PDE6D_HUMAN
ID PDE6D_HUMAN Reviewed; 150 AA.
AC O43924; O43250;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta;
DE Short=GMP-PDE delta;
DE AltName: Full=Protein p17;
GN Name=PDE6D; Synonyms=PDED;
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 [GENOMIC DNA].
RX PubMed=9570951; DOI=10.1006/geno.1998.5210;
RA Li N., Florio S.K., Pettenati M.J., Rao P.N., Beavo J.A., Baehr W.;
RT "Characterization of human and mouse rod cGMP phosphodiesterase delta
RT subunit (PDE6D) and chromosomal localization of the human gene.";
RL Genomics 49:76-82(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9533031; DOI=10.1159/000134701;
RA Erchova G., Derre J., Chatelin S., Nancy V., Berger R., Kaplan J.,
RA Munnich A., de Gunzburg J.;
RT "cDNA sequence, genomic organization and mapping of PDE6D, the human gene
RT encoding the delta subunit of the cGMP phosphodiesterase of retinal rod
RT cells to chromosome 2q36.";
RL Cytogenet. Cell Genet. 79:139-141(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9781033; DOI=10.1038/sj.ejhg.5200215;
RA Lorenz B., Migliaccio C., Lichtner P., Meyer C., Strom T.M., D'Urso M.,
RA Becker J., Ciccodicola A., Meitinger T.;
RT "Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit
RT gene (PDED) in man and mouse.";
RL Eur. J. Hum. Genet. 6:283-290(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB13, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9712853; DOI=10.1074/jbc.273.35.22340;
RA Marzesco A.M., Galli T., Louvard D., Zahraoui A.;
RT "The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase
RT Rab13 from membranes.";
RL J. Biol. Chem. 273:22340-22345(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 ARL3.
RX PubMed=10518933; DOI=10.1016/s0014-5793(99)01117-5;
RA Linari M., Hanzal-Bayer M., Becker J.;
RT "The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta,
RT interacts with the Arf-like protein Arl3 in a GTP specific manner.";
RL FEBS Lett. 458:55-59(1999).
RN [8]
RP INTERACTION WITH RPGR.
RX PubMed=9990021; DOI=10.1073/pnas.96.4.1315;
RA Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.;
RT "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta
RT subunit of rod cyclic GMP phosphodiesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INVOLVEMENT IN JBTS22, FUNCTION, INTERACTION WITH RPGR; ARL2; ARL3 AND
RP INPP5E, AND SUBCELLULAR LOCATION.
RX PubMed=24166846; DOI=10.1002/humu.22470;
RA Thomas S., Wright K.J., Le Corre S., Micalizzi A., Romani M., Abhyankar A.,
RA Saada J., Perrault I., Amiel J., Litzler J., Filhol E., Elkhartoufi N.,
RA Kwong M., Casanova J.L., Boddaert N., Baehr W., Lyonnet S., Munnich A.,
RA Burglen L., Chassaing N., Encha-Ravazi F., Vekemans M., Gleeson J.G.,
RA Valente E.M., Jackson P.K., Drummond I.A., Saunier S., Attie-Bitach T.;
RT "A homozygous PDE6D mutation in Joubert syndrome impairs targeting of
RT farnesylated INPP5E protein to the primary cilium.";
RL Hum. Mutat. 35:137-146(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MOUSE ARL2 AND GTP,
RP AND INTERACTION WITH HRAS.
RX PubMed=11980706; DOI=10.1093/emboj/21.9.2095;
RA Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.;
RT "The complex of Arl2-GTP and PDE delta: from structure to function.";
RL EMBO J. 21:2095-2106(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH RHEB, FUNCTION,
RP INTERACTION WITH RHEB; NRAS AND ARL2, AND SUBCELLULAR LOCATION.
RX PubMed=22002721; DOI=10.1038/nchembio.686;
RA Ismail S.A., Chen Y.X., Rusinova A., Chandra A., Bierbaum M., Gremer L.,
RA Triola G., Waldmann H., Bastiaens P.I., Wittinghofer A.;
RT "Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for
RT farnesylated cargo.";
RL Nat. Chem. Biol. 7:942-949(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH RPGR, FUNCTION, AND
RP INTERACTION WITH RPGR.
RX PubMed=23559067; DOI=10.1038/embor.2013.37;
RA Watzlich D., Vetter I., Gotthardt K., Miertzschke M., Chen Y.X.,
RA Wittinghofer A., Ismail S.;
RT "The interplay between RPGR, PDE? and Arl2/3 regulate the ciliary targeting
RT of farnesylated cargo.";
RL EMBO Rep. 14:465-472(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), FUNCTION, INTERACTION WITH RHEB AND
RP KRAS, AND SUBCELLULAR LOCATION.
RX PubMed=23698361; DOI=10.1038/nature12205;
RA Zimmermann G., Papke B., Ismail S., Vartak N., Chandra A., Hoffmann M.,
RA Hahn S.A., Triola G., Wittinghofer A., Bastiaens P.I., Waldmann H.;
RT "Small molecule inhibition of the KRAS-PDE? interaction impairs oncogenic
RT KRAS signalling.";
RL Nature 497:638-642(2013).
CC -!- FUNCTION: Promotes the release of prenylated target proteins from
CC cellular membranes (PubMed:9712853). Modulates the activity of
CC prenylated or palmitoylated Ras family members by regulating their
CC subcellular location (PubMed:22002721, PubMed:23698361). Required for
CC normal ciliary targeting of farnesylated target proteins, such as
CC INPP5E (PubMed:24166846). Modulates the subcellular location of target
CC proteins by acting as a GTP specific dissociation inhibitor (GDI) (By
CC similarity). Increases the affinity of ARL3 for GTP by several orders
CC of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide
CC dissociation rate (By similarity). {ECO:0000250|UniProtKB:O55057,
CC ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:22002721,
CC ECO:0000269|PubMed:23559067, ECO:0000269|PubMed:23698361,
CC ECO:0000269|PubMed:24166846, ECO:0000269|PubMed:9712853}.
CC -!- SUBUNIT: Interacts with the prenylated catalytic subunits of PDE6, an
CC oligomer composed of two catalytic chains (PDE6A and PDE6B) and two
CC inhibitory chains (gamma); has no effect on enzyme activity but
CC promotes the release of the prenylated enzyme from cell membrane (By
CC similarity). Interacts with prenylated GRK1 and GRK7 (By similarity).
CC Interacts with prenylated Ras family members, including RAP2A and RAP2C
CC (By similarity). Interacts with prenylated RHEB and NRAS
CC (PubMed:22002721). Interacts with prenylated HRAS and KRAS. Interacts
CC with RAB13 (prenylated form); dissociates RAB13 from membranes
CC (PubMed:9712853). Interacts with prenylated INPP5E (PubMed:24166846).
CC Interacts with RPGR (PubMed:9990021, PubMed:24166846, PubMed:23559067).
CC Interacts with ARL2 (PubMed:24166846, PubMed:22002721). Interacts with
CC ARL3; the interaction occurs specifically with the GTP-bound form of
CC ARL3 (PubMed:24166846). Interaction with ARL2 and ARL3 promotes release
CC of farnesylated cargo proteins (PubMed:22002721).
CC {ECO:0000250|UniProtKB:O55057, ECO:0000250|UniProtKB:Q95142,
CC ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:11980706,
CC ECO:0000269|PubMed:22002721, ECO:0000269|PubMed:23559067,
CC ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24166846,
CC ECO:0000269|PubMed:9990021}.
CC -!- INTERACTION:
CC O43924; Q9NXU5: ARL15; NbExp=4; IntAct=EBI-712685, EBI-711759;
CC O43924; Q0P5N6: ARL16; NbExp=13; IntAct=EBI-712685, EBI-10186132;
CC O43924; P36404: ARL2; NbExp=18; IntAct=EBI-712685, EBI-752365;
CC O43924; P36405: ARL3; NbExp=8; IntAct=EBI-712685, EBI-712710;
CC O43924; Q5XKR4: OTP; NbExp=3; IntAct=EBI-712685, EBI-12865884;
CC O43924; P51153: RAB13; NbExp=2; IntAct=EBI-712685, EBI-1780121;
CC O43924; PRO_0000082708 [Q15382]: RHEB; NbExp=5; IntAct=EBI-712685, EBI-6860739;
CC O43924; Q92834: RPGR; NbExp=10; IntAct=EBI-712685, EBI-6558417;
CC O43924; Q92834-2: RPGR; NbExp=3; IntAct=EBI-712685, EBI-6558503;
CC O43924; Q9D0J4: Arl2; Xeno; NbExp=6; IntAct=EBI-712685, EBI-1033319;
CC O43924; Q9WUL7: Arl3; Xeno; NbExp=4; IntAct=EBI-712685, EBI-6860857;
CC O43924; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-712685, EBI-6480811;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22002721,
CC ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:9712853}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:9712853}; Peripheral membrane
CC protein {ECO:0000269|PubMed:9712853}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:24166846}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in various tissues
CC including spleen, prostate gland, testis, ovary, small intestine,
CC colon, retina, and peripheral blood. {ECO:0000269|PubMed:9712853}.
CC -!- DISEASE: Joubert syndrome 22 (JBTS22) [MIM:615665]: A disorder
CC presenting with cerebellar ataxia, oculomotor apraxia, hypotonia,
CC neonatal breathing abnormalities and psychomotor delay.
CC Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. {ECO:0000269|PubMed:24166846}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; AF045999; AAC39720.1; -; Genomic_DNA.
DR EMBL; AF022912; AAB87872.1; -; mRNA.
DR EMBL; AF042835; AAC25953.1; -; Genomic_DNA.
DR EMBL; AF042833; AAC25953.1; JOINED; Genomic_DNA.
DR EMBL; AF042834; AAC25953.1; JOINED; Genomic_DNA.
DR EMBL; AJ001626; CAA04880.1; -; mRNA.
DR EMBL; BT007278; AAP35942.1; -; mRNA.
DR EMBL; BC007831; AAH07831.1; -; mRNA.
DR CCDS; CCDS33398.1; -.
DR RefSeq; NP_001277947.1; NM_001291018.1.
DR RefSeq; NP_002592.1; NM_002601.3.
DR PDB; 1KSG; X-ray; 2.30 A; B=1-150.
DR PDB; 1KSH; X-ray; 1.80 A; B=1-150.
DR PDB; 1KSJ; X-ray; 2.60 A; B=1-150.
DR PDB; 3T5G; X-ray; 1.70 A; B=1-150.
DR PDB; 3T5I; X-ray; 2.10 A; A/B/C/D=1-150.
DR PDB; 4JHP; X-ray; 1.90 A; B=1-150.
DR PDB; 4JV6; X-ray; 1.87 A; B=1-150.
DR PDB; 4JV8; X-ray; 1.45 A; B=1-150.
DR PDB; 4JVB; X-ray; 1.75 A; B=1-150.
DR PDB; 4JVF; X-ray; 2.40 A; B=1-150.
DR PDB; 5E80; X-ray; 2.60 A; A/B=2-150.
DR PDB; 5E8F; X-ray; 2.10 A; A/C=2-150.
DR PDB; 5F2U; X-ray; 1.85 A; A/B=2-150.
DR PDB; 5ML2; X-ray; 1.60 A; B=2-150.
DR PDB; 5ML3; X-ray; 1.40 A; B=2-150.
DR PDB; 5ML4; X-ray; 2.40 A; B=2-150.
DR PDB; 5ML6; X-ray; 1.87 A; B=2-150.
DR PDB; 5ML8; X-ray; 2.60 A; B=2-150.
DR PDB; 5NAL; X-ray; 2.20 A; B=1-150.
DR PDB; 5TAR; X-ray; 1.90 A; B=3-150.
DR PDB; 5TB5; X-ray; 2.00 A; B/D=1-150.
DR PDB; 5X72; X-ray; 1.95 A; A=1-150.
DR PDB; 5X73; X-ray; 2.50 A; A=1-150.
DR PDB; 5X74; X-ray; 2.25 A; A=1-150.
DR PDB; 5YAV; X-ray; 1.99 A; B=1-150.
DR PDB; 5YAW; X-ray; 2.03 A; B=1-150.
DR PDB; 7Q9Q; X-ray; 1.45 A; BBB=2-150.
DR PDB; 7Q9R; X-ray; 2.50 A; BBB=1-150.
DR PDB; 7Q9S; X-ray; 1.85 A; AAA/BBB=1-150.
DR PDB; 7Q9U; X-ray; 2.24 A; CCC/DDD=1-150.
DR PDB; 7QF9; X-ray; 1.95 A; AAA/BBB=2-150.
DR PDB; 7QJK; X-ray; 3.10 A; AAA/BBB/CCC/DDD=1-150.
DR PDBsum; 1KSG; -.
DR PDBsum; 1KSH; -.
DR PDBsum; 1KSJ; -.
DR PDBsum; 3T5G; -.
DR PDBsum; 3T5I; -.
DR PDBsum; 4JHP; -.
DR PDBsum; 4JV6; -.
DR PDBsum; 4JV8; -.
DR PDBsum; 4JVB; -.
DR PDBsum; 4JVF; -.
DR PDBsum; 5E80; -.
DR PDBsum; 5E8F; -.
DR PDBsum; 5F2U; -.
DR PDBsum; 5ML2; -.
DR PDBsum; 5ML3; -.
DR PDBsum; 5ML4; -.
DR PDBsum; 5ML6; -.
DR PDBsum; 5ML8; -.
DR PDBsum; 5NAL; -.
DR PDBsum; 5TAR; -.
DR PDBsum; 5TB5; -.
DR PDBsum; 5X72; -.
DR PDBsum; 5X73; -.
DR PDBsum; 5X74; -.
DR PDBsum; 5YAV; -.
DR PDBsum; 5YAW; -.
DR PDBsum; 7Q9Q; -.
DR PDBsum; 7Q9R; -.
DR PDBsum; 7Q9S; -.
DR PDBsum; 7Q9U; -.
DR PDBsum; 7QF9; -.
DR PDBsum; 7QJK; -.
DR AlphaFoldDB; O43924; -.
DR SMR; O43924; -.
DR BioGRID; 111173; 55.
DR CORUM; O43924; -.
DR DIP; DIP-36660N; -.
DR IntAct; O43924; 30.
DR MINT; O43924; -.
DR STRING; 9606.ENSP00000287600; -.
DR BindingDB; O43924; -.
DR ChEMBL; CHEMBL3860; -.
DR DrugCentral; O43924; -.
DR iPTMnet; O43924; -.
DR PhosphoSitePlus; O43924; -.
DR BioMuta; PDE6D; -.
DR EPD; O43924; -.
DR jPOST; O43924; -.
DR MassIVE; O43924; -.
DR PaxDb; O43924; -.
DR PeptideAtlas; O43924; -.
DR PRIDE; O43924; -.
DR ProteomicsDB; 49239; -.
DR Antibodypedia; 34421; 152 antibodies from 26 providers.
DR DNASU; 5147; -.
DR Ensembl; ENST00000287600.9; ENSP00000287600.4; ENSG00000156973.14.
DR GeneID; 5147; -.
DR KEGG; hsa:5147; -.
DR MANE-Select; ENST00000287600.9; ENSP00000287600.4; NM_002601.4; NP_002592.1.
DR CTD; 5147; -.
DR DisGeNET; 5147; -.
DR GeneCards; PDE6D; -.
DR GeneReviews; PDE6D; -.
DR HGNC; HGNC:8788; PDE6D.
DR HPA; ENSG00000156973; Low tissue specificity.
DR MalaCards; PDE6D; -.
DR MIM; 602676; gene.
DR MIM; 615665; phenotype.
DR neXtProt; NX_O43924; -.
DR OpenTargets; ENSG00000156973; -.
DR Orphanet; 2754; Orofaciodigital syndrome type 6.
DR PharmGKB; PA33136; -.
DR VEuPathDB; HostDB:ENSG00000156973; -.
DR eggNOG; KOG4038; Eukaryota.
DR GeneTree; ENSGT00390000000263; -.
DR HOGENOM; CLU_119682_0_0_1; -.
DR OMA; FKGRCLE; -.
DR OrthoDB; 1192412at2759; -.
DR PhylomeDB; O43924; -.
DR TreeFam; TF314474; -.
DR PathwayCommons; O43924; -.
DR Reactome; R-HSA-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR Reactome; R-HSA-9648002; RAS processing.
DR SignaLink; O43924; -.
DR BioGRID-ORCS; 5147; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; PDE6D; human.
DR EvolutionaryTrace; O43924; -.
DR GeneWiki; PDE6D; -.
DR GenomeRNAi; 5147; -.
DR Pharos; O43924; Tclin.
DR PRO; PR:O43924; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43924; protein.
DR Bgee; ENSG00000156973; Expressed in left testis and 198 other tissues.
DR ExpressionAtlas; O43924; baseline and differential.
DR Genevisible; O43924; HS.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 2.70.50.40; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008015; PDED_dom.
DR InterPro; IPR037036; PDED_dom_sf.
DR InterPro; IPR017287; Rhodop-sen_GMP-Pdiesterase_dsu.
DR Pfam; PF05351; GMP_PDE_delta; 1.
DR PIRSF; PIRSF037825; GMP-Pdiesterase_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; cGMP; Ciliopathy; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Joubert syndrome; Membrane;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..150
FT /note="Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic
FT phosphodiesterase subunit delta"
FT /id="PRO_0000221208"
FT REGION 144..150
FT /note="Required for association with membranes"
FT /evidence="ECO:0000269|PubMed:9712853"
FT CONFLICT 117
FT /note="M -> V (in Ref. 4; CAA04880)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="R -> G (in Ref. 4; CAA04880)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:5ML3"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:5ML3"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 57..69
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5ML3"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3T5G"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5ML3"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5ML3"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:5ML3"
SQ SEQUENCE 150 AA; 17420 MW; AB8D9309C33B4411 CRC64;
MSAKDERARE ILRGFKLNWM NLRDAETGKI LWQGTEDLSV PGVEHEARVP KKILKCKAVS
RELNFSSTEQ MEKFRLEQKV YFKGQCLEEW FFEFGFVIPN STNTWQSLIE AAPESQMMPA
SVLTGNVIIE TKFFDDDLLV STSRVRLFYV
