DAAM2_HUMAN
ID DAAM2_HUMAN Reviewed; 1068 AA.
AC Q86T65; G5EA45; Q5T4T8; Q5T4U0; Q9NQI5; Q9Y4G0;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Disheveled-associated activator of morphogenesis 2;
GN Name=DAAM2 {ECO:0000312|HGNC:HGNC:18143};
GN Synonyms=KIAA0381 {ECO:0000303|PubMed:9205841};
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 [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH INF2, INVOLVEMENT IN NPHS24,
RP VARIANTS NPHS24 GLN-121; GLN-335; 445-ARG--TYR-1068 DEL; HIS-582 AND
RP LEU-1028, AND CHARACTERIZATION OF VARIANTS NPHS24 GLN-121; GLN-335;
RP 445-ARG--TYR-1068 DEL; HIS-582 AND LEU-1028.
RX PubMed=33232676; DOI=10.1016/j.ajhg.2020.11.008;
RA Schneider R., Deutsch K., Hoeprich G.J., Marquez J., Hermle T., Braun D.A.,
RA Seltzsam S., Kitzler T.M., Mao Y., Buerger F., Majmundar A.J.,
RA Onuchic-Whitford A.C., Kolvenbach C.M., Schierbaum L., Schneider S.,
RA Halawi A.A., Nakayama M., Mann N., Connaughton D.M., Klaembt V., Wagner M.,
RA Riedhammer K.M., Renders L., Katsura Y., Thumkeo D., Soliman N.A., Mane S.,
RA Lifton R.P., Shril S., Khokha M.K., Hoefele J., Goode B.L., Hildebrandt F.;
RT "DAAM2 variants cause nephrotic syndrome via actin dysregulation.";
RL Am. J. Hum. Genet. 107:1113-1128(2020).
CC -!- FUNCTION: Key regulator of the Wnt signaling pathway, which is required
CC for various processes during development, such as dorsal patterning,
CC determination of left/right symmetry or myelination in the central
CC nervous system. Acts downstream of Wnt ligands and upstream of beta-
CC catenin (CTNNB1). Required for canonical Wnt signaling pathway during
CC patterning in the dorsal spinal cord by promoting the aggregation of
CC Disheveled (Dvl) complexes, thereby clustering and formation of Wnt
CC receptor signalosomes and potentiating Wnt activity. During dorsal
CC patterning of the spinal cord, inhibits oligodendrocytes
CC differentiation via interaction with PIP5K1A. Also regulates non-
CC canonical Wnt signaling pathway. Acts downstream of PITX2 in the
CC developing gut and is required for left/right asymmetry within dorsal
CC mesentery: affects mesenchymal condensation by lengthening cadherin-
CC based junctions through WNT5A and non-canonical Wnt signaling, inducing
CC polarized condensation in the left dorsal mesentery necessary to
CC initiate gut rotation. Together with DAAM1, required for myocardial
CC maturation and sarcomere assembly. Is a regulator of actin nucleation
CC and elongation, filopodia formation and podocyte migration
CC (PubMed:33232676). {ECO:0000250|UniProtKB:Q80U19,
CC ECO:0000269|PubMed:33232676}.
CC -!- SUBUNIT: Interacts with DVL3. Interacts with INF2 (PubMed:33232676).
CC {ECO:0000250|UniProtKB:Q80U19, ECO:0000269|PubMed:33232676}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86T65-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86T65-4; Sequence=VSP_047360;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues examined. Expressed in
CC kidney glomeruli (PubMed:33232676). {ECO:0000269|PubMed:33232676,
CC ECO:0000269|PubMed:9205841}.
CC -!- DOMAIN: The DAD domain regulates activation via an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250|UniProtKB:O08808}.
CC -!- DISEASE: Nephrotic syndrome 24 (NPHS24) [MIM:619263]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS24 is an autosomal recessive, slowly progressive form. Most
CC patients eventually develop end-stage renal disease.
CC {ECO:0000269|PubMed:33232676}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20835.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002379; BAA20835.2; ALT_INIT; mRNA.
DR EMBL; AL833083; CAD89973.1; -; mRNA.
DR EMBL; AL136089; CAI20010.2; -; Genomic_DNA.
DR EMBL; FO393411; CAI20010.2; JOINED; Genomic_DNA.
DR EMBL; AL161439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03996.1; -; Genomic_DNA.
DR CCDS; CCDS54999.1; -. [Q86T65-4]
DR CCDS; CCDS56426.1; -. [Q86T65-3]
DR RefSeq; NP_001188356.1; NM_001201427.1. [Q86T65-3]
DR RefSeq; NP_056160.2; NM_015345.3. [Q86T65-4]
DR AlphaFoldDB; Q86T65; -.
DR SMR; Q86T65; -.
DR BioGRID; 117049; 27.
DR IntAct; Q86T65; 9.
DR STRING; 9606.ENSP00000381876; -.
DR iPTMnet; Q86T65; -.
DR PhosphoSitePlus; Q86T65; -.
DR BioMuta; DAAM2; -.
DR DMDM; 62906888; -.
DR EPD; Q86T65; -.
DR jPOST; Q86T65; -.
DR MassIVE; Q86T65; -.
DR MaxQB; Q86T65; -.
DR PaxDb; Q86T65; -.
DR PeptideAtlas; Q86T65; -.
DR PRIDE; Q86T65; -.
DR ProteomicsDB; 34135; -.
DR ProteomicsDB; 69664; -. [Q86T65-3]
DR Antibodypedia; 53613; 216 antibodies from 28 providers.
DR DNASU; 23500; -.
DR Ensembl; ENST00000274867.9; ENSP00000274867.4; ENSG00000146122.17. [Q86T65-3]
DR Ensembl; ENST00000398904.6; ENSP00000381876.2; ENSG00000146122.17. [Q86T65-3]
DR Ensembl; ENST00000538976.5; ENSP00000437808.1; ENSG00000146122.17. [Q86T65-4]
DR GeneID; 23500; -.
DR KEGG; hsa:23500; -.
DR MANE-Select; ENST00000274867.9; ENSP00000274867.4; NM_001201427.2; NP_001188356.1.
DR UCSC; uc003oow.4; human. [Q86T65-3]
DR CTD; 23500; -.
DR DisGeNET; 23500; -.
DR GeneCards; DAAM2; -.
DR HGNC; HGNC:18143; DAAM2.
DR HPA; ENSG00000146122; Group enriched (brain, choroid plexus).
DR MIM; 606627; gene.
DR MIM; 619263; phenotype.
DR neXtProt; NX_Q86T65; -.
DR OpenTargets; ENSG00000146122; -.
DR Orphanet; 567550; Idiopathic multidrug-resistant nephrotic syndrome.
DR PharmGKB; PA27130; -.
DR VEuPathDB; HostDB:ENSG00000146122; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000157801; -.
DR HOGENOM; CLU_002356_1_0_1; -.
DR InParanoid; Q86T65; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q86T65; -.
DR TreeFam; TF314602; -.
DR PathwayCommons; Q86T65; -.
DR SignaLink; Q86T65; -.
DR BioGRID-ORCS; 23500; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; DAAM2; human.
DR GenomeRNAi; 23500; -.
DR Pharos; Q86T65; Tbio.
DR PRO; PR:Q86T65; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q86T65; protein.
DR Bgee; ENSG00000146122; Expressed in corpus callosum and 188 other tissues.
DR ExpressionAtlas; Q86T65; baseline and differential.
DR Genevisible; Q86T65; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0021516; P:dorsal spinal cord development; ISS:UniProtKB.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0090521; P:podocyte cell migration; IDA:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:2000050; P:regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Disease variant; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..1068
FT /note="Disheveled-associated activator of morphogenesis 2"
FT /id="PRO_0000194909"
FT DOMAIN 40..416
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 518..594
FT /note="FH1"
FT DOMAIN 595..994
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1016..1048
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 514..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..516
FT /evidence="ECO:0000255"
FT COMPBIAS 538..580
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 894
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_047360"
FT VARIANT 105
FT /note="R -> H (in dbSNP:rs6919807)"
FT /id="VAR_055805"
FT VARIANT 121
FT /note="E -> Q (in NPHS24; unknown pathological
FT significance; affects the regulation of filopodia
FT formation)"
FT /evidence="ECO:0000269|PubMed:33232676"
FT /id="VAR_085585"
FT VARIANT 335
FT /note="R -> Q (in NPHS24; unknown pathological
FT significance; affects the regulation of filopodia
FT formation)"
FT /evidence="ECO:0000269|PubMed:33232676"
FT /id="VAR_085586"
FT VARIANT 445..1068
FT /note="Missing (in NPHS24; affects the regulation of
FT filopodia formation)"
FT /evidence="ECO:0000269|PubMed:33232676"
FT /id="VAR_085587"
FT VARIANT 582
FT /note="P -> H (in NPHS24; unknown pathological
FT significance; affects the regulation of filopodia
FT formation)"
FT /evidence="ECO:0000269|PubMed:33232676"
FT /id="VAR_085588"
FT VARIANT 617
FT /note="R -> H (in dbSNP:rs34699846)"
FT /id="VAR_055806"
FT VARIANT 1028
FT /note="S -> L (in NPHS24; unknown pathological
FT significance; affects the regulation of filopodia
FT formation)"
FT /evidence="ECO:0000269|PubMed:33232676"
FT /id="VAR_085589"
FT CONFLICT 414
FT /note="R -> W (in Ref. 3; CAD89973)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="Q -> R (in Ref. 3; CAD89973)"
FT /evidence="ECO:0000305"
FT CONFLICT 1003
FT /note="R -> W (in Ref. 3; CAD89973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1068 AA; 123499 MW; 90B071DD1BC13F9A CRC64;
MAPRKRSHHG LGFLCCFGGS DIPEINLRDN HPLQFMEFSS PIPNAEELNI RFAELVDELD
LTDKNREAMF ALPPEKKWQI YCSKKKEQED PNKLATSWPD YYIDRINSMA AMQSLYAFDE
EETEMRNQVV EDLKTALRTQ PMRFVTRFIE LEGLTCLLNF LRSMDHATCE SRIHTSLIGC
IKALMNNSQG RAHVLAQPEA ISTIAQSLRT ENSKTKVAVL EILGAVCLVP GGHKKVLQAM
LHYQVYAAER TRFQTLLNEL DRSLGRYRDE VNLKTAIMSF INAVLNAGAG EDNLEFRLHL
RYEFLMLGIQ PVIDKLRQHE NAILDKHLDF FEMVRNEDDL ELARRFDMVH IDTKSASQMF
ELIHKKLKYT EAYPCLLSVL HHCLQMPYKR NGGYFQQWQL LDRILQQIVL QDERGVDPDL
APLENFNVKN IVNMLINENE VKQWRDQAEK FRKEHMELVS RLERKERECE TKTLEKEEMM
RTLNKMKDKL ARESQELRQA RGQVAELVAQ LSELSTGPVS SPPPPGGPLT LSSSMTTNDL
PPPPPPLPFA CCPPPPPPPL PPGGPPTPPG APPCLGMGLP LPQDPYPSSD VPLRKKRVPQ
PSHPLKSFNW VKLNEERVPG TVWNEIDDMQ VFRILDLEDF EKMFSAYQRH QKELGSTEDI
YLASRKVKEL SVIDGRRAQN CIILLSKLKL SNEEIRQAIL KMDEQEDLAK DMLEQLLKFI
PEKSDIDLLE EHKHEIERMA RADRFLYEMS RIDHYQQRLQ ALFFKKKFQE RLAEAKPKVE
AILLASRELV RSKRLRQMLE VILAIGNFMN KGQRGGAYGF RVASLNKIAD TKSSIDRNIS
LLHYLIMILE KHFPDILNMP SELQHLPEAA KVNLAELEKE VGNLRRGLRA VEVELEYQRR
QVREPSDKFV PVMSDFITVS SFSFSELEDQ LNEARDKFAK ALMHFGEHDS KMQPDEFFGI
FDTFLQAFSE ARQDLEAMRR RKEEEERRAR MEAMLKEQRE RERWQRQRKV LAAGSSLEEG
GEFDDLVSAL RSGEVFDKDL CKLKRSRKRS GSQALEVTRE RAINRLNY
