PLD2_HUMAN
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 03-AUG-2022, entry version 199.
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 PDBsum; 6OHM; -.
DR PDBsum; 6OHO; -.
DR PDBsum; 6OHP; -.
DR PDBsum; 6OHQ; -.
DR PDBsum; 6OHS; -.
DR AlphaFoldDB; O14939; -.
DR SMR; O14939; -.
DR BioGRID; 111354; 124.
DR DIP; DIP-38903N; -.
DR IntAct; O14939; 21.
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; O14939; -.
DR PeptideAtlas; O14939; -.
DR PRIDE; O14939; -.
DR ProteomicsDB; 46910; -.
DR ProteomicsDB; 48324; -. [O14939-1]
DR ProteomicsDB; 48326; -. [O14939-3]
DR Antibodypedia; 2859; 288 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 CTD; 5338; -.
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; 755722at2759; -.
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; 8 hits in 1077 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 189 other tissues.
DR ExpressionAtlas; O14939; baseline and differential.
DR Genevisible; O14939; HS.
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:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
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 Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1520.10; -; 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; PTHR18896; 2.
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; SSF64268; SSF64268; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
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
