PA24D_HUMAN
ID PA24D_HUMAN Reviewed; 818 AA.
AC Q86XP0; Q8N176;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cytosolic phospholipase A2 delta {ECO:0000305};
DE Short=cPLA2-delta {ECO:0000303|PubMed:14709560};
DE EC=3.1.1.4 {ECO:0000269|PubMed:14709560};
DE AltName: Full=Phospholipase A2 group IVD;
GN Name=PLA2G4D {ECO:0000312|HGNC:HGNC:30038};
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 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE
RP SPECIFICITY, AND DOMAIN.
RX PubMed=14709560; DOI=10.1074/jbc.m305801200;
RA Chiba H., Michibata H., Wakimoto K., Seishima M., Kawasaki S., Okubo K.,
RA Mitsui H., Torii H., Imai Y.;
RT "Cloning of a gene for a novel epithelium-specific cytosolic phospholipase
RT A2, cPLA2delta, induced in psoriatic skin.";
RL J. Biol. Chem. 279:12890-12897(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 491-818 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZ5, ECO:0007744|PDB:5IZR}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-810 IN COMPLEX WITH SUBSTRATE
RP ANALOG, REGION, AND ACTIVE SITE.
RX PubMed=27220631; DOI=10.1016/j.jmb.2016.05.012;
RA Wang H., Klein M.G., Snell G., Lane W., Zou H., Levin I., Li K., Sang B.C.;
RT "Structure of human GIVD cytosolic phospholipase A2 reveals insights into
RT substrate recognition.";
RL J. Mol. Biol. 428:2769-2779(2016).
RN [5]
RP VARIANT GLY-747.
RX PubMed=16213696; DOI=10.1016/j.plefa.2005.08.008;
RA Tao R., Yu Y., Zhang X., Shi J., Guo Y., Wang C., Han B., Xu Q., Shang H.,
RA Zhang X., Xie L., Liu S., Ju G., Shen Y., Wei J.;
RT "A family based study of the genetic association between the PLA2G4D gene
RT and schizophrenia.";
RL Prostaglandins Leukot. Essent. Fatty Acids 73:419-422(2005).
CC -!- FUNCTION: Calcium-dependent phospholipase A2 that selectively
CC hydrolyzes glycerophospholipids in the sn-2 position (PubMed:14709560).
CC Has a preference for linoleic acid at the sn-2 position
CC (PubMed:14709560). {ECO:0000269|PubMed:14709560}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:14709560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:14709560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:14709560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:14709560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:14709560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:14709560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:14709560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:14709560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:Q50L43};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q50L43};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:Q50L43};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q50L43};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+).
CC {ECO:0000269|PubMed:14709560}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=9.23 pmol/min/mg enzyme with 1-palmitoyl-2-arachidonyl-
CC phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560};
CC Vmax=58.56 pmol/min/mg enzyme with 1-palmitoyl-2-linoleoyl-
CC phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560};
CC Vmax=11 pmol/min/mg enzyme with 1-palmitoyl-2-oleoyl-
CC phosphatidylcholine as substrate {ECO:0000269|PubMed:14709560};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:14709560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q50L43}. Membrane
CC {ECO:0000250|UniProtKB:Q50L43}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q50L43}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q50L43}. Note=Translocates to perinuclear
CC membranes that may correspond to endoplasmic reticulum or Golgi in a
CC calcium-dependent fashion. {ECO:0000250|UniProtKB:Q50L43}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86XP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XP0-2; Sequence=VSP_019881, VSP_019882;
CC -!- TISSUE SPECIFICITY: Expressed in stratified squamous epithelia, such as
CC those in skin and cervix, but not in other tissues (PubMed:14709560).
CC Strongly expressed in the upper spinous layer of the psoriatic
CC epidermis, expressed weakly and discontinuously in atopic dermatitis
CC and mycosis fungoides, and not detected in the epidermis of normal skin
CC (PubMed:14709560). {ECO:0000269|PubMed:14709560}.
CC -!- DOMAIN: The N-terminal C2 domain mediates the association with lipid
CC membranes upon calcium binding (Probable). An additional second C2
CC domain may stand in between the C2 domain and the PLA2c domain
CC (Probable). {ECO:0000305|PubMed:14709560}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB090876; BAC67158.1; -; mRNA.
DR EMBL; AC084693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034571; AAH34571.1; ALT_INIT; mRNA.
DR CCDS; CCDS32203.1; -. [Q86XP0-1]
DR RefSeq; NP_828848.3; NM_178034.3. [Q86XP0-1]
DR PDB; 5IXC; X-ray; 2.65 A; A/B=2-810.
DR PDB; 5IZ5; X-ray; 2.20 A; A/B=2-810.
DR PDB; 5IZR; X-ray; 3.25 A; A/B/C/D=2-810.
DR PDBsum; 5IXC; -.
DR PDBsum; 5IZ5; -.
DR PDBsum; 5IZR; -.
DR AlphaFoldDB; Q86XP0; -.
DR SMR; Q86XP0; -.
DR BioGRID; 129664; 36.
DR STRING; 9606.ENSP00000290472; -.
DR ChEMBL; CHEMBL2287; -.
DR SwissLipids; SLP:000001080; -.
DR iPTMnet; Q86XP0; -.
DR PhosphoSitePlus; Q86XP0; -.
DR BioMuta; PLA2G4D; -.
DR DMDM; 269849641; -.
DR MassIVE; Q86XP0; -.
DR MaxQB; Q86XP0; -.
DR PaxDb; Q86XP0; -.
DR PeptideAtlas; Q86XP0; -.
DR PRIDE; Q86XP0; -.
DR ProteomicsDB; 70307; -. [Q86XP0-1]
DR ProteomicsDB; 70308; -. [Q86XP0-2]
DR Antibodypedia; 23488; 77 antibodies from 22 providers.
DR DNASU; 283748; -.
DR Ensembl; ENST00000290472.4; ENSP00000290472.3; ENSG00000159337.7. [Q86XP0-1]
DR GeneID; 283748; -.
DR KEGG; hsa:283748; -.
DR MANE-Select; ENST00000290472.4; ENSP00000290472.3; NM_178034.4; NP_828848.3.
DR UCSC; uc001zox.3; human. [Q86XP0-1]
DR CTD; 283748; -.
DR DisGeNET; 283748; -.
DR GeneCards; PLA2G4D; -.
DR HGNC; HGNC:30038; PLA2G4D.
DR HPA; ENSG00000159337; Group enriched (prostate, skin, vagina).
DR MIM; 612864; gene.
DR neXtProt; NX_Q86XP0; -.
DR OpenTargets; ENSG00000159337; -.
DR PharmGKB; PA134974074; -.
DR VEuPathDB; HostDB:ENSG00000159337; -.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; Q86XP0; -.
DR OMA; NSSHPVW; -.
DR OrthoDB; 302848at2759; -.
DR PhylomeDB; Q86XP0; -.
DR TreeFam; TF325228; -.
DR BRENDA; 3.1.1.4; 2681.
DR PathwayCommons; Q86XP0; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; Q86XP0; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 283748; 15 hits in 1068 CRISPR screens.
DR GenomeRNAi; 283748; -.
DR Pharos; Q86XP0; Tbio.
DR PRO; PR:Q86XP0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q86XP0; protein.
DR Bgee; ENSG00000159337; Expressed in skin of abdomen and 50 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0008970; F:phospholipase A1 activity; TAS:Reactome.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
DR CDD; cd04036; C2_cPLA2; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR041847; C2_cPLA2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR040723; cPLA2_C2.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF18695; cPLA2_C2; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasm; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Reference proteome.
FT CHAIN 1..818
FT /note="Cytosolic phospholipase A2 delta"
FT /id="PRO_0000247023"
FT DOMAIN 5..124
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 273..818
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT ACT_SITE 361
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:27220631,
FT ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR"
FT ACT_SITE 647
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330..331
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27220631,
FT ECO:0007744|PDB:5IXC, ECO:0007744|PDB:5IZR"
FT VAR_SEQ 682..723
FT /note="ALQQTELYCRARGLPFPRVEPSPQDQHQPRECHLFSDPACPE -> VPWSPQ
FT GNPSAQPGQAPEASSRATEPLPHTAGVPKGRRGVRP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019881"
FT VAR_SEQ 724..818
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019882"
FT VARIANT 275
FT /note="P -> R (in dbSNP:rs11635685)"
FT /id="VAR_057676"
FT VARIANT 434
FT /note="S -> T (in dbSNP:rs4924618)"
FT /id="VAR_057677"
FT VARIANT 573
FT /note="R -> W (in dbSNP:rs17747505)"
FT /id="VAR_027049"
FT VARIANT 649
FT /note="A -> G (in dbSNP:rs17690899)"
FT /id="VAR_027050"
FT VARIANT 747
FT /note="R -> G (in dbSNP:rs2459692)"
FT /evidence="ECO:0000269|PubMed:16213696"
FT /id="VAR_027051"
FT VARIANT 783
FT /note="R -> Q (in dbSNP:rs750052)"
FT /id="VAR_057678"
FT VARIANT 807
FT /note="R -> Q (in dbSNP:rs750051)"
FT /id="VAR_057679"
FT CONFLICT 10
FT /note="P -> T (in Ref. 1; BAC67158)"
FT /evidence="ECO:0000305"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 21..33
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5IXC"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 288..309
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 331..347
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 382..393
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 402..418
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 424..436
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 469..473
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 520..527
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:5IXC"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 584..590
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 605..608
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 618..621
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 656..660
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 667..672
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 681..692
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 704..708
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 719..723
FT /evidence="ECO:0007829|PDB:5IXC"
FT STRAND 726..730
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 736..739
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:5IZ5"
FT TURN 749..751
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:5IZ5"
FT STRAND 760..763
FT /evidence="ECO:0007829|PDB:5IZR"
FT HELIX 775..790
FT /evidence="ECO:0007829|PDB:5IZ5"
FT HELIX 793..806
FT /evidence="ECO:0007829|PDB:5IZ5"
FT CONFLICT Q86XP0-2:713
FT /note="G -> R (in Ref. 2; AAH34571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 91952 MW; 06187324748A4C21 CRC64;
MESLSPGGPP GHPYQGEAST CWQLTVRVLE ARNLRWADLL SEADPYVILQ LSTAPGMKFK
TKTLTDTSHP VWNEAFRFLI QSQVKNVLEL SIYDEDSVTE DDICFKVLYD ISEVLPGKLL
RKTFSQSPQG EEELDVEFLM EETSDRPENL ITNKVIVARE LSCLDVHLDS TGSTAVVADQ
DKLELELVLK GSYEDTQTSF LGTASAFRFH YMAALETELS GRLRSSRSNG WNGDNSAGYL
TVPLRPLTIG KEVTMDVPAP NAPGVRLQLK AEGCPEELAV HLGFNLCAEE QAFLSRRKQV
VAKALKQALQ LDRDLQEDEV PVVGIMATGG GARAMTSLYG HLLALQKLGL LDCVTYFSGI
SGSTWTMAHL YGDPEWSQRD LEGPIRYARE HLAKSKLEVF SPERLASYRR ELELRAEQGH
PTTFVDLWAL VLESMLHGQV MDQKLSGQRA ALERGQNPLP LYLSLNVKEN NLETLDFKEW
VEFSPYEVGF LKYGAFVPPE LFGSEFFMGR LMRRIPEPRI CFLEAIWSNI FSLNLLDAWY
DLTSSGESWK QHIKDKTRSL EKEPLTTSGT SSRLEASWLQ PGTALAQAFK GFLTGRPLHQ
RSPNFLQGLQ LHQDYCSHKD FSTWADYQLD SMPSQLTPKE PRLCLVDAAY FINTSSPSMF
RPGRRLDLIL SFDYSLSAPF EALQQTELYC RARGLPFPRV EPSPQDQHQP RECHLFSDPA
CPEAPILLHF PLVNASFKDH SAPGVQRSPA ELQGGQVDLT GATCPYTLSN MTYKEEDFER
LLRLSDYNVQ TSQGAILQAL RTALKHRTLE ARPPRAQT
