ID   PLD2_HUMAN              Reviewed;         933 AA.
AC   O14939; I3L2C9; O43540; O43579; O43580; Q6PGR0; Q96BY3;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Phospholipase D2 {ECO:0000305};
DE            Short=PLD 2;
DE            Short=hPLD2;
DE            EC=3.1.4.4 {ECO:0000269|PubMed:9582313};
DE   AltName: Full=Choline phosphatase 2;
DE   AltName: Full=PLD1C;
DE   AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D2;
GN   Name=PLD2 {ECO:0000312|HGNC:HGNC:9068};
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] (ISOFORMS PLD2A; PLD2B AND PLD2C),
RP   CHARACTERIZATION, AND VARIANT CYS-172.
RC   TISSUE=Brain;
RX   PubMed=9761774; DOI=10.1096/fasebj.12.13.1309;
RA   Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.;
RT   "Characterization of human PLD2 and the analysis of PLD isoform splice
RT   variants.";
RL   FASEB J. 12:1309-1317(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD2A), CHARACTERIZATION, VARIANT
RP   ILE-577, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   TISSUE=B-cell;
RX   PubMed=9582313; DOI=10.1074/jbc.273.21.12846;
RA   Lopez I., Arnold R.S., Lambeth J.D.;
RT   "Cloning and initial characterization of a human phospholipase D2 (hPLD2).
RT   ADP-ribosylation factor regulates hPLD2.";
RL   J. Biol. Chem. 273:12846-12852(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD2A AND PLD2B), AND VARIANTS GLY-632
RP   AND SER-821.
RA   Saqib K.M., Clark J.M., Byrd P.J., Armstrong S.J., Wakelam M.J.O.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD2A), AND VARIANTS
RP   CYS-172; ILE-577 AND GLY-632.
RC   TISSUE=Skin, and Uterus;
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   [7]
RP   INTERACTION WITH PIP5K1B.
RX   PubMed=11032811; DOI=10.1093/emboj/19.20.5440;
RA   Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M.,
RA   Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
RT   "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for
RT   the local generation of phosphatidylinositol 4, 5-bisphosphate in the
RT   regulation of PLD2 activity.";
RL   EMBO J. 19:5440-5449(2000).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] GLU-807.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Function as phospholipase selective for phosphatidylcholine
CC       (PubMed:9582313). May have a role in signal-induced cytoskeletal
CC       regulation and/or endocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:P97813, ECO:0000269|PubMed:9582313}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000269|PubMed:9582313};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446;
CC         Evidence={ECO:0000305|PubMed:9582313};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC         dihexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC         Xref=Rhea:RHEA:44872, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:72859, ChEBI:CHEBI:72999;
CC         Evidence={ECO:0000269|PubMed:9582313};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873;
CC         Evidence={ECO:0000305|PubMed:9582313};
CC   -!- ACTIVITY REGULATION: Stimulated by phosphatidylinositol 4,5-
CC       bisphosphate and slightly activated by the ADP-ribosylation factor-1
CC       (ARF-1). {ECO:0000269|PubMed:9582313}.
CC   -!- SUBUNIT: Interacts with PIP5K1B (PubMed:11032811). Interacts with EGFR
CC       (By similarity). {ECO:0000250|UniProtKB:P97813,
CC       ECO:0000269|PubMed:11032811}.
CC   -!- INTERACTION:
CC       O14939; P05067: APP; NbExp=3; IntAct=EBI-1053996, EBI-77613;
CC       O14939; P23528: CFL1; NbExp=2; IntAct=EBI-1053996, EBI-352733;
CC       O14939; P62993: GRB2; NbExp=4; IntAct=EBI-1053996, EBI-401755;
CC       O14939; P15153: RAC2; NbExp=4; IntAct=EBI-1053996, EBI-489652;
CC       O14939; P13051-2: UNG; NbExp=3; IntAct=EBI-1053996, EBI-25834258;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97813};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P97813}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=PLD2A;
CC         IsoId=O14939-1; Sequence=Displayed;
CC       Name=PLD2C;
CC         IsoId=O14939-3; Sequence=VSP_005027;
CC       Name=PLD2B;
CC         IsoId=O14939-4; Sequence=VSP_054769;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9582313}.
CC   -!- PTM: Phosphorylated by FGR. {ECO:0000250|UniProtKB:P70498}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Phospholipase D entry;
CC       URL="https://en.wikipedia.org/wiki/Phospholipase_D";
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DR   EMBL; AF033850; AAD04197.1; -; mRNA.
DR   EMBL; AF035483; AAC24498.1; -; mRNA.
DR   EMBL; AF038440; AAB96655.1; -; mRNA.
DR   EMBL; AF038441; AAB96656.1; -; mRNA.
DR   EMBL; AC233723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471108; EAW90405.1; -; Genomic_DNA.
DR   EMBL; BC015033; AAH15033.1; -; mRNA.
DR   EMBL; BC056871; AAH56871.1; -; mRNA.
DR   CCDS; CCDS11057.1; -. [O14939-1]
DR   CCDS; CCDS58507.1; -. [O14939-4]
DR   RefSeq; NP_001230037.1; NM_001243108.1. [O14939-4]
DR   RefSeq; NP_002654.3; NM_002663.4. [O14939-1]
DR   PDB; 6OHM; X-ray; 1.90 A; A/B=294-933.
DR   PDB; 6OHO; X-ray; 2.00 A; A/B=294-933.
DR   PDB; 6OHP; X-ray; 2.60 A; A/B/C/D=294-933.
DR   PDB; 6OHQ; X-ray; 2.69 A; A/B=294-933.
DR   PDB; 6OHS; X-ray; 3.20 A; A/B/C/D=294-933.
DR   PDB; 7SVP; X-ray; 2.90 A; A/B/C/D=294-933.
DR   PDBsum; 6OHM; -.
DR   PDBsum; 6OHO; -.
DR   PDBsum; 6OHP; -.
DR   PDBsum; 6OHQ; -.
DR   PDBsum; 6OHS; -.
DR   PDBsum; 7SVP; -.
DR   AlphaFoldDB; O14939; -.
DR   SMR; O14939; -.
DR   BioGRID; 111354; 161.
DR   DIP; DIP-38903N; -.
DR   IntAct; O14939; 22.
DR   MINT; O14939; -.
DR   STRING; 9606.ENSP00000263088; -.
DR   BindingDB; O14939; -.
DR   ChEMBL; CHEMBL2734; -.
DR   DrugBank; DB00122; Choline.
DR   DrugBank; DB14006; Choline salicylate.
DR   DrugCentral; O14939; -.
DR   GuidetoPHARMACOLOGY; 1434; -.
DR   SwissLipids; SLP:000000108; -.
DR   iPTMnet; O14939; -.
DR   PhosphoSitePlus; O14939; -.
DR   SwissPalm; O14939; -.
DR   BioMuta; PLD2; -.
DR   EPD; O14939; -.
DR   jPOST; O14939; -.
DR   MassIVE; O14939; -.
DR   MaxQB; O14939; -.
DR   PaxDb; 9606-ENSP00000263088; -.
DR   PeptideAtlas; O14939; -.
DR   ProteomicsDB; 46910; -.
DR   ProteomicsDB; 48324; -. [O14939-1]
DR   ProteomicsDB; 48326; -. [O14939-3]
DR   Pumba; O14939; -.
DR   Antibodypedia; 2859; 312 antibodies from 34 providers.
DR   DNASU; 5338; -.
DR   Ensembl; ENST00000263088.11; ENSP00000263088.5; ENSG00000129219.14. [O14939-1]
DR   Ensembl; ENST00000572940.5; ENSP00000459571.1; ENSG00000129219.14. [O14939-4]
DR   GeneID; 5338; -.
DR   KEGG; hsa:5338; -.
DR   MANE-Select; ENST00000263088.11; ENSP00000263088.5; NM_002663.5; NP_002654.3.
DR   UCSC; uc002fzc.4; human. [O14939-1]
DR   AGR; HGNC:9068; -.
DR   DisGeNET; 5338; -.
DR   GeneCards; PLD2; -.
DR   HGNC; HGNC:9068; PLD2.
DR   HPA; ENSG00000129219; Low tissue specificity.
DR   MIM; 602384; gene.
DR   neXtProt; NX_O14939; -.
DR   OpenTargets; ENSG00000129219; -.
DR   PharmGKB; PA33397; -.
DR   VEuPathDB; HostDB:ENSG00000129219; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   GeneTree; ENSGT00940000160229; -.
DR   HOGENOM; CLU_000690_2_0_1; -.
DR   InParanoid; O14939; -.
DR   OMA; VRHPHRE; -.
DR   OrthoDB; 335467at2759; -.
DR   PhylomeDB; O14939; -.
DR   TreeFam; TF300589; -.
DR   BRENDA; 3.1.4.4; 2681.
DR   BRENDA; 4.2.1.1; 2681.
DR   PathwayCommons; O14939; -.
DR   Reactome; R-HSA-1483148; Synthesis of PG.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR   SignaLink; O14939; -.
DR   SIGNOR; O14939; -.
DR   BioGRID-ORCS; 5338; 11 hits in 1158 CRISPR screens.
DR   ChiTaRS; PLD2; human.
DR   GeneWiki; PLD2; -.
DR   GenomeRNAi; 5338; -.
DR   Pharos; O14939; Tchem.
DR   PRO; PR:O14939; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O14939; Protein.
DR   Bgee; ENSG00000129219; Expressed in lower esophagus mucosa and 191 other cell types or tissues.
DR   ExpressionAtlas; O14939; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR   GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR   GO; GO:0036465; P:synaptic vesicle recycling; TAS:ParkinsonsUK-UCL.
DR   CDD; cd01254; PH_PLD; 1.
DR   CDD; cd09845; PLDc_vPLD2_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF121; PHOSPHOLIPASE D2; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS50195; PX; 1.
DR   Genevisible; O14939; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..933
FT                   /note="Phospholipase D2"
FT                   /id="PRO_0000218805"
FT   DOMAIN          65..195
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          203..311
FT                   /note="PH"
FT   DOMAIN          437..464
FT                   /note="PLD phosphodiesterase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   DOMAIN          751..778
FT                   /note="PLD phosphodiesterase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..788
FT                   /note="Catalytic"
FT   REGION          477..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         337..933
FT                   /note="Missing (in isoform PLD2C)"
FT                   /evidence="ECO:0000303|PubMed:9761774"
FT                   /id="VSP_005027"
FT   VAR_SEQ         810..821
FT                   /note="RFALSLRKHCFG -> S (in isoform PLD2B)"
FT                   /evidence="ECO:0000303|PubMed:9761774, ECO:0000303|Ref.3"
FT                   /id="VSP_054769"
FT   VARIANT         172
FT                   /note="R -> C (in dbSNP:rs2286672)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9761774"
FT                   /id="VAR_051704"
FT   VARIANT         577
FT                   /note="T -> I (in dbSNP:rs1052748)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9582313"
FT                   /id="VAR_051705"
FT   VARIANT         632
FT                   /note="E -> G (in dbSNP:rs17854914)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_061750"
FT   VARIANT         804
FT                   /note="A -> T (in dbSNP:rs11545163)"
FT                   /id="VAR_051706"
FT   VARIANT         807
FT                   /note="Q -> E (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036503"
FT   VARIANT         821
FT                   /note="G -> R (in dbSNP:rs3764897)"
FT                   /id="VAR_051707"
FT   VARIANT         821
FT                   /note="G -> S (in dbSNP:rs3764897)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_059774"
FT   CONFLICT        16
FT                   /note="D -> G (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="Y -> C (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="R -> C (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="Q -> R (in Ref. 3; AAB96655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        325
FT                   /note="S -> R (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        445
FT                   /note="L -> P (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510
FT                   /note="D -> G (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="T -> I (in Ref. 3; AAB96655)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        784
FT                   /note="D -> G (in Ref. 3; AAB96656)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        801..802
FT                   /note="MN -> ID (in Ref. 2; AAC24498)"
FT                   /evidence="ECO:0000305"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:6OHO"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          330..340
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           341..353
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          356..365
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          371..375
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           383..392
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          396..402
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            406..408
FT                   /evidence="ECO:0007829|PDB:6OHP"
FT   HELIX           413..423
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          427..432
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          445..448
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            449..451
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          452..457
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            514..516
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            532..534
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          543..549
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           550..567
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           571..574
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          600..610
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           612..615
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           621..632
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          634..642
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          650..652
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           657..671
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          676..680
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           691..693
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           697..710
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          712..716
FT                   /evidence="ECO:0007829|PDB:6OHP"
FT   HELIX           717..725
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           726..731
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          733..744
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          747..752
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          758..762
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            763..765
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          766..771
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           776..779
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          780..801
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          804..809
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           810..824
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            826..828
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          837..839
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           840..861
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           872..878
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           884..887
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           889..896
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   STRAND          901..905
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   TURN            908..913
FT                   /evidence="ECO:0007829|PDB:6OHM"
FT   HELIX           929..931
FT                   /evidence="ECO:0007829|PDB:6OHM"
SQ   SEQUENCE   933 AA;  105987 MW;  F25F6B73B45F57ED CRC64;
     MTATPESLFP TGDELDSSQL QMESDEVDTL KEGEDPADRM HPFLAIYELQ SLKVHPLVFA
     PGVPVTAQVV GTERYTSGSK VGTCTLYSVR LTHGDFSWTT KKKYRHFQEL HRDLLRHKVL
     MSLLPLARFA VAYSPARDAG NREMPSLPRA GPEGSTRHAA SKQKYLENYL NRLLTMSFYR
     NYHAMTEFLE VSQLSFIPDL GRKGLEGMIR KRSGGHRVPG LTCCGRDQVC YRWSKRWLVV
     KDSFLLYMCL ETGAISFVQL FDPGFEVQVG KRSTEARHGV RIDTSHRSLI LKCSSYRQAR
     WWAQEITELA QGPGRDFLQL HRHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF
     ITDWWLSPEV YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRAL
     MLLHPNIKVM RHPDQVTLWA HHEKLLVVDQ VVAFLGGLDL AYGRWDDLHY RLTDLGDSSE
     SAASQPPTPR PDSPATPDLS HNQFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW
     RDVGVVVHGL PARDLARHFI QRWNFTKTTK AKYKTPTYPY LLPKSTSTAN QLPFTLPGGQ
     CTTVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE
     IVDRILKAHK QGWCYRVYVL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEYSILHR
     LKAAMGTAWR DYISICGLRT HGELGGHPVS ELIYIHSKVL IADDRTVIIG SANINDRSLL
     GKRDSELAVL IEDTETEPSL MNGAEYQAGR FALSLRKHCF GVILGANTRP DLDLRDPICD
     DFFQLWQDMA ESNANIYEQI FRCLPSNATR SLRTLREYVA VEPLATVSPP LARSELTQVQ
     GHLVHFPLKF LEDESLLPPL GSKEGMIPLE VWT
//