PKN1_RAT
ID PKN1_RAT Reviewed; 946 AA.
AC Q63433; Q6P748; Q8VIJ2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Serine/threonine-protein kinase N1;
DE EC=2.7.11.13 {ECO:0000269|PubMed:8051089};
DE AltName: Full=Protease-activated kinase 1;
DE Short=PAK-1;
DE AltName: Full=Protein kinase C-like 1;
DE AltName: Full=Protein kinase C-like PKN;
DE AltName: Full=Protein-kinase C-related kinase 1;
DE AltName: Full=Serine-threonine protein kinase N;
GN Name=Pkn1; Synonyms=Pkn, Prk1, Prkcl1;
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].
RC TISSUE=Lung;
RX PubMed=8135837; DOI=10.1006/bbrc.1994.1313;
RA Mukai H., Ono Y.;
RT "A novel protein kinase with leucine zipper-like sequences: its catalytic
RT domain is highly homologous to that of protein kinase C.";
RL Biochem. Biophys. Res. Commun. 199:897-904(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8943281; DOI=10.1074/jbc.271.50.32233;
RA Peng B., Morrice N.A., Groenen L.C., Wettenhall R.E.;
RT "Phosphorylation events associated with different states of activation of a
RT hepatic cardiolipin/protease-activated protein kinase. Structural identity
RT to the protein kinase N-type protein kinases.";
RL J. Biol. Chem. 271:32233-32240(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 633-648; 747-767; 776-822; 880-889 AND 938-946,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=8051089; DOI=10.1016/s0021-9258(17)32124-5;
RA Morrice N.A., Gabrielli B., Kemp B.E., Wettenhall R.E.;
RT "A cardiolipin-activated protein kinase from rat liver structurally
RT distinct from the protein kinases C.";
RL J. Biol. Chem. 269:20040-20046(1994).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-377.
RX PubMed=15375078; DOI=10.1096/fj.04-1876fje;
RA Zhu Y., Stolz D.B., Guo F., Ross M.A., Watkins S.C., Tan B.J., Qi R.Z.,
RA Manser E., Li Q.T., Bay B.H., Teo T.S., Duan W.;
RT "Signaling via a novel integral plasma membrane pool of a serine/threonine
RT protein kinase PRK1 in mammalian cells.";
RL FASEB J. 18:1722-1724(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC various processes such as regulation of the intermediate filaments of
CC the actin cytoskeleton, cell migration, tumor cell invasion and
CC transcription regulation (PubMed:8051089, PubMed:15375078). Part of a
CC signaling cascade that begins with the activation of the adrenergic
CC receptor ADRA1B and leads to the activation of MAPK14 (By similarity).
CC Regulates the cytoskeletal network by phosphorylating proteins such as
CC VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit
CC their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669'
CC of MAPT/Tau, lowering its ability to bind to microtubules, resulting in
CC disruption of tubulin assembly. Acts as a key coactivator of androgen
CC receptor (ANDR)-dependent transcription, by being recruited to ANDR
CC target genes and specifically mediating phosphorylation of 'Thr-11' of
CC histone H3 (H3T11ph), a specific tag for epigenetic transcriptional
CC activation that promotes demethylation of histone H3 'Lys-9' (H3K9me)
CC by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to
CC impair their import in the nucleus. Phosphorylates 'Thr-38' of
CC PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able
CC to phosphorylate RPS6 in vitro (By similarity).
CC {ECO:0000250|UniProtKB:Q16512, ECO:0000269|PubMed:15375078,
CC ECO:0000269|PubMed:8051089}.
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=2.7.11.13;
CC Evidence={ECO:0000269|PubMed:8051089};
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=2.7.11.13; Evidence={ECO:0000269|PubMed:8051089};
CC -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to Rho
CC proteins (RHOA, RHOB and RAC1). Activated by lipids, particularly
CC cardiolipin and to a lesser extent by other acidic phospholipids.
CC Activated by caspase-3 (CASP3) cleavage during apoptosis. Two specific
CC sites, Thr-778 (activation loop of the kinase domain) and Ser-920 (turn
CC motif), need to be phosphorylated for its full activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ZFAND6 (By similarity). Interacts with ANDR.
CC Interacts with PRKCB. Interacts (via REM 1 and REM 2 repeats) with
CC RAC1. Interacts (via REM 1 repeat) with RHOA. Interacts with RHOB.
CC Interacts (via C-terminus) with PDPK1. Interacts with CCNT2; enhances
CC MYOD1-dependent transcription. Component of a signaling complex
CC containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this
CC complex, AKAP13 interacts directly with PKN1, which in turn recruits
CC MAPK14, MAP2K3 and ZAK (By similarity). {ECO:0000250|UniProtKB:P70268,
CC ECO:0000250|UniProtKB:Q16512}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15375078}. Nucleus
CC {ECO:0000250|UniProtKB:Q16512}. Endosome
CC {ECO:0000250|UniProtKB:Q16512}. Cell membrane
CC {ECO:0000269|PubMed:15375078}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15375078}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q16512}. Midbody {ECO:0000250|UniProtKB:Q16512}.
CC Note=Associates with chromatin in a ligand-dependent manner (By
CC similarity). Localization to endosomes is mediated via its interaction
CC with RHOB. Accumulates during telophase at the cleavage furrow and
CC finally concentrates around the midbody in cytokinesis (By similarity).
CC Association to the cell membrane is dependent on Ser-377
CC phosphorylation. {ECO:0000250|UniProtKB:Q16512,
CC ECO:0000269|PubMed:15375078}.
CC -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated; preferably on serine. Phosphorylated during
CC mitosis. {ECO:0000250|UniProtKB:Q16512}.
CC -!- PTM: Activated by limited proteolysis with trypsin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; D26180; BAA05168.1; -; mRNA.
DR EMBL; L35634; AAL31374.1; -; mRNA.
DR EMBL; BC061836; AAH61836.1; -; mRNA.
DR PIR; JC2130; JC2130.
DR RefSeq; NP_058871.2; NM_017175.2.
DR AlphaFoldDB; Q63433; -.
DR SMR; Q63433; -.
DR BioGRID; 248010; 1.
DR DIP; DIP-60097N; -.
DR IntAct; Q63433; 9.
DR STRING; 10116.ENSRNOP00000005770; -.
DR iPTMnet; Q63433; -.
DR PhosphoSitePlus; Q63433; -.
DR jPOST; Q63433; -.
DR PaxDb; Q63433; -.
DR PRIDE; Q63433; -.
DR Ensembl; ENSRNOT00000005770; ENSRNOP00000005770; ENSRNOG00000004131.
DR GeneID; 29355; -.
DR KEGG; rno:29355; -.
DR CTD; 5585; -.
DR RGD; 69308; Pkn1.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154990; -.
DR HOGENOM; CLU_000288_132_1_1; -.
DR InParanoid; Q63433; -.
DR OMA; CTELRIE; -.
DR OrthoDB; 520651at2759; -.
DR BRENDA; 2.7.11.13; 5301.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q63433; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000004131; Expressed in spleen and 19 other tissues.
DR Genevisible; Q63433; RN.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR GO; GO:0035402; F:histone kinase activity (H3-T11 specific); ISS:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
DR GO; GO:0004697; F:protein kinase C activity; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
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:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0001783; P:B cell apoptotic process; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0035407; P:histone H3-T11 phosphorylation; ISO:RGD.
DR GO; GO:0006972; P:hyperosmotic response; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0002634; P:regulation of germinal center formation; ISO:RGD.
DR GO; GO:0002637; P:regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0003014; P:renal system process; ISO:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11630; HR1_PKN1_2; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037317; PKN1_HR1_2.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Chromatin regulator; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Endosome; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT CHAIN 2..946
FT /note="Serine/threonine-protein kinase N1"
FT /id="PRO_0000055721"
FT DOMAIN 25..100
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 114..193
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 202..283
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 310..473
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 619..878
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 879..946
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 345..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 744
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 625..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 108..109
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 457..458
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT SITE 561..562
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15375078"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 778
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 918
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16512"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 298
FT /note="A -> R (in Ref. 2; AAL31374)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="Q -> H (in Ref. 1; BAA05168)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="L -> V (in Ref. 2; AAL31374)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="V -> G (in Ref. 1; BAA05168)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="L -> F (in Ref. 1; BAA05168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 104468 MW; 63DF250C8D2DA444 CRC64;
MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL KLKEGAENLR
RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL PDPTAGSDAP QSLAEGSPVC
SSTNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSTKDR KLLLTAQQML QDSKTKIDII
RMQLRRALQA LQAGQLESQA APDEAHGDPD LGAVELRIEE LRHHFRVEHA VAEGAKNVLR
LLSAAKAPDR KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS
AAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS VGASGTPDSR
TPFLSRPARG LYNRSGSLSG RSSLKGEAEN STEVSTVLKL DNTVVGQTAW KPCGPNAWDQ
SFTLELERAR ELELAVFWRD QRGLCALKFL KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR
NPIIERIPRL QRQKKIFSKQ QGQTFQRARQ MNIDVATWVR LLRRLIPNAV ATGSFSPNAS
PGSEIRSTGD ISMEKLNLGA DSDSSSQKSP AGLPSTSCSL SSPTHESTTS PELPSETQET
PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFHS SGELFAIKAL KKGDIVARDE
VESLMCEKRI LATVTRAGHP FLVNLFGCFQ TPEHVCFVME YSAGGDLMLH IHSDVFSEPR
AVFYSACVVL GLQFLHEHKI VYRDLKLDNL LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC
GTPEFLAPEV LTDTSYTRAV DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR
FLSAEAIGIM RRLLRRNPER RLGSTERDAE DVKKQPFFRT LDWDALLARR LPPPFVPTLS
GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY
