MRCKB_RAT
ID MRCKB_RAT Reviewed; 1713 AA.
AC Q7TT49; O54875;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase MRCK beta;
DE EC=2.7.11.1;
DE AltName: Full=CDC42-binding protein kinase beta;
DE AltName: Full=DMPK-like beta;
DE AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase beta;
DE Short=MRCK beta;
DE Short=Myotonic dystrophy protein kinase-like beta;
GN Name=Cdc42bpb {ECO:0000312|EMBL:AAP34403.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC02942.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:AAC02942.1};
RX PubMed=9418861; DOI=10.1128/mcb.18.1.130;
RA Leung T., Chen X.-Q., Tan I., Manser E., Lim L.;
RT "Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42
RT effector in promoting cytoskeletal reorganization.";
RL Mol. Cell. Biol. 18:130-140(1998).
RN [2] {ECO:0000312|EMBL:AAP34403.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.Q., Wu S.L., Cheng Z.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND INTERACTION WITH LURAP1 AND MYO18A.
RX PubMed=18854160; DOI=10.1016/j.cell.2008.09.018;
RA Tan I., Yong J., Dong J.M., Lim L., Leung T.;
RT "A tripartite complex containing MRCK modulates lamellar actomyosin
RT retrograde flow.";
RL Cell 135:123-136(2008).
RN [4]
RP FUNCTION, INTERACTION WITH TJP1, MUTAGENESIS OF PHE-952; TYR-954; LEU-964
RP AND PHE-966, AND SUBCELLULAR LOCATION.
RX PubMed=21240187; DOI=10.1038/emboj.2010.353;
RA Huo L., Wen W., Wang R., Kam C., Xia J., Feng W., Zhang M.;
RT "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge
RT controls cell migration.";
RL EMBO J. 30:665-678(2011).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF PPP1R12A AND MYL9/MLC2, AND ACTIVITY
RP REGULATION.
RX PubMed=21457715; DOI=10.1016/j.febslet.2011.03.054;
RA Tan I., Lai J., Yong J., Li S.F., Leung T.;
RT "Chelerythrine perturbs lamellar actomyosin filaments by selective
RT inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.";
RL FEBS Lett. 585:1260-1268(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1688; SER-1692 AND SER-1695,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP INTERACTION WITH FAM89B AND LURAP1.
RC TISSUE=Brain;
RX PubMed=25107909; DOI=10.1074/jbc.m114.588079;
RA Lee I.C., Leung T., Tan I.;
RT "Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-
RT binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin
RT dynamics.";
RL J. Biol. Chem. 289:26989-27003(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase which is an important
CC downstream effector of CDC42 and plays a role in the regulation of
CC cytoskeleton reorganization and cell migration. Regulates actin
CC cytoskeletal reorganization via phosphorylation of PPP1R12C and
CC MYL9/MLC2 (PubMed:21240187, PubMed:21457715). In concert with MYO18A
CC and LURAP1, is involved in modulating lamellar actomyosin retrograde
CC flow that is crucial to cell protrusion and migration. Phosphorylates
CC PPP1R12A (PubMed:18854160). In concert with FAM89B/LRAP25 mediates the
CC targeting of LIMK1 to the lamellipodium resulting in its activation and
CC subsequent phosphorylation of CFL1 which is important for lamellipodial
CC F-actin regulation (By similarity). {ECO:0000250|UniProtKB:Q7TT50,
CC ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21240187,
CC ECO:0000269|PubMed:21457715}.
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:Q5VT25};
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:Q5VT25};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q5VT25};
CC -!- ACTIVITY REGULATION: Maintained in an inactive, closed conformation by
CC an interaction between the kinase domain and the negative
CC autoregulatory C-terminal coiled-coil region. Agonist binding to the
CC phorbol ester binding site disrupts this, releasing the kinase domain
CC to allow N-terminus-mediated dimerization and kinase activation by
CC transautophosphorylation (By similarity). Inhibited by chelerythrine
CC chloride. {ECO:0000250, ECO:0000269|PubMed:21457715}.
CC -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC Interacts tightly with GTP-bound but not GDP-bound CDC42 (By
CC similarity). Interacts with TJP1; this interaction requires the
CC presence of catalytically active CDC42 (PubMed:21240187). Forms a
CC tripartite complex with MYO18A and LURAP1 with the latter acting as an
CC adapter connecting CDC42BPB and MYO18A. LURAP1 binding results in
CC activation of CDC42BPB by abolition of its negative autoregulation
CC (PubMed:18854160). Interacts with STRIP1, STRN3 and SIKE1 (By
CC similarity). Interacts with CPNE4 (via VWFA domain) (By similarity).
CC Interacts with LURAP1 (PubMed:25107909). Interacts (via AGC-kinase C-
CC terminal domain) with FAM89B/LRAP25 (via LRR repeat) (PubMed:25107909).
CC Forms a tripartite complex with FAM89B/LRAP25 and LIMK1 (By
CC similarity). {ECO:0000250|UniProtKB:Q7TT50,
CC ECO:0000250|UniProtKB:Q9Y5S2, ECO:0000269|PubMed:18854160,
CC ECO:0000269|PubMed:21240187, ECO:0000269|PubMed:25107909}.
CC -!- INTERACTION:
CC Q7TT49; D4A8G3: Lurap1; NbExp=4; IntAct=EBI-692673, EBI-2015467;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:21240187}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21240187}; Cytoplasmic side
CC {ECO:0000269|PubMed:21240187}. Cell junction
CC {ECO:0000269|PubMed:21240187}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q3UU96}. Note=Displays a dispersed punctate
CC distribution and concentrates along the cell periphery, especially at
CC the leading edge and cell-cell junction. This concentration is PH-
CC domain dependent (By similarity). Detected at the leading edge of
CC migrating and wounded cells; this localization requires the presence of
CC catalytically active CDC42 (PubMed:21240187). Localizes in the
CC lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:O54874, ECO:0000250|UniProtKB:Q3UU96,
CC ECO:0000269|PubMed:21240187}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC levels in lung and kidney. {ECO:0000269|PubMed:9418861}.
CC -!- PTM: Proteolytically cleaved by caspases upon apoptosis induction.
CC {ECO:0000250|UniProtKB:Q9Y5S2}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02942.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF021936; AAC02942.1; ALT_FRAME; mRNA.
DR EMBL; AY277590; AAP34403.1; -; mRNA.
DR PIR; T14050; T14050.
DR RefSeq; NP_446072.2; NM_053620.3.
DR AlphaFoldDB; Q7TT49; -.
DR SMR; Q7TT49; -.
DR IntAct; Q7TT49; 16.
DR MINT; Q7TT49; -.
DR STRING; 10116.ENSRNOP00000036487; -.
DR iPTMnet; Q7TT49; -.
DR PhosphoSitePlus; Q7TT49; -.
DR jPOST; Q7TT49; -.
DR PaxDb; Q7TT49; -.
DR PRIDE; Q7TT49; -.
DR Ensembl; ENSRNOT00000039059; ENSRNOP00000036487; ENSRNOG00000009675.
DR GeneID; 113960; -.
DR KEGG; rno:113960; -.
DR UCSC; RGD:621753; rat.
DR CTD; 9578; -.
DR RGD; 621753; Cdc42bpb.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR InParanoid; Q7TT49; -.
DR OMA; CGRSHHV; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q7TT49; -.
DR TreeFam; TF313551; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR PRO; PR:Q7TT49; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000009675; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q7TT49; baseline and differential.
DR Genevisible; Q7TT49; RN.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR CDD; cd00029; C1; 1.
DR CDD; cd05624; STKc_MRCK_beta; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033232; MRCK_beta.
DR InterPro; IPR042718; MRCKB_STKc.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988:SF34; PTHR22988:SF34; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1713
FT /note="Serine/threonine-protein kinase MRCK beta"
FT /id="PRO_0000086396"
FT DOMAIN 76..342
FT /note="Protein kinase"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 343..413
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1096..1215
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1241..1515
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT DOMAIN 1585..1598
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT ZN_FING 1026..1076
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..649
FT /evidence="ECO:0000255"
FT COILED 681..815
FT /evidence="ECO:0000255"
FT COILED 882..939
FT /evidence="ECO:0000255"
FT COMPBIAS 461..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P54265,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P54265,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q5VT25,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 221
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 233
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 671
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT50"
FT MOD_RES 954
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7TT50"
FT MOD_RES 1682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 1684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5S2"
FT MOD_RES 1688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 952
FT /note="F->Q: Abolishes interaction with TJP1; when
FT associated with Q-954."
FT /evidence="ECO:0000269|PubMed:21240187"
FT MUTAGEN 954
FT /note="Y->Q: Abolishes interaction with TJP1; when
FT associated with Q-952."
FT /evidence="ECO:0000269|PubMed:21240187"
FT MUTAGEN 964
FT /note="L->Q: Abolishes interaction with TJP1; when
FT associated with Q-966."
FT /evidence="ECO:0000269|PubMed:21240187"
FT MUTAGEN 966
FT /note="F->Q: Abolishes interaction with TJP1; when
FT associated with Q-964."
FT /evidence="ECO:0000269|PubMed:21240187"
FT CONFLICT 706
FT /note="A -> R (in Ref. 1; AAC02942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="R -> C (in Ref. 1; AAC02942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1713 AA; 194888 MW; 80C999262C96DAA6 CRC64;
MSAKVRLKKL EQLLLDGPWR NESSLSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC
FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY
IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP
DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD
VSSPSDTSNF DVDDDVLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMIQ
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD
KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS ESFSKQMERE
LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
ESESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGAMKD KYERERAMLF DENKKLTAEN
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV
KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP IFEYFNTAPL
AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA RSQQRPSTVP LPNTQALAMA
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP
GVIASQVLDL RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV DGDRIAVGLE
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR NHHVHLYPWT SFDGAEASNF
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW
MAMFKDRLCV GYPSGFSLLS IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL
LCFSHMGLYV DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML RTRSKRRFVF
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTAQEE
KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
PSNSSNPSGP PSPNSPHRSQ LPLEGLDQPA CDA
