MARK1_MOUSE
ID MARK1_MOUSE Reviewed; 795 AA.
AC Q8VHJ5; E9QL17; Q69ZI7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase MARK1;
DE EC=2.7.11.1;
DE EC=2.7.11.26;
DE AltName: Full=ELKL motif serine/threonine-protein kinase 3;
DE AltName: Full=MAP/microtubule affinity-regulating kinase 1;
DE AltName: Full=PAR1 homolog c;
DE Short=Par-1c;
DE Short=mPar-1c;
GN Name=Mark1 {ECO:0000312|MGI:MGI:2664902};
GN Synonyms=Emk3 {ECO:0000312|EMBL:AAL50826.1}, Kiaa1477;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL50826.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Darmon Y.M., Le Morvan V.;
RT "Mus musculus Emk3/Mark1 mRNA.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-795.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-666, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382; SER-390; SER-393;
RP SER-403; SER-423 AND SER-475, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in
CC cell polarity and microtubule dynamics regulation. Phosphorylates DCX,
CC MAP2 and MAP4. Phosphorylates the microtubule-associated protein
CC MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating
CC the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS
CC motifs, causing detachment from microtubules, and their disassembly.
CC Involved in the regulation of neuronal migration through its dual
CC activities in regulating cellular polarity and microtubule dynamics,
CC possibly by phosphorylating and regulating DCX. Also acts as a positive
CC regulator of the Wnt signaling pathway, probably by mediating
CC phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3).
CC {ECO:0000250|UniProtKB:Q9P0L2}.
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:0000250|UniProtKB:Q9POL2};
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:0000250|UniProtKB:Q9POL2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9POL2};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylation at Ser-219. Activated
CC by phosphorylation on Thr-215 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAPT/TAU. {ECO:0000250|UniProtKB:Q9P0L2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9P0L2}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9P0L2}. Note=Appears to localize to an
CC intracellular network. {ECO:0000250}.
CC -!- DOMAIN: The UBA domain does not seem to bind ubiquitin and ubiquitin-
CC like and might play a role in regulating the enzyme conformation and
CC localization. Activation of the kinase activity following
CC phosphorylation at Thr-208 is accompanied by a conformational change
CC that alters the orientation of the UBA domain with respect to the
CC catalytic domain (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The KA1 domain mediates binding to phospholipids and targeting
CC to membranes. Binds phosphatidic acid (PA), phosphatidylserine (PtdSer)
CC and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated at Thr-215 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation
CC at Thr-215 by TAOK1 activates the kinase activity, leading to
CC phosphorylation and detachment of MAPT/TAU from microtubules.
CC Phosphorylation at Ser-219 by GSK3-beta (GSK3B) inhibits the kinase
CC activity. Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized
CC epithelial cells inhibits the kinase activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AF453686; AAL50826.1; -; mRNA.
DR EMBL; AC117826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173181; BAD32459.1; -; mRNA.
DR CCDS; CCDS35817.1; -.
DR RefSeq; NP_663490.2; NM_145515.2.
DR AlphaFoldDB; Q8VHJ5; -.
DR SMR; Q8VHJ5; -.
DR BioGRID; 230554; 9.
DR IntAct; Q8VHJ5; 3.
DR MINT; Q8VHJ5; -.
DR STRING; 10090.ENSMUSP00000027929; -.
DR iPTMnet; Q8VHJ5; -.
DR PhosphoSitePlus; Q8VHJ5; -.
DR jPOST; Q8VHJ5; -.
DR MaxQB; Q8VHJ5; -.
DR PaxDb; Q8VHJ5; -.
DR PRIDE; Q8VHJ5; -.
DR ProteomicsDB; 292170; -.
DR Antibodypedia; 2072; 458 antibodies from 32 providers.
DR DNASU; 226778; -.
DR Ensembl; ENSMUST00000027929; ENSMUSP00000027929; ENSMUSG00000026620.
DR GeneID; 226778; -.
DR KEGG; mmu:226778; -.
DR UCSC; uc007dyt.2; mouse.
DR CTD; 4139; -.
DR MGI; MGI:2664902; Mark1.
DR VEuPathDB; HostDB:ENSMUSG00000026620; -.
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000157560; -.
DR HOGENOM; CLU_000288_157_5_1; -.
DR InParanoid; Q8VHJ5; -.
DR OMA; DWVIFED; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q8VHJ5; -.
DR TreeFam; TF315213; -.
DR BioGRID-ORCS; 226778; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q8VHJ5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VHJ5; protein.
DR Bgee; ENSMUSG00000026620; Expressed in trigeminal ganglion and 235 other tissues.
DR ExpressionAtlas; Q8VHJ5; baseline and differential.
DR Genevisible; Q8VHJ5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IMP:ARUK-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:ARUK-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:ARUK-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033627; MARK1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346:SF21; PTHR24346:SF21; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Kinase; Lipid-binding; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..795
FT /note="Serine/threonine-protein kinase MARK1"
FT /id="PRO_0000086299"
FT DOMAIN 60..311
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 329..370
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 746..795
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H0K1,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H0K1,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O08678,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L2"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L2"
FT MOD_RES 215
FT /note="Phosphothreonine; by LKB1 and TAOK1"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L2"
FT MOD_RES 219
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:O08678"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08678"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L2"
FT MOD_RES 613
FT /note="Phosphothreonine; by PKC/PRKCZ"
FT /evidence="ECO:0000250"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CONFLICT 32
FT /note="A -> T (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="L -> I (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="I -> T (in Ref. 3; BAD32459)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="I -> V (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> D (in Ref. 3; BAD32459)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="S -> N (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> N (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="G -> D (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="G -> GS (in Ref. 3; BAD32459)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="P -> R (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="F -> L (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="A -> T (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="D -> E (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="D -> E (in Ref. 1; AAL50826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 88335 MW; F43F2B541C346697 CRC64;
MSARTPLPTV NERDTENHTS VDGYTETHIP PAKSSSRQNL PRCRNSITSA TDEQPHIGNY
RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS LQKLFREVRI MKILNHPNIV
KLFEVIETEK TLYLVMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYCHQKCIVH
RDLKAENLLL DADMNIKIAD FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV
WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG
SLEQIMKDRW MNVGHEEEEL KPYSEPELDL SDAKRIDIMV TMGFARDEIN DALVSQKYDE
VMATYILLGR KPPEFEGGES LSSGSLCQRS RPSSDLNNST LQSPAHLKVQ RSISANQKQR
RFSDHAGPSI PPAVSYTKRP QANSVESEQK EEWGKDTARR LGSTTVGSKS EVTASPLVGP
DRKKSTASPS NNVYSGGSMA RRNTYVCERS TDRYAALQNG RDSSLTEMSA SSMSSAGSTV
ASAGPSARPR HQKSMSTSGH PIKVTLPTIK DGSEAYRPGA AQRVPAASPS AHSISASTPD
RTRFPRGSSS RSTFHGEQLR ERRSAAYNGP PASPSHETGA FAHARRGTST GIISKITSKF
VRRDPSEGEA SGRADTARGS SGDPKERDKD EGKEAKPRSL RFTWSMKTTS SMDPNDMLRE
IRKVLDANTC DYEQKERFLL FCVHGDARQD SLVQWEMEVC KLPRLSLNGV RFKRISGTSI
AFKNIASKIA NELKL
