BRSK1_RAT
ID BRSK1_RAT Reviewed; 778 AA.
AC B2DD29; F1M6Y8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Serine/threonine-protein kinase BRSK1;
DE EC=2.7.11.1;
DE EC=2.7.11.26;
DE AltName: Full=Brain-specific serine/threonine-protein kinase 1;
DE Short=BR serine/threonine-protein kinase 1;
DE AltName: Full=Serine/threonine-protein kinase SAD-B {ECO:0000303|PubMed:16630837};
GN Name=Brsk1; Synonyms=Sadb {ECO:0000303|PubMed:16630837};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT THR-189.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=18324781; DOI=10.1021/bi702528r;
RA Fujimoto T., Yurimoto S., Hatano N., Nozaki N., Sueyoshi N., Kameshita I.,
RA Mizutani A., Mikoshiba K., Kobayashi R., Tokumitsu H.;
RT "Activation of SAD kinase by Ca2+/calmodulin-dependent protein kinase
RT kinase.";
RL Biochemistry 47:4151-4159(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF LYS-63; THR-189 AND SER-193.
RX PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
RA Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M.,
RA Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I., Setou M.,
RA Ohtsuka T., Takai Y.;
RT "SAD: a presynaptic kinase associated with synaptic vesicles and the active
RT zone cytomatrix that regulates neurotransmitter release.";
RL Neuron 50:261-275(2006).
RN [4]
RP REGULATION OF TRANSLATION.
RX PubMed=18794346; DOI=10.1101/gad.1685008;
RA Choi Y.J., Di Nardo A., Kramvis I., Meikle L., Kwiatkowski D.J., Sahin M.,
RA He X.;
RT "Tuberous sclerosis complex proteins control axon formation.";
RL Genes Dev. 22:2485-2495(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; SER-450; SER-508;
RP THR-583; SER-586; SER-587 AND SER-601, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a key role in
CC polarization of neurons and centrosome duplication. Phosphorylates
CC CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following
CC phosphorylation and activation by STK11/LKB1, acts as a key regulator
CC of polarization of cortical neurons, probably by mediating
CC phosphorylation of microtubule-associated proteins such as MAPT/TAU at
CC 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by
CC mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons,
CC leading to down-regulate WEE1 activity in polarized neurons. Also acts
CC as a positive regulator of centrosome duplication by mediating
CC phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131',
CC leading to translocation of gamma-tubulin and its associated proteins
CC to the centrosome. Involved in the UV-induced DNA damage checkpoint
CC response, probably by inhibiting CDK1 activity through phosphorylation
CC and activation of WEE1, and inhibition of CDC25B and CDC25C (By
CC similarity). In neurons, localizes to synaptic vesicles and plays a
CC role in neurotransmitter release, possibly by phosphorylating RIMS1.
CC {ECO:0000250, ECO:0000269|PubMed:16630837}.
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 -!- 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;
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; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-189 by
CC STK11/LKB1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Synapse {ECO:0000269|PubMed:16630837}. Presynaptic
CC active zone {ECO:0000269|PubMed:16630837}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:16630837}.
CC Note=Nuclear in the absence of DNA damage. Translocated to the nucleus
CC in response to UV- or MMS-induced DNA damage (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly present in brain. Present in presynaptic
CC nerve terminals (at protein level). {ECO:0000269|PubMed:16630837}.
CC -!- PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. Not
CC phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated
CC and activated by CaMKK1. May be inactivated via dephosphorylation of
CC Thr-189 by PP2C. May be autophosphorylated.
CC {ECO:0000269|PubMed:18324781}.
CC -!- MISCELLANEOUS: Protein synthesis is inhibited by the TSC1-TSC2 complex
CC acting through TORC1 in neurons, leading to regulate neuron
CC polarization. {ECO:0000305|PubMed:18794346}.
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; AB365521; BAG28183.1; -; mRNA.
DR RefSeq; NP_001120809.1; NM_001127337.1.
DR AlphaFoldDB; B2DD29; -.
DR SMR; B2DD29; -.
DR BioGRID; 270382; 2.
DR IntAct; B2DD29; 1.
DR STRING; 10116.ENSRNOP00000033679; -.
DR iPTMnet; B2DD29; -.
DR PhosphoSitePlus; B2DD29; -.
DR PaxDb; B2DD29; -.
DR PRIDE; B2DD29; -.
DR Ensembl; ENSRNOT00000097053; ENSRNOP00000087514; ENSRNOG00000017673.
DR GeneID; 499073; -.
DR KEGG; rno:499073; -.
DR UCSC; RGD:1563268; rat.
DR CTD; 84446; -.
DR RGD; 1563268; Brsk1.
DR eggNOG; KOG0588; Eukaryota.
DR GeneTree; ENSGT00940000161254; -.
DR HOGENOM; CLU_000288_156_2_1; -.
DR InParanoid; B2DD29; -.
DR OMA; LFALLVX; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; B2DD29; -.
DR PRO; PR:B2DD29; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017673; Expressed in frontal cortex and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0150034; C:distal axon; IMP:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; ISO:RGD.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0009411; P:response to UV; ISO:RGD.
DR GO; GO:0099504; P:synaptic vesicle cycle; ISO:RGD.
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 InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 cycle; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; DNA damage; Kinase; Magnesium; Metal-binding; Methylation;
KW Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..778
FT /note="Serine/threonine-protein kinase BRSK1"
FT /id="PRO_0000412649"
FT DOMAIN 34..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 314..356
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 189
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000269|PubMed:18324781"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 466
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 484
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 498
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 525
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 550
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5RJI5"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 63
FT /note="K->R: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:16630837"
FT MUTAGEN 189
FT /note="T->A: Decreased autophosphorylation; when associated
FT with A-193."
FT /evidence="ECO:0000269|PubMed:16630837"
FT MUTAGEN 193
FT /note="S->A: Decreased autophosphorylation; when associated
FT with A-189."
FT /evidence="ECO:0000269|PubMed:16630837"
SQ SEQUENCE 778 AA; 85183 MW; A4F1E7E107359BDD CRC64;
MSSGSKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
AVKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGS GGSPVPTRRA
LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG VGDEARGGGS PTSKTQTLPS
RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
VRFQVDISSS EGPEPSPRRD GSSGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
SVQALADEKN GAQTRPAGTP PRSLQPPPGR PDPDLSSSPR RGPSKDKKLL ATNGTPLP
