KPCT_MOUSE
ID KPCT_MOUSE Reviewed; 707 AA.
AC Q02111;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Protein kinase C theta type;
DE EC=2.7.11.13 {ECO:0000250|UniProtKB:Q04759};
DE AltName: Full=nPKC-theta;
GN Name=Prkcq; Synonyms=Pkcq;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AUTOPHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=1508194; DOI=10.1128/mcb.12.9.3930-3938.1992;
RA Osada S., Mizuno K., Saido T.C., Suzuki K., Kuroki T., Ohno S.;
RT "A new member of the protein kinase C family, nPKC theta, predominantly
RT expressed in skeletal muscle.";
RL Mol. Cell. Biol. 12:3930-3938(1992).
RN [2]
RP FUNCTION IN ACTIVATION OF NF-KAPPA-B, AND TISSUE SPECIFICITY.
RX PubMed=10746729; DOI=10.1038/35006090;
RA Sun Z., Arendt C.W., Ellmeier W., Schaeffer E.M., Sunshine M.J., Gandhi L.,
RA Annes J., Petrzilka D., Kupfer A., Schwartzberg P.L., Littman D.R.;
RT "PKC-theta is required for TCR-induced NF-kappaB activation in mature but
RT not immature T lymphocytes.";
RL Nature 404:402-407(2000).
RN [3]
RP FUNCTION IN ACTIVATION OF NFATC1 AND NFATC2.
RX PubMed=12782715; DOI=10.1084/jem.20020234;
RA Pfeifhofer C., Kofler K., Gruber T., Tabrizi N.G., Lutz C., Maly K.,
RA Leitges M., Baier G.;
RT "Protein kinase C theta affects Ca2+ mobilization and NFAT cell activation
RT in primary mouse T cells.";
RL J. Exp. Med. 197:1525-1535(2003).
RN [4]
RP FUNCTION IN T-HELPER 2 ACTIVATION.
RX PubMed=15263025; DOI=10.1084/jem.20032229;
RA Marsland B.J., Soos T.J., Spaeth G., Littman D.R., Kopf M.;
RT "Protein kinase C theta is critical for the development of in vivo T helper
RT (Th)2 cell but not Th1 cell responses.";
RL J. Exp. Med. 200:181-189(2004).
RN [5]
RP FUNCTION IN T-HELPER 17 ACTIVATION.
RX PubMed=16493044; DOI=10.4049/jimmunol.176.5.2872;
RA Tan S.L., Zhao J., Bi C., Chen X.C., Hepburn D.L., Wang J., Sedgwick J.D.,
RA Chintalacharuvu S.R., Na S.;
RT "Resistance to experimental autoimmune encephalomyelitis and impaired IL-17
RT production in protein kinase C theta-deficient mice.";
RL J. Immunol. 176:2872-2879(2006).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF PDPK1.
RX PubMed=19047061; DOI=10.1074/jbc.m806336200;
RA Wang C., Liu M., Riojas R.A., Xin X., Gao Z., Zeng R., Wu J., Dong L.Q.,
RA Liu F.;
RT "Protein kinase C theta (PKCtheta)-dependent phosphorylation of PDK1 at
RT Ser504 and Ser532 contributes to palmitate-induced insulin resistance.";
RL J. Biol. Chem. 284:2038-2044(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
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: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase that mediates non-redundant
CC functions in T-cell receptor (TCR) signaling, including T-cells
CC activation, proliferation, differentiation and survival, by mediating
CC activation of multiple transcription factors such as NF-kappa-B, JUN,
CC NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required
CC for the activation of NF-kappa-B and JUN, which in turn are essential
CC for IL2 production, and participates in the calcium-dependent NFATC1
CC and NFATC2 transactivation. Mediates the activation of the canonical
CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on
CC several serine residues, inducing CARD11 association with lipid rafts
CC and recruitment of the BCL10-MALT1 complex, which then activates IKK
CC complex, resulting in nuclear translocation and activation of NFKB1.
CC May also play an indirect role in activation of the non-canonical NF-
CC kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN
CC activation, acts by phosphorylating the mediator STK39/SPAK and may not
CC act through MAP kinases signaling. Plays a critical role in TCR/CD28-
CC induced NFATC1 and NFATC2 transactivation by participating in the
CC regulation of reduced inositol 1,4,5-trisphosphate generation and
CC intracellular calcium mobilization. After costimulation of T-cells
CC through CD28 can phosphorylate CBLB and is required for the
CC ubiquitination and subsequent degradation of CBLB, which is a
CC prerequisite for the activation of TCR. During T-cells differentiation,
CC plays an important role in the development of T-helper 2 (Th2) cells
CC following immune and inflammatory responses, and, in the development of
CC inflammatory autoimmune diseases, is necessary for the activation of
CC IL17-producing Th17 cells. May play a minor role in Th1 response. Upon
CC TCR stimulation, mediates T-cell protective survival signal by
CC phosphorylating BAD, thus protecting T-cells from BAD-induced
CC apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-
CC kappa-B and JUN pathways. In platelets, regulates signal transduction
CC downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors,
CC playing a positive role in 'outside-in' signaling and granule secretion
CC signal transduction. May relay signals from the activated ITGA2B
CC receptor by regulating the uncoupling of WASP and WIPF1, thereby
CC permitting the regulation of actin filament nucleation and branching
CC activity of the Arp2/3 complex. May mediate inhibitory effects of free
CC fatty acids on insulin signaling by phosphorylating IRS1, which in turn
CC blocks IRS1 tyrosine phosphorylation and downstream activation of the
CC PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of
CC phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at
CC 'Ser-504' and 'Ser-532' and negatively regulates its ability to
CC phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its
CC guanine nucleotide exchange factor activity (By similarity).
CC {ECO:0000250|UniProtKB:Q04759, ECO:0000269|PubMed:10746729,
CC ECO:0000269|PubMed:12782715, ECO:0000269|PubMed:1508194,
CC ECO:0000269|PubMed:15263025, ECO:0000269|PubMed:16493044,
CC ECO:0000269|PubMed:19047061}.
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:0000250|UniProtKB:Q04759};
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
CC calcium-insensitive, but activated by diacylglycerol (DAG) and
CC phosphatidylserine. Three specific sites; Thr-538 (activation loop of
CC the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic
CC region), need to be phosphorylated for its full activation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of a membrane raft complex composed at least of BCL10,
CC CARD11, MALT1 and IKBKB (By similarity). Interacts with GLRX3 (via N-
CC terminus) (By similarity). Interacts with ECT2 (By similarity).
CC Interacts with CCDC88A/GIV; the interaction leads to phosphorylation of
CC CCDC88A and inhibition of its guanine nucleotide exchange factor
CC activity (By similarity). {ECO:0000250|UniProtKB:Q04759}.
CC -!- INTERACTION:
CC Q02111; Q99JP0: Map4k3; NbExp=2; IntAct=EBI-2639157, EBI-5324222;
CC Q02111; P70257-2: Nfix; NbExp=3; IntAct=EBI-2639157, EBI-2639084;
CC Q02111; Q8IVH8: MAP4K3; Xeno; NbExp=4; IntAct=EBI-2639157, EBI-1758170;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein. Note=In resting T-cells,
CC mostly localized in cytoplasm. In response to TCR stimulation,
CC associates with lipid rafts and then localizes in the immunological
CC synapse (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: T-lymphocytes and skeletal muscle.
CC {ECO:0000269|PubMed:10746729, ECO:0000269|PubMed:1508194}.
CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1
CC (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a
CC non-calcium binding domain.
CC -!- PTM: Autophosphorylation at Thr-219 is required for targeting to the
CC TCR and cellular function of PRKCQ upon antigen receptor ligation.
CC Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685 (By
CC similarity). {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; D11091; BAA01864.1; -; mRNA.
DR CCDS; CCDS15682.1; -.
DR PIR; A44500; A44500.
DR RefSeq; NP_032885.1; NM_008859.2.
DR PDB; 4FKD; X-ray; 1.63 A; A=232-281.
DR PDBsum; 4FKD; -.
DR AlphaFoldDB; Q02111; -.
DR SMR; Q02111; -.
DR BioGRID; 202202; 5.
DR DIP; DIP-55947N; -.
DR IntAct; Q02111; 6.
DR STRING; 10090.ENSMUSP00000028118; -.
DR BindingDB; Q02111; -.
DR ChEMBL; CHEMBL1075295; -.
DR iPTMnet; Q02111; -.
DR PhosphoSitePlus; Q02111; -.
DR EPD; Q02111; -.
DR jPOST; Q02111; -.
DR MaxQB; Q02111; -.
DR PaxDb; Q02111; -.
DR PRIDE; Q02111; -.
DR ProteomicsDB; 264864; -.
DR Antibodypedia; 10940; 849 antibodies from 41 providers.
DR DNASU; 18761; -.
DR Ensembl; ENSMUST00000028118; ENSMUSP00000028118; ENSMUSG00000026778.
DR GeneID; 18761; -.
DR KEGG; mmu:18761; -.
DR UCSC; uc008iic.1; mouse.
DR CTD; 5588; -.
DR MGI; MGI:97601; Prkcq.
DR VEuPathDB; HostDB:ENSMUSG00000026778; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000157638; -.
DR HOGENOM; CLU_000288_54_4_1; -.
DR InParanoid; Q02111; -.
DR OMA; IHLVKCH; -.
DR OrthoDB; 222529at2759; -.
DR PhylomeDB; Q02111; -.
DR TreeFam; TF102004; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-373752; Netrin-1 signaling.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 18761; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q02111; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q02111; protein.
DR Bgee; ENSMUSG00000026778; Expressed in habenula and 170 other tissues.
DR ExpressionAtlas; Q02111; baseline and differential.
DR Genevisible; Q02111; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0004697; F:protein kinase C activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IMP:UniProtKB.
DR GO; GO:2000570; P:positive regulation of T-helper 2 cell activation; IMP:UniProtKB.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0090330; P:regulation of platelet aggregation; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR CDD; cd00029; C1; 2.
DR CDD; cd05619; STKc_nPKC_theta; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034668; nPKC_theta.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027264; PKC_theta.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PIRSF; PIRSF501105; Protein_kin_C_theta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; Immunity;
KW Inflammatory response; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="Protein kinase C theta type"
FT /id="PRO_0000055709"
FT DOMAIN 1..107
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 380..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 635..706
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 159..209
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 231..281
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 327..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 504
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 386..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 90
FT /note="Phosphotyrosine; by LCK"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 219
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 538
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 676
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04759, ECO:0000255"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04759"
FT MOD_RES 695
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04759, ECO:0000255"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4FKD"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4FKD"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4FKD"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4FKD"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4FKD"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:4FKD"
SQ SEQUENCE 707 AA; 81573 MW; 7A16492116CD2880 CRC64;
MSPFLRIGLS NFDCGTCQAC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF
DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GRTEIWLELK PQGRMLMNAR
YFLEMSDTKD MSEFENEGFF ALHQRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV
WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK
SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ
ARSLRDSEHI FREGPVEIGL PCSTKNETRP PCVPTPGKRE PQGISWDSPL DGSNKSAGPP
EPEVSMRRTS LQLKLKIDDF ILHKMLGKGS FGKVFLAEFK RTNQFFAIKA LKKDVVLMDD
DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR
ATFYAAEVIL GLQFLHSKGI VYRDLKLDNI LLDRDGHIKI ADFGMCKENM LGDAKTNTFC
GTPDYIAPEI LLGQKYNHSV DWWSFGVLVY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR
WLEREAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPYD
CSNFDKEFLS EKPRLSFADR ALINSMDQNM FSNFSFINPG METLICS
