.,
RA Triballeau N., Monjardet A., Wakselman E., Roncoroni V., Le Tallec S.,
RA Blanque R., Cottereaux C., Vandervoort N., Christophe T., Mollat P.,
RA Lamers M., Auberval M., Hrvacic B., Ralic J., Oste L., van der Aar E.,
RA Brys R., Heckmann B.;
RT "Discovery of 2-[[2-Ethyl-6-[4-[2-(3-hydroxyazetidin-1-yl)-2-
RT oxoethyl]piperazin-1-yl]-8-methylimidazo[1,2-a]pyridin-3-yl]methylamino]-4-
RT (4-fluorophenyl)thiazole-5-carbonitrile (GLPG1690), a First-in-Class
RT Autotaxin Inhibitor Undergoing Clinical Evaluation for the Treatment of
RT Idiopathic Pulmonary Fibrosis.";
RL J. Med. Chem. 60:3580-3590(2017).
RN [18] {ECO:0007744|PDB:5KXA}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR;
RP CALCIUM AND ZINC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBCELLULAR
RP LOCATION, AND DISULFIDE BONDS.
RX PubMed=27754931; DOI=10.1124/jpet.116.237156;
RA Bain G., Shannon K.E., Huang F., Darlington J., Goulet L., Prodanovich P.,
RA Ma G.L., Santini A.M., Stein A.J., Lonergan D., King C.D., Calderon I.,
RA Lai A., Hutchinson J.H., Evans J.F.;
RT "Selective Inhibition of Autotaxin Is Efficacious in Mouse Models of Liver
RT Fibrosis.";
RL J. Pharmacol. Exp. Ther. 360:1-13(2017).
CC -!- FUNCTION: Hydrolyzes lysophospholipids to produce the signaling
CC molecule lysophosphatidic acid (LPA) in extracellular fluids
CC (PubMed:15769751, PubMed:26371182, PubMed:27754931, PubMed:14500380,
CC PubMed:12354767,). Major substrate is lysophosphatidylcholine
CC (PubMed:12176993, PubMed:27754931, PubMed:14500380). Can also act on
CC sphingosylphosphorylcholine producing sphingosine-1-phosphate, a
CC modulator of cell motility (PubMed:14500380). Can hydrolyze, in vitro,
CC bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:15769751,
CC PubMed:12176993). Involved in several motility-related processes such
CC as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by
CC stimulating migration of smooth muscle cells and microtubule formation
CC (PubMed:11559573). Stimulates migration of melanoma cells, probably via
CC a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role
CC in induction of parturition (PubMed:12176993). Possible involvement in
CC cell proliferation and adipose tissue development (Probable). Tumor
CC cell motility-stimulating factor (PubMed:1733949, PubMed:11559573).
CC Required for LPA production in activated platelets, cleaves the sn-1
CC lysophospholipids to generate sn-1 lysophosphatidic acids containing
CC predominantly 18:2 and 20:4 fatty acids (PubMed:21393252). Shows a
CC preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-
CC phosphocholine (lyso-PAF) (PubMed:21393252).
CC {ECO:0000269|PubMed:11559573, ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:14500380,
CC ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:1733949,
CC ECO:0000269|PubMed:21240271, ECO:0000269|PubMed:21393252,
CC ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931,
CC ECO:0000305|PubMed:15700135}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-O-alkyl-
CC sn-glycero-3-phosphate + ethanolamine + H(+); Xref=Rhea:RHEA:15965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57603,
CC ChEBI:CHEBI:58014, ChEBI:CHEBI:76168; EC=3.1.4.39;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:15769751,
CC ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:21240271,
CC ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(9Z-octadecenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-
CC (9Z-octadecenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41684, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64396, ChEBI:CHEBI:78402;
CC Evidence={ECO:0000269|PubMed:21393252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41685;
CC Evidence={ECO:0000305|PubMed:21393252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:41712,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57875, ChEBI:CHEBI:64982;
CC Evidence={ECO:0000269|PubMed:21393252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41713;
CC Evidence={ECO:0000305|PubMed:21393252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-sn-
CC glycerol 3-phosphate + H(+) + L-serine; Xref=Rhea:RHEA:41716,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:64982, ChEBI:CHEBI:65214;
CC Evidence={ECO:0000269|PubMed:21393252};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41717;
CC Evidence={ECO:0000305|PubMed:21393252};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + H2O = 1-dodecanoyl-
CC sn-glycerol 3-phosphate + choline + H(+); Xref=Rhea:RHEA:38991,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72682, ChEBI:CHEBI:74966;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:21240271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38992;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:21240271};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine-phosphocholine = choline + H(+) + sphing-
CC 4-enine 1-phosphate; Xref=Rhea:RHEA:38919, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58906,
CC ChEBI:CHEBI:60119; Evidence={ECO:0000269|PubMed:14500380};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38920;
CC Evidence={ECO:0000305|PubMed:14500380};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:14500380};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:14500380};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycerol 3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38983, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64489, ChEBI:CHEBI:72683;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:21240271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38984;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:21240271};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoyl-sn-glycero-3-phosphocholine + H2O = 1-decanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41131,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:77724, ChEBI:CHEBI:77726;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41132;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:21240271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:21240271};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38979, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73858, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:21240271};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38980;
CC Evidence={ECO:0000305|PubMed:12176993, ECO:0000305|PubMed:21240271};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41135, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28733, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41136;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate +
CC choline + H(+); Xref=Rhea:RHEA:41139, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344,
CC ChEBI:CHEBI:74938; Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41140;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexanoyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:41400,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:78215, ChEBI:CHEBI:78223;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41401;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dioctanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41416, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78228, ChEBI:CHEBI:78229;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41417;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC didecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41412, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:78226, ChEBI:CHEBI:78227;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41413;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = 1-O-(1Z-
CC alkenyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41588, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:77283, ChEBI:CHEBI:77287;
CC Evidence={ECO:0000269|PubMed:12176993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41589;
CC Evidence={ECO:0000305|PubMed:12176993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ethanolamine + H(+);
CC Xref=Rhea:RHEA:38927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:74544, ChEBI:CHEBI:74971;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38928;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + L-serine;
CC Xref=Rhea:RHEA:38931, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:74544, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38932;
CC Evidence={ECO:0000250|UniProtKB:Q64610};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931,
CC ECO:0000269|PubMed:28414242};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:26371182,
CC ECO:0000269|PubMed:27754931, ECO:0000269|PubMed:28414242};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931,
CC ECO:0000269|PubMed:28414242};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:26371182,
CC ECO:0000269|PubMed:27754931, ECO:0000269|PubMed:28414242};
CC -!- ACTIVITY REGULATION: Inhibited by lysophosphatidic acid (LPA) and
CC sphingosine-1-phosphate (S1P). Inhibited by EDTA and EGTA (Probable).
CC {ECO:0000305|PubMed:15769751, ECO:0000305|PubMed:18175805,
CC ECO:0000305|PubMed:21240271}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for 16:0-LPC (at pH 8.5) {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC KM=5.5 mM for pNP-TMP (at pH 8.5) {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC KM=11.3 mM for pNppp (isoform 1) {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC KM=5.7 mM for pNppp (isoform 2) {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC KM=19.8 mM for pNppp (isoform 3) {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC KM=96 uM for sn-1 lyso-PAF {ECO:0000269|PubMed:21393252};
CC KM=51 uM for sn-2 lyso-PAF {ECO:0000269|PubMed:21393252};
CC KM=0.10 mM for lysophosphatidylcholine {ECO:0000269|PubMed:14500380};
CC KM=0.23 mM for sphingosylphosphorylcholine
CC {ECO:0000269|PubMed:14500380};
CC Vmax=1.9 nmol/min/ug enzyme with pNppp as substrate (isoform 1)
CC {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:18175805};
CC Vmax=0.67 nmol/min/ug enzyme with pNppp as substrate (isoform 2)
CC {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:18175805};
CC Vmax=1.6 nmol/min/ug enzyme with pNppp as substrate (isoform 3)
CC {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:18175805};
CC Vmax=0.11 umol/min/mg enzyme with sn-1 lyso-PAF as substrate
CC {ECO:0000269|PubMed:21393252};
CC Vmax=0.025 umol/min/mg enzyme with sn-2 lyso-PAF as substrate
CC {ECO:0000269|PubMed:21393252};
CC Vmax=11.8 nmol/min/ug enzyme with lysophosphatidylcholine as
CC substrate {ECO:0000269|PubMed:14500380};
CC Vmax=6.1 nmol/min/ug enzyme with sphingosylphosphorylcholine as
CC substrate {ECO:0000269|PubMed:14500380};
CC pH dependence:
CC Optimum pH is 9.0 (isoform 1), 8.0 (isoform 3). Isoform 1 is less
CC sensitive to pH. Isoform 1, isoform 2 and isoform 3 all retain some
CC activity at pH 9.5. {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805};
CC Temperature dependence:
CC Isoform 1 and isoform 3 are active from 45 to 60 degrees Celsius.
CC {ECO:0000269|PubMed:12176993, ECO:0000269|PubMed:18175805};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:1733949,
CC ECO:0000269|PubMed:26371182, ECO:0000269|PubMed:27754931}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ATXter, Beta;
CC IsoId=Q13822-1; Sequence=Displayed;
CC Name=2; Synonyms=ATXmel, Alpha;
CC IsoId=Q13822-2; Sequence=VSP_006750;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q13822-3; Sequence=VSP_036398;
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:12176993, PubMed:26371182). Predominantly expressed in brain,
CC placenta, ovary, and small intestine. Expressed in a number of
CC carcinomas such as hepatocellular and prostate carcinoma, neuroblastoma
CC and non-small-cell lung cancer. Expressed in body fluids such as
CC plasma, cerebral spinal fluid (CSF), saliva, follicular and amniotic
CC fluids. Not detected in leukocytes. Isoform 1 is more highly expressed
CC in peripheral tissues than in the central nervous system (CNS).
CC Adipocytes only express isoform 1. Isoform 3 is more highly expressed
CC in the brain than in peripheral tissues. {ECO:0000269|PubMed:12176993,
CC ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:26371182,
CC ECO:0000269|PubMed:8579579, ECO:0000269|PubMed:8586446}.
CC -!- INDUCTION: Up-regulated in massively obese subjects with glucose
CC intolerance, and during adipogenesis. {ECO:0000269|PubMed:15700135}.
CC -!- PTM: N-glycosylation, but not furin-cleavage, plays a critical role on
CC secretion and on lysoPLD activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- PTM: The interdomain disulfide bond between Cys-414 and Cys-806 is
CC essential for catalytic activity. {ECO:0000250|UniProtKB:Q9R1E6}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ENPP2ID40455ch8q24.html";
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DR EMBL; L35594; AAA64785.1; -; mRNA.
DR EMBL; D45421; BAA08260.1; -; mRNA.
DR EMBL; D45914; BAA08342.1; -; Genomic_DNA.
DR EMBL; L46720; AAB00855.1; -; mRNA.
DR EMBL; EU131011; ABW38316.2; -; mRNA.
DR EMBL; AC099818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034961; AAH34961.1; -; mRNA.
DR CCDS; CCDS34936.1; -. [Q13822-1]
DR CCDS; CCDS47914.1; -. [Q13822-3]
DR CCDS; CCDS6329.1; -. [Q13822-2]
DR PIR; A55144; A55144.
DR RefSeq; NP_001035181.1; NM_001040092.2. [Q13822-1]
DR RefSeq; NP_001124335.1; NM_001130863.2. [Q13822-3]
DR RefSeq; NP_006200.3; NM_006209.4. [Q13822-2]
DR PDB; 4ZG6; X-ray; 1.80 A; A/B=17-863.
DR PDB; 4ZG7; X-ray; 1.75 A; A=55-860.
DR PDB; 4ZG9; X-ray; 2.95 A; A/B=1-863.
DR PDB; 4ZGA; X-ray; 2.60 A; A=1-863.
DR PDB; 5KXA; X-ray; 2.59 A; A=1-863.
DR PDB; 5M7M; X-ray; 2.70 A; A=1-863.
DR PDB; 5MHP; X-ray; 2.43 A; A=1-863.
DR PDBsum; 4ZG6; -.
DR PDBsum; 4ZG7; -.
DR PDBsum; 4ZG9; -.
DR PDBsum; 4ZGA; -.
DR PDBsum; 5KXA; -.
DR PDBsum; 5M7M; -.
DR PDBsum; 5MHP; -.
DR AlphaFoldDB; Q13822; -.
DR SMR; Q13822; -.
DR BioGRID; 111194; 4.
DR IntAct; Q13822; 3.
DR MINT; Q13822; -.
DR STRING; 9606.ENSP00000259486; -.
DR BindingDB; Q13822; -.
DR ChEMBL; CHEMBL3691; -.
DR DrugCentral; Q13822; -.
DR GuidetoPHARMACOLOGY; 2901; -.
DR SwissLipids; SLP:000000393; -.
DR SwissLipids; SLP:000000641; -. [Q13822-1]
DR GlyConnect; 1197; 4 N-Linked glycans (1 site).
DR GlyGen; Q13822; 4 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q13822; -.
DR PhosphoSitePlus; Q13822; -.
DR BioMuta; ENPP2; -.
DR DMDM; 290457674; -.
DR jPOST; Q13822; -.
DR MassIVE; Q13822; -.
DR PeptideAtlas; Q13822; -.
DR PRIDE; Q13822; -.
DR ProteomicsDB; 20576; -.
DR ProteomicsDB; 59692; -. [Q13822-1]
DR ProteomicsDB; 59693; -. [Q13822-2]
DR ProteomicsDB; 59694; -. [Q13822-3]
DR Antibodypedia; 13653; 418 antibodies from 39 providers.
DR DNASU; 5168; -.
DR Ensembl; ENST00000075322.11; ENSP00000075322.6; ENSG00000136960.13. [Q13822-1]
DR Ensembl; ENST00000259486.10; ENSP00000259486.6; ENSG00000136960.13. [Q13822-2]
DR Ensembl; ENST00000522826.5; ENSP00000428291.1; ENSG00000136960.13. [Q13822-3]
DR GeneID; 5168; -.
DR KEGG; hsa:5168; -.
DR MANE-Select; ENST00000075322.11; ENSP00000075322.6; NM_001040092.3; NP_001035181.1.
DR UCSC; uc003yos.3; human. [Q13822-1]
DR CTD; 5168; -.
DR DisGeNET; 5168; -.
DR GeneCards; ENPP2; -.
DR HGNC; HGNC:3357; ENPP2.
DR HPA; ENSG00000136960; Tissue enhanced (brain, choroid plexus).
DR MIM; 601060; gene.
DR neXtProt; NX_Q13822; -.
DR OpenTargets; ENSG00000136960; -.
DR PharmGKB; PA27792; -.
DR VEuPathDB; HostDB:ENSG00000136960; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000155778; -.
DR HOGENOM; CLU_012256_0_0_1; -.
DR InParanoid; Q13822; -.
DR OMA; TNYHVVC; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q13822; -.
DR TreeFam; TF330032; -.
DR BioCyc; MetaCyc:HS06258-MON; -.
DR BRENDA; 3.1.4.39; 2681.
DR PathwayCommons; Q13822; -.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR SABIO-RK; Q13822; -.
DR SignaLink; Q13822; -.
DR BioGRID-ORCS; 5168; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; ENPP2; human.
DR GeneWiki; Autotaxin; -.
DR GenomeRNAi; 5168; -.
DR Pharos; Q13822; Tchem.
DR PRO; PR:Q13822; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q13822; protein.
DR Bgee; ENSG00000136960; Expressed in pigmented layer of retina and 206 other tissues.
DR ExpressionAtlas; Q13822; baseline and differential.
DR Genevisible; Q13822; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004551; F:nucleotide diphosphatase activity; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IBA:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0048870; P:cell motility; TAS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; NAS:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IGI:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0030149; P:sphingolipid catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR029881; ENPP2.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR10151:SF21; PTHR10151:SF21; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Chemotaxis;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Obesity; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:Q64610"
FT PROPEP 28..35
FT /note="Removed by furin"
FT /evidence="ECO:0000269|PubMed:12176993,
FT ECO:0000269|PubMed:18175805"
FT /id="PRO_0000281649"
FT CHAIN 36..863
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 2"
FT /id="PRO_0000188567"
FT DOMAIN 55..98
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 99..143
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REGION 830..851
FT /note="Required for secretion"
FT /evidence="ECO:0000250"
FT MOTIF 127..129
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:5KXA"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:5KXA"
FT BINDING 211..214
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26371182,
FT ECO:0007744|PDB:4ZG7"
FT BINDING 244..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:5KXA"
FT BINDING 360
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:5KXA"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA"
FT BINDING 740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA"
FT BINDING 742
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA"
FT BINDING 744
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA"
FT BINDING 746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA"
FT BINDING 748
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0000269|PubMed:27754931, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA"
FT SITE 853
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q9R1E6"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:26371182,
FT ECO:0007744|PDB:4ZG6, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:4ZGA"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 63..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 74..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 80..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 103..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 108..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 118..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 124..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 149..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 157..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 367..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:4ZG9, ECO:0007744|PDB:5M7M"
FT DISULFID 414..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 567..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 569..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG7,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT DISULFID 775..785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350,
FT ECO:0000269|PubMed:26371182, ECO:0007744|PDB:4ZG6,
FT ECO:0007744|PDB:4ZG7, ECO:0007744|PDB:4ZG9,
FT ECO:0007744|PDB:4ZGA, ECO:0007744|PDB:5KXA,
FT ECO:0007744|PDB:5M7M, ECO:0007744|PDB:5MHP"
FT VAR_SEQ 324
FT /note="E -> EESSYGSPFTPAKRPKRKVAPKRRQERPVAPPKKRRRKIHRMDHYAA
FT ETRQDK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18175805,
FT ECO:0000303|PubMed:7982964"
FT /id="VSP_006750"
FT VAR_SEQ 593
FT /note="E -> EAETRKFRGSRNENKENINGNFEPRK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18175805"
FT /id="VSP_036398"
FT VARIANT 493
FT /note="S -> P (in dbSNP:rs10283100)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15769751, ECO:0000269|PubMed:1733949,
FT ECO:0000269|PubMed:18175805, ECO:0000269|PubMed:7982964,
FT ECO:0000269|PubMed:8579579, ECO:0000269|PubMed:8586446"
FT /id="VAR_060469"
FT VARIANT 577
FT /note="N -> S (in dbSNP:rs2289886)"
FT /id="VAR_057472"
FT VARIANT 726
FT /note="S -> L (in dbSNP:rs16892767)"
FT /id="VAR_057473"
FT MUTAGEN 170
FT /note="S->E: Reduces lysophospholipase activity by about
FT 70%."
FT MUTAGEN 210
FT /note="T->A: Loss of lysophospholipase activity and ability
FT to hydrolyze sphingosylphosphorylcholine."
FT /evidence="ECO:0000269|PubMed:14500380,
FT ECO:0000269|PubMed:21240271"
FT MUTAGEN 211
FT /note="F->Y: Reduces lysophospholipase activity by about
FT 70%."
FT /evidence="ECO:0000269|PubMed:21240271"
FT MUTAGEN 218
FT /note="A->V: Reduces lysophospholipase activity by about
FT 50%."
FT /evidence="ECO:0000269|PubMed:21240271"
FT MUTAGEN 231
FT /note="N->A: Strongly reduced lysophospholipase activity."
FT /evidence="ECO:0000269|PubMed:21240271"
FT MUTAGEN 307
FT /note="Y->Q: Reduces lysophospholipase activity by about
FT 70%."
FT /evidence="ECO:0000269|PubMed:21240271"
FT MUTAGEN 316
FT /note="H->Q: Loss of ability to hydrolyze
FT sphingosylphosphorylcholine."
FT /evidence="ECO:0000269|PubMed:14500380"
FT MUTAGEN 360
FT /note="H->Q: Loss of ability to hydrolyze
FT sphingosylphosphorylcholine."
FT /evidence="ECO:0000269|PubMed:14500380"
FT CONFLICT 23
FT /note="N -> S (in Ref. 1; AAA64785 and 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> H (in Ref. 2; BAA08260)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="G -> A (in Ref. 3; AAB00855)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Q -> R (in Ref. 1; AAA64785 and 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="H -> R (in Ref. 1; AAA64785 and 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="K -> P (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="V -> S (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="E -> N (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="P -> L (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="P -> L (in Ref. 1; AAA64785 and 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="S -> R (in Ref. 2; BAA08260)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="V -> A (in Ref. 2; BAA08260)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="Y -> H (in Ref. 2; BAA08260)"
FT /evidence="ECO:0000305"
FT TURN 60..64
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4ZG9"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4ZG9"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4ZGA"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 326..345
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:4ZG6"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 388..399
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:5M7M"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 509..516
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:4ZG6"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 624..627
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 628..636
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 647..649
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 667..672
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 690..692
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 699..701
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 720..728
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 730..738
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 744..746
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 766..777
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 782..784
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 789..797
FT /evidence="ECO:0007829|PDB:4ZG7"
FT TURN 806..809
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 816..822
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 827..834
FT /evidence="ECO:0007829|PDB:4ZG7"
FT STRAND 841..844
FT /evidence="ECO:0007829|PDB:4ZG7"
FT HELIX 846..854
FT /evidence="ECO:0007829|PDB:4ZG7"
FT CONFLICT Q13822-3:23
FT /note="N -> S (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:291
FT /note="Q -> R (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:349
FT /note="H -> R (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:493
FT /note="S -> P (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:599
FT /note="F -> Y (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:602
FT /note="S -> T (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
FT CONFLICT Q13822-3:654
FT /note="P -> L (in Ref. 5; ABW38316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 98994 MW; 94A7A2B3701F0993 CRC64;
MARRSSFQSC QIISLFTFAV GVNICLGFTA HRIKRAEGWE EGPPTVLSDS PWTNISGSCK
GRCFELQEAG PPDCRCDNLC KSYTSCCHDF DELCLKTARG WECTKDRCGE VRNEENACHC
SEDCLARGDC CTNYQVVCKG ESHWVDDDCE EIKAAECPAG FVRPPLIIFS VDGFRASYMK
KGSKVMPNIE KLRSCGTHSP YMRPVYPTKT FPNLYTLATG LYPESHGIVG NSMYDPVFDA
TFHLRGREKF NHRWWGGQPL WITATKQGVK AGTFFWSVVI PHERRILTIL QWLTLPDHER
PSVYAFYSEQ PDFSGHKYGP FGPEMTNPLR EIDKIVGQLM DGLKQLKLHR CVNVIFVGDH
GMEDVTCDRT EFLSNYLTNV DDITLVPGTL GRIRSKFSNN AKYDPKAIIA NLTCKKPDQH
FKPYLKQHLP KRLHYANNRR IEDIHLLVER RWHVARKPLD VYKKPSGKCF FQGDHGFDNK
VNSMQTVFVG YGSTFKYKTK VPPFENIELY NVMCDLLGLK PAPNNGTHGS LNHLLRTNTF
RPTMPEEVTR PNYPGIMYLQ SDFDLGCTCD DKVEPKNKLD ELNKRLHTKG STEERHLLYG
RPAVLYRTRY DILYHTDFES GYSEIFLMPL WTSYTVSKQA EVSSVPDHLT SCVRPDVRVS
PSFSQNCLAY KNDKQMSYGF LFPPYLSSSP EAKYDAFLVT NMVPMYPAFK RVWNYFQRVL
VKKYASERNG VNVISGPIFD YDYDGLHDTE DKIKQYVEGS SIPVPTHYYS IITSCLDFTQ
PADKCDGPLS VSSFILPHRP DNEESCNSSE DESKWVEELM KMHTARVRDI EHLTSLDFFR
KTSRSYPEIL TLKTYLHTYE SEI
