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 27-MAR-2024, entry version 171. 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}. 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; 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; 10. DR IntAct; Q8VHJ5; 3. DR MINT; Q8VHJ5; -. DR STRING; 10090.ENSMUSP00000027929; -. DR GlyGen; Q8VHJ5; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; Q8VHJ5; -. DR PhosphoSitePlus; Q8VHJ5; -. DR jPOST; Q8VHJ5; -. DR MaxQB; Q8VHJ5; -. DR PaxDb; 10090-ENSMUSP00000027929; -. DR ProteomicsDB; 292170; -. DR Pumba; Q8VHJ5; -. DR Antibodypedia; 2072; 508 antibodies from 33 providers. DR DNASU; 226778; -. DR Ensembl; ENSMUST00000027929.10; ENSMUSP00000027929.5; ENSMUSG00000026620.12. DR GeneID; 226778; -. DR KEGG; mmu:226778; -. DR UCSC; uc007dyt.2; mouse. DR AGR; MGI:2664902; -. 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; YDEVMAC; -. DR OrthoDB; 5475340at2759; -. DR PhylomeDB; Q8VHJ5; -. DR TreeFam; TF315213; -. DR BioGRID-ORCS; 226778; 2 hits in 81 CRISPR screens. DR PRO; PR:Q8VHJ5; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; Q8VHJ5; Protein. DR Bgee; ENSMUSG00000026620; Expressed in trigeminal ganglion and 237 other cell types or tissues. DR ExpressionAtlas; Q8VHJ5; baseline and differential. 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; IBA:GO_Central. 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 CDD; cd12196; MARK1-3_C; 1. DR CDD; cd14072; STKc_MARK; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR001772; KA1_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR049508; MARK1-4_cat. 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; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF21; SERINE_THREONINE-PROTEIN KINASE MARK1; 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; KA1-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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. DR Genevisible; Q8VHJ5; MM. 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 //