PRKX_HUMAN
ID PRKX_HUMAN Reviewed; 358 AA.
AC P51817;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit PRKX;
DE Short=PrKX;
DE Short=Protein kinase X;
DE Short=Protein kinase X-linked;
DE Short=Serine/threonine-protein kinase PRKX;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase PKX1;
GN Name=PRKX; Synonyms=PKX1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=7633447; DOI=10.1093/hmg/4.5.869;
RA Klink A., Schiebel K., Winkelmann M., Rao E., Horsthemke B.,
RA Luedecke H.-J., Claussen U., Scherer G., Rappold G.;
RT "The human protein kinase gene PKX1 on Xp22.3 displays Xp/Yp homology and
RT is a site of chromosomal instability.";
RL Hum. Mol. Genet. 4:869-878(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [3]
RP CHROMOSOMAL TRANSLOCATION WITH PRKY.
RX PubMed=9302280; DOI=10.1093/hmg/6.11.1985;
RA Schiebel K., Winkelmann M., Mertz A., Xu X., Page D.C., Weil D., Petit C.,
RA Rappold G.A.;
RT "Abnormal XY interchange between a novel isolated protein kinase gene,
RT PRKY, and its homologue, PRKX, accounts for one third of all (Y+)XX males
RT and (Y-)XY females.";
RL Hum. Mol. Genet. 6:1985-1989(1997).
RN [4]
RP FUNCTION IN MYELOID CELL DIFFERENTIATION, TISSUE SPECIFICITY, AND INDUCTION
RP BY PMA.
RX PubMed=9860982; DOI=10.1073/pnas.95.26.15412;
RA Semizarov D., Glesne D., Laouar A., Schiebel K., Huberman E.;
RT "A lineage-specific protein kinase crucial for myeloid maturation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15412-15417(1998).
RN [5]
RP CATALYTIC ACTIVITY, KINETIC PARAMETERS, INTERACTION WITH PRKAR1A AND PKI,
RP ACTIVITY REGULATION BY PRKAR1A AND PKI, SUBCELLULAR LOCATION, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=10026146; DOI=10.1074/jbc.274.9.5370;
RA Zimmermann B., Chiorini J.A., Ma Y., Kotin R.M., Herberg F.W.;
RT "PrKX is a novel catalytic subunit of the cAMP-dependent protein kinase
RT regulated by the regulatory subunit type I.";
RL J. Biol. Chem. 274:5370-5378(1999).
RN [6]
RP FUNCTION IN CREB-DEPENDENT TRANSCRIPTION, FUNCTION IN RENAL EPITHELIAL CELL
RP MIGRATION AND TUBULOGENESIS, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-78, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12082174; DOI=10.1073/pnas.132051799;
RA Li X., Li H.P., Amsler K., Hyink D., Wilson P.D., Burrow C.R.;
RT "PRKX, a phylogenetically and functionally distinct cAMP-dependent protein
RT kinase, activates renal epithelial cell migration and morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9260-9265(2002).
RN [7]
RP FUNCTION IN NEPHROGENESIS, MUTAGENESIS OF HIS-93 AND TRP-202, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16236808; DOI=10.1681/asn.2005030240;
RA Li X., Hyink D.P., Polgar K., Gusella G.L., Wilson P.D., Burrow C.R.;
RT "Protein kinase X activates ureteric bud branching morphogenesis in
RT developing mouse metanephric kidney.";
RL J. Am. Soc. Nephrol. 16:3543-3552(2005).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15879576; DOI=10.1369/jhc.4a6568.2005;
RA Li W., Yu Z.X., Kotin R.M.;
RT "Profiles of PrKX expression in developmental mouse embryo and human
RT tissues.";
RL J. Histochem. Cytochem. 53:1003-1009(2005).
RN [9]
RP FUNCTION IN MYELOID CELL DIFFERENTIATION, FUNCTION IN PHOSPHORYLATION OF
RP SMAD6, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH GPKOW;
RP PRKAR1A; SMAD6, AND INDUCTION BY PMA.
RX PubMed=16491121; DOI=10.1038/sj.onc.1209436;
RA Glesne D., Huberman E.;
RT "Smad6 is a protein kinase X phosphorylation substrate and is required for
RT HL-60 cell differentiation.";
RL Oncogene 25:4086-4098(2006).
RN [10]
RP FUNCTION IN NEPHROGENESIS, FUNCTION IN PHOSPHORYLATION OF PKD1, AND
RP INTERACTION WITH PKD1.
RX PubMed=17980165; DOI=10.1016/j.bbadis.2007.09.003;
RA Li X., Burrow C.R., Polgar K., Hyink D.P., Gusella G.L., Wilson P.D.;
RT "Protein kinase X (PRKX) can rescue the effects of polycystic kidney
RT disease-1 gene (PKD1) deficiency.";
RL Biochim. Biophys. Acta 1782:1-9(2008).
RN [11]
RP FUNCTION IN NEPHROGENESIS, AND INTERACTION WITH PIN1.
RX PubMed=19367327; DOI=10.1038/ki.2009.95;
RA Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N.,
RA Wilson P.D.;
RT "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney
RT development.";
RL Kidney Int. 76:54-62(2009).
RN [12]
RP ACTIVITY REGULATION, INTERACTION WITH PRKAR1A AND PRKAR1B, AND MUTAGENESIS
RP OF ARG-283.
RX PubMed=20819953; DOI=10.1074/jbc.m110.155150;
RA Diskar M., Zenn H.M., Kaupisch A., Kaufholz M., Brockmeyer S., Sohmen D.,
RA Berrera M., Zaccolo M., Boshart M., Herberg F.W., Prinz A.;
RT "Regulation of cAMP-dependent protein kinases: the human protein kinase X
RT (PrKX) reveals the role of the catalytic subunit alphaH-alphaI loop.";
RL J. Biol. Chem. 285:35910-35918(2010).
RN [13]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=21684272; DOI=10.1016/j.ydbio.2011.05.673;
RA Li X., Iomini C., Hyink D., Wilson P.D.;
RT "PRKX critically regulates endothelial cell proliferation, migration, and
RT vascular-like structure formation.";
RL Dev. Biol. 356:475-485(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Serine/threonine protein kinase regulated by and mediating
CC cAMP signaling in cells. Acts through phosphorylation of downstream
CC targets that may include CREB, SMAD6 and PKD1 and has multiple
CC functions in cellular differentiation and epithelial morphogenesis.
CC Regulates myeloid cell differentiation through SMAD6 phosphorylation.
CC Involved in nephrogenesis by stimulating renal epithelial cell
CC migration and tubulogenesis. Also involved in angiogenesis through
CC stimulation of endothelial cell proliferation, migration and vascular-
CC like structure formation. {ECO:0000269|PubMed:12082174,
CC ECO:0000269|PubMed:16236808, ECO:0000269|PubMed:16491121,
CC ECO:0000269|PubMed:17980165, ECO:0000269|PubMed:19367327,
CC ECO:0000269|PubMed:21684272, ECO:0000269|PubMed:9860982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:10026146, ECO:0000269|PubMed:12082174};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10026146,
CC ECO:0000269|PubMed:12082174};
CC -!- ACTIVITY REGULATION: Binding of cAMP to the PRKAR1A or PRKAR1B
CC regulatory subunits induces dissociation of the holoenzyme
CC heterotetramer. The released monomeric PRKX is then active and able to
CC phosphorylate its substrates. {ECO:0000269|PubMed:10026146,
CC ECO:0000269|PubMed:12082174, ECO:0000269|PubMed:20819953}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=127 uM for ATP (in the presence of 10 mM magnesium chloride)
CC {ECO:0000269|PubMed:10026146, ECO:0000269|PubMed:12082174};
CC KM=58 uM for kemptide (in the presence of 10 mM magnesium chloride)
CC {ECO:0000269|PubMed:10026146, ECO:0000269|PubMed:12082174};
CC KM=6.7 uM for kemptide (in the presence of 1 uM Br-cAMP at 30 degrees
CC Celsius) {ECO:0000269|PubMed:10026146, ECO:0000269|PubMed:12082174};
CC -!- SUBUNIT: Like other cAMP-dependent protein kinases, the inactive
CC holoenzyme is probably composed of 2 PRKX catalytic subunits and a
CC dimer of regulatory subunits. Interacts (cAMP-dependent) specifically
CC with the regulatory subunits PRKAR1A and PRKAR1B. Compared to other
CC cAMP-dependent serine/threonine protein kinases, does not interact with
CC the 2 other PKA regulatory subunits PRKAR2A and PRKAR2B. Interacts with
CC cAMP-dependent protein kinase inhibitor/PKI proteins; inhibits PRKX.
CC Interacts with GPKOW. Interacts with SMAD6. Interacts with PKD1;
CC involved in differentiation and controlled morphogenesis of the kidney.
CC Interacts with PIN1 (via WW domain). {ECO:0000269|PubMed:10026146,
CC ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:17980165,
CC ECO:0000269|PubMed:19367327, ECO:0000269|PubMed:20819953}.
CC -!- INTERACTION:
CC P51817; Q92917: GPKOW; NbExp=2; IntAct=EBI-4302903, EBI-746309;
CC P51817; P08238: HSP90AB1; NbExp=3; IntAct=EBI-4302903, EBI-352572;
CC P51817; P10644: PRKAR1A; NbExp=2; IntAct=EBI-4302903, EBI-476431;
CC P51817; O43541: SMAD6; NbExp=5; IntAct=EBI-4302903, EBI-976374;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=cAMP induces nuclear
CC translocation.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Specifically
CC expressed in blood by macrophages and granulocytes according to
CC PubMed:9860982. {ECO:0000269|PubMed:15879576,
CC ECO:0000269|PubMed:16236808, ECO:0000269|PubMed:7633447,
CC ECO:0000269|PubMed:9860982}.
CC -!- DEVELOPMENTAL STAGE: Expression is developmentally regulated being high
CC and specific in a wide range of developing tissues including liver,
CC kidney, brain and pancreas (at protein level).
CC {ECO:0000269|PubMed:12082174, ECO:0000269|PubMed:15879576,
CC ECO:0000269|PubMed:16236808}.
CC -!- INDUCTION: Up-regulated by phorbol 12-myristate 13-acetate (PMA).
CC {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:9860982}.
CC -!- PTM: Phosphorylated; autophosphorylates in vitro.
CC -!- DISEASE: Note=A chromosomal aberration involving PRKX is a cause of sex
CC reversal disorder. Translocation t(X;Y)(p22;p11) with PRKY. Chromosomal
CC translocations proximal to PRKY account for about 30% of the cases of
CC sex reversal disorder in XX males and XY females.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; X85545; CAA59733.1; -; mRNA.
DR EMBL; BC041073; AAH41073.1; -; mRNA.
DR CCDS; CCDS14125.1; -.
DR PIR; I38121; I38121.
DR RefSeq; NP_005035.1; NM_005044.4.
DR AlphaFoldDB; P51817; -.
DR SMR; P51817; -.
DR BioGRID; 111599; 44.
DR IntAct; P51817; 16.
DR STRING; 9606.ENSP00000262848; -.
DR BindingDB; P51817; -.
DR ChEMBL; CHEMBL5818; -.
DR DrugCentral; P51817; -.
DR GuidetoPHARMACOLOGY; 2175; -.
DR iPTMnet; P51817; -.
DR PhosphoSitePlus; P51817; -.
DR BioMuta; PRKX; -.
DR DMDM; 1709648; -.
DR EPD; P51817; -.
DR jPOST; P51817; -.
DR MassIVE; P51817; -.
DR MaxQB; P51817; -.
DR PaxDb; P51817; -.
DR PeptideAtlas; P51817; -.
DR PRIDE; P51817; -.
DR ProteomicsDB; 56426; -.
DR Antibodypedia; 7924; 237 antibodies from 30 providers.
DR DNASU; 5613; -.
DR Ensembl; ENST00000262848.6; ENSP00000262848.5; ENSG00000183943.6.
DR GeneID; 5613; -.
DR KEGG; hsa:5613; -.
DR MANE-Select; ENST00000262848.6; ENSP00000262848.5; NM_005044.5; NP_005035.1.
DR UCSC; uc010nde.4; human.
DR CTD; 5613; -.
DR DisGeNET; 5613; -.
DR GeneCards; PRKX; -.
DR HGNC; HGNC:9441; PRKX.
DR HPA; ENSG00000183943; Tissue enhanced (thyroid).
DR MIM; 300083; gene.
DR neXtProt; NX_P51817; -.
DR OpenTargets; ENSG00000183943; -.
DR PharmGKB; PA33786; -.
DR VEuPathDB; HostDB:ENSG00000183943; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000159832; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P51817; -.
DR OMA; QEDPPRY; -.
DR OrthoDB; 963519at2759; -.
DR PhylomeDB; P51817; -.
DR TreeFam; TF313399; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P51817; -.
DR Reactome; R-HSA-111931; PKA-mediated phosphorylation of CREB.
DR Reactome; R-HSA-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR SABIO-RK; P51817; -.
DR SignaLink; P51817; -.
DR SIGNOR; P51817; -.
DR BioGRID-ORCS; 5613; 8 hits in 731 CRISPR screens.
DR ChiTaRS; PRKX; human.
DR GenomeRNAi; 5613; -.
DR Pharos; P51817; Tchem.
DR PRO; PR:P51817; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51817; protein.
DR Bgee; ENSG00000183943; Expressed in ganglionic eminence and 153 other tissues.
DR ExpressionAtlas; P51817; baseline and differential.
DR Genevisible; P51817; HS.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0060562; P:epithelial tube morphogenesis; IDA:UniProtKB.
DR GO; GO:0060993; P:kidney morphogenesis; IDA:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:2000696; P:regulation of epithelial cell differentiation involved in kidney development; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Angiogenesis; ATP-binding; cAMP; Chromosomal rearrangement;
KW Cytoplasm; Developmental protein; Differentiation; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..358
FT /note="cAMP-dependent protein kinase catalytic subunit
FT PRKX"
FT /id="PRO_0000086582"
FT DOMAIN 49..303
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 304..358
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q922R0"
FT VARIANT 43
FT /note="V -> A (in dbSNP:rs3752362)"
FT /id="VAR_061744"
FT MUTAGEN 78
FT /note="K->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:12082174"
FT MUTAGEN 93
FT /note="H->Q: Constitutive kinase activity; when associated
FT with R-202."
FT /evidence="ECO:0000269|PubMed:16236808"
FT MUTAGEN 202
FT /note="W->R: Constitutive kinase activity; when associated
FT with Q-93."
FT /evidence="ECO:0000269|PubMed:16236808"
FT MUTAGEN 283
FT /note="R->L: Increases the affinity for PRKAR2A and
FT PRKAR2B."
FT /evidence="ECO:0000269|PubMed:20819953"
SQ SEQUENCE 358 AA; 40896 MW; B603834E3541CB56 CRC64;
MEAPGLAQAA AAESDSRKVA EETPDGAPAL CPSPEALSPE PPVYSLQDFD TLATVGTGTF
GRVHLVKEKT AKHFFALKVM SIPDVIRLKQ EQHVHNEKSV LKEVSHPFLI RLFWTWHDER
FLYMLMEYVP GGELFSYLRN RGRFSSTTGL FYSAEIICAI EYLHSKEIVY RDLKPENILL
DRDGHIKLTD FGFAKKLVDR TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG
FPPFFDDNPF GIYQKILAGK IDFPRHLDFH VKDLIKKLLV VDRTRRLGNM KNGANDVKHH
RWFRSVDWEA VPQRKLKPPI VPKIAGDGDT SNFETYPEND WDTAAPVPQK DLEIFKNF
