ID PAK2_RAT Reviewed; 524 AA.
AC Q64303; Q9QYU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 194.
DE RecName: Full=Serine/threonine-protein kinase PAK 2;
DE EC=2.7.11.1;
DE AltName: Full=Gamma-PAK;
DE AltName: Full=p21-activated kinase 2;
DE Short=PAK-2;
DE Contains:
DE RecName: Full=PAK-2p27;
DE Contains:
DE RecName: Full=PAK-2p34;
GN Name=Pak2;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain, and Testis;
RX PubMed=7592896; DOI=10.1074/jbc.270.44.26690;
RA Teo M., Manser E., Lim L.;
RT "Identification and molecular cloning of a p21cdc42/rac1-activated
RT serine/threonine kinase that is rapidly activated by thrombin in
RT platelets.";
RL J. Biol. Chem. 270:26690-26697(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mabel T.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Forebrain;
RA Marcus S., Polverino A., Robbins D., Hutchison M., Xu H., Asouline G.,
RA Cobb M., Wigler M.;
RT "Conservation of STE20-responsive MAP kinase activation in eukaryotic
RT organisms.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-59; SER-141; THR-143
RP AND SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 role in a
CC variety of different signaling pathways including cytoskeleton
CC regulation, cell motility, cell cycle progression, apoptosis or
CC proliferation. Acts as a downstream effector of the small GTPases CDC42
CC and RAC1. Activation by the binding of active CDC42 and RAC1 results in
CC a conformational change and a subsequent autophosphorylation on several
CC serine and/or threonine residues. Full-length PAK2 stimulates cell
CC survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates
CC the downstream target MAPKAPK5, a regulator of F-actin polymerization
CC and cell migration. Phosphorylates JUN and plays an important role in
CC EGF-induced cell proliferation. Phosphorylates many other substrates
CC including histone H4 to promote assembly of H3.3 and H4 into
CC nucleosomes, BAD, ribosomal protein S6, or MBP. Phosphorylates CASP7,
CC thereby preventing its activity. Additionally, associates with ARHGEF7
CC and GIT1 to perform kinase-independent functions such as spindle
CC orientation control during mitosis. On the other hand, apoptotic
CC stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2,
CC generating PAK-2p34, an active p34 fragment that translocates to the
CC nucleus and promotes cellular apoptosis involving the JNK signaling
CC pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces
CC cellular translation (By similarity). {ECO:0000250|UniProtKB:Q13177}.
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:Q13177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q13177};
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:Q13177};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q13177};
CC -!- ACTIVITY REGULATION: Activated by binding small G proteins. Binding of
CC GTP-bound CDC42 or RAC1 to the autoregulatory region releases monomers
CC from the autoinhibited dimer, enables phosphorylation of Thr-402 and
CC allows the kinase domain to adopt an active structure. Following
CC caspase cleavage, autophosphorylated PAK-2p34 is constitutively active
CC (By similarity). {ECO:0000250|UniProtKB:Q13177}.
CC -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound CDC42/p21
CC and RAC1. Interacts with SH3MD4. Interacts with SCRIB. Interacts with
CC ARHGEF7 and GIT1. PAK-2p34 interacts with ARHGAP10. Interacts with RAC1
CC (By similarity). {ECO:0000250|UniProtKB:Q13177}.
CC -!- SUBCELLULAR LOCATION: [Serine/threonine-protein kinase PAK 2]:
CC Cytoplasm {ECO:0000250|UniProtKB:Q13177}. Nucleus
CC {ECO:0000250|UniProtKB:Q13177}. Note=MYO18A mediates the cellular
CC distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of
CC the cell membrane. {ECO:0000250|UniProtKB:Q13177}.
CC -!- SUBCELLULAR LOCATION: [PAK-2p34]: Nucleus
CC {ECO:0000250|UniProtKB:Q13177}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q13177}. Membrane
CC {ECO:0000250|UniProtKB:Q13177}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q13177}. Note=Interaction with ARHGAP10 probably
CC changes PAK-2p34 location to cytoplasmic perinuclear region.
CC Myristoylation changes PAK-2p34 location to the membrane.
CC {ECO:0000250|UniProtKB:Q13177}.
CC -!- PTM: Full-length PAK2 is autophosphorylated when activated by
CC CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-2p34,
CC become highly autophosphorylated. Autophosphorylation of PAK-2p27 can
CC occur in the absence of any effectors and is dependent on
CC phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous
CC substrate (By similarity). {ECO:0000250|UniProtKB:Q13177}.
CC -!- PTM: During apoptosis proteolytically cleaved by caspase-3 or caspase-
CC 3-like proteases to yield active PAK-2p34.
CC {ECO:0000250|UniProtKB:Q13177}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q13177}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; S80221; AAB35608.1; -; mRNA.
DR EMBL; U35345; AAA79064.1; -; mRNA.
DR EMBL; U19967; AAF06695.1; -; mRNA.
DR RefSeq; NP_445758.2; NM_053306.3.
DR RefSeq; XP_003751114.1; XM_003751066.3.
DR RefSeq; XP_006248535.1; XM_006248473.2.
DR RefSeq; XP_008767000.1; XM_008768778.2.
DR PDB; 2DF6; X-ray; 1.30 A; C/D=180-197.
DR PDBsum; 2DF6; -.
DR AlphaFoldDB; Q64303; -.
DR SMR; Q64303; -.
DR BioGRID; 248079; 5.
DR IntAct; Q64303; 1.
DR STRING; 10116.ENSRNOP00000065949; -.
DR iPTMnet; Q64303; -.
DR PhosphoSitePlus; Q64303; -.
DR jPOST; Q64303; -.
DR PaxDb; 10116-ENSRNOP00000040162; -.
DR Ensembl; ENSRNOT00000049862.4; ENSRNOP00000040162.2; ENSRNOG00000001747.6.
DR Ensembl; ENSRNOT00060043834; ENSRNOP00060036373; ENSRNOG00060025077.
DR Ensembl; ENSRNOT00065034281; ENSRNOP00065027452; ENSRNOG00065020237.
DR GeneID; 29432; -.
DR KEGG; rno:29432; -.
DR UCSC; RGD:61953; rat.
DR AGR; RGD:61953; -.
DR CTD; 5062; -.
DR RGD; 61953; Pak2.
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00950000182988; -.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; Q64303; -.
DR OMA; MDFPPLR; -.
DR OrthoDB; 460351at2759; -.
DR PhylomeDB; Q64303; -.
DR TreeFam; TF105351; -.
DR BRENDA; 2.7.12.2; 5301.
DR Reactome; R-RNO-202433; Generation of second messenger molecules.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q64303; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001747; Expressed in spleen and 19 other cell types or tissues.
DR Genevisible; Q64303; RN.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; 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; ISS:UniProtKB.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0034333; P:adherens junction assembly; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0060996; P:dendritic spine development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0051179; P:localization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; ISO:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0150105; P:protein localization to cell-cell junction; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06655; STKc_PAK2; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035064; STK_PAK2.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF22; SERINE_THREONINE-PROTEIN KINASE PAK 2; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Lipoprotein; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT CHAIN 2..524
FT /note="Serine/threonine-protein kinase PAK 2"
FT /id="PRO_0000086468"
FT CHAIN 2..212
FT /note="PAK-2p27"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT /id="PRO_0000304928"
FT CHAIN 213..524
FT /note="PAK-2p34"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT /id="PRO_0000304929"
FT DOMAIN 74..87
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 249..500
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..137
FT /note="Autoregulatory region"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT REGION 69..112
FT /note="GTPase-binding"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT REGION 88..248
FT /note="Linker"
FT REGION 142..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..251
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT COMPBIAS 61..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 255..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 212..213
FT /note="Cleavage; by caspase-3 or caspase-3-like proteases"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIN4"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 143
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CIN4"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT MOD_RES 402
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13177"
FT CONFLICT 82
FT /note="H -> Y (in Ref. 3; AAF06695)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="K -> E (in Ref. 3; AAF06695)"
FT /evidence="ECO:0000305"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2DF6"
SQ SEQUENCE 524 AA; 57960 MW; A3F2FEE81C8D4294 CRC64;
MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR NKIISIFSST
EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP
QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNTK GSETSAVVTE EDDDDEDAAP
PVIAPRPDHT KSIYTRSVID PIPAPVGDSN VDSGAKSSDK QKKKAKMTDE EIMEKLRTIV
SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE
LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH
ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY
GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC
LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLILAAKEAM KSNR
//
