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Database: UniProt
Entry: Q5R5M7
LinkDB: Q5R5M7
Original site: Q5R5M7 
ID   RAF1_PONAB              Reviewed;         648 AA.
AC   Q5R5M7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=RAF proto-oncogene serine/threonine-protein kinase;
DE            EC=2.7.11.1 {ECO:0000250|UniProtKB:P04049};
DE   AltName: Full=Proto-oncogene c-RAF;
DE            Short=cRaf;
DE   AltName: Full=Raf-1;
GN   Name=RAF1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase that acts as a regulatory
CC       link between the membrane-associated Ras GTPases and the MAPK/ERK
CC       cascade, and this critical regulatory link functions as a switch
CC       determining cell fate decisions including proliferation,
CC       differentiation, apoptosis, survival and oncogenic transformation. RAF1
CC       activation initiates a mitogen-activated protein kinase (MAPK) cascade
CC       that comprises a sequential phosphorylation of the dual-specific MAPK
CC       kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-
CC       regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form
CC       of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates
CC       BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl
CC       cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation.
CC       Phosphorylates PPP1R12A resulting in inhibition of the phosphatase
CC       activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote
CC       NF-kB activation and inhibit signal transducers involved in motility
CC       (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and
CC       angiogenesis (RB1). Can protect cells from apoptosis also by
CC       translocating to the mitochondria where it binds BCL2 and displaces
CC       BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and
CC       migration, and is required for normal wound healing. Plays a role in
CC       the oncogenic transformation of epithelial cells via repression of the
CC       TJ protein, occludin (OCLN) by inducing the up-regulation of a
CC       transcriptional repressor SNAI2/SLUG, which induces down-regulation of
CC       OCLN. Restricts caspase activation in response to selected stimuli,
CC       notably Fas stimulation, pathogen-mediated macrophage apoptosis, and
CC       erythroid differentiation (By similarity).
CC       {ECO:0000250|UniProtKB:P04049}.
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:P04049};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000250|UniProtKB:P04049};
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:P04049};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000250|UniProtKB:P04049};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Regulation is a highly complex process involving
CC       membrane recruitment, protein-protein interactions, dimerization, and
CC       phosphorylation/dephosphorylation events. Ras-GTP recruits RAF1 to the
CC       membrane, thereby promoting its activation. The inactive conformation
CC       of RAF1 is maintained by autoinhibitory interactions occurring between
CC       the N-terminal regulatory and the C-terminal catalytic domains and by
CC       the binding of a 14-3-3 protein that contacts two phosphorylation
CC       sites, Ser-259 and Ser-621. Upon mitogenic stimulation, Ras and PPP2R1A
CC       cooperate to release autoinhibition and the subsequent phosphorylation
CC       of activating sites: Ser-338, Tyr-341, Thr-491, and Ser-494, yields a
CC       fully active kinase. Through a negative feedback mechanism involving
CC       MAPK1/ERK2, RAF1 is phosphorylated on Ser-29, Ser-43, Ser-289, Ser-296,
CC       Ser-301 and Ser-642 by MAPK1/ERK2, which yields an inactive,
CC       desensitized kinase. The signaling-competent conformation of RAF1 is
CC       finally re-established by the coordinated action of PIN1, a prolyl
CC       isomerase that converts pSer and pThr residues from the cis to the
CC       trans conformation, which is preferentially recognized and
CC       dephosphorylated by PPP2R1A. Activated by homodimerization and
CC       heterodimerization (with BRAF). Also regulated through association with
CC       other proteins such as KSR2, CNKSR1/CNK1, PEBP1/RKIP, PHB/prohibitin
CC       and SPRY4. PEBP1/RKIP acts by dissociating RAF1 from its substrates
CC       MAP2K1/MEK1 and MAP2K2/MEK2. PHB/prohibitin facilitates the
CC       displacement of 14-3-3 from RAF1 by activated Ras, thereby promoting
CC       cell membrane localization and phosphorylation of RAF1 at the
CC       activating Ser-338. SPRY4 inhibits Ras-independent, but not Ras-
CC       dependent, activation of RAF1. CNKSR1/CNK1 regulates Src-mediated RAF1
CC       activation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer. Heterodimerizes with BRAF and this
CC       heterodimer possesses a highly increased kinase activity compared to
CC       the respective homodimers or monomers. Heterodimerization is mitogen-
CC       regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2 activation can
CC       induce a negative feedback that promotes the dissociation of the
CC       heterodimer. Forms a multiprotein complex with Ras (M-Ras/MRAS), SHOC2
CC       and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts with
CC       LZTR1. Interacts with Ras proteins; the interaction is antagonized by
CC       RIN1 (By similarity). Weakly interacts with RIT1. Interacts (via N-
CC       terminus) with RGS14 (via RBD domains); the interaction mediates the
CC       formation of a ternary complex with BRAF, a ternary complex inhibited
CC       by GNAI1 (By similarity). Probably forms a complex composed of
CC       chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and client
CC       protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not contain
CC       co-chaperones STIP1/HOP and PTGES3/p23. Interacts with STK3/MST2; the
CC       interaction inhibits its pro-apoptotic activity. Interacts (when
CC       phosphorylated at Ser-259) with YWHAZ (unphosphorylated at 'Thr-232')
CC       (By similarity). Interacts with MAP2K1/MEK1 and MAP2K2/MEK2 (By
CC       similarity). Interacts with MAP3K5/ASF1 (via N-terminus) and this
CC       interaction inhibits the proapoptotic function of MAP3K5/ASK1.
CC       Interacts with PAK1 (via kinase domain) (By similarity). The
CC       phosphorylated form interacts with PIN1 (By similarity). The Ser-338
CC       and Ser-339 phosphorylated form (by PAK1) interacts with BCL2.
CC       Interacts with PEBP1/RKIP and this interaction is enhanced if RAF1 is
CC       phosphorylated on residues Ser-338, Ser-339, Tyr-340 and Tyr-341.
CC       Interacts with ADCY2, ADCY5, ADCY6, DGKH, RCAN1/DSCR1, PPP1R12A,
CC       PKB/AKT1, PPP2CA, PPP2R1B, SPRY2, SPRY4, CNKSR1/CNK1, KSR2 and
CC       PHB/prohibitin (By similarity). Interacts with ROCK2 (By similarity).
CC       In its active form, interacts with PRMT5. Interacts with FAM83B;
CC       displaces 14-3-3 proteins from RAF1 and activates RAF1. Interacts with
CC       PDE8A; the interaction promotes RAF1 activity. Interacts with MFHAS1.
CC       Interacts with GLS (By similarity). Interacts with NEK10 and MAP2K1;
CC       the interaction is direct with NEK10 and required for ERK1/2-signaling
CC       pathway activation in response to UV irradiation (By similarity).
CC       {ECO:0000250|UniProtKB:P04049, ECO:0000250|UniProtKB:P11345,
CC       ECO:0000250|UniProtKB:Q99N57}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and
CC       membranes. Phosphorylation at Ser-259 impairs its membrane
CC       accumulation. Recruited to the cell membrane by the active Ras protein.
CC       Phosphorylation at Ser-338 and Ser-339 by PAK1 is required for its
CC       mitochondrial localization. Retinoic acid-induced Ser-621
CC       phosphorylated form of RAF1 is predominantly localized at the nucleus
CC       (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494
CC       results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289,
CC       Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation.
CC       Phosphorylation at Ser-259 induces the interaction with YWHAZ and
CC       inactivates kinase activity. Dephosphorylation of Ser-259 by the
CC       complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS relieves
CC       inactivation, leading to stimulate RAF1 activity. Phosphorylation at
CC       Ser-338 by PAK1 and PAK5 and Ser-339 by PAK1 is required for its
CC       mitochondrial localization (By similarity). Phosphorylation at Ser-621
CC       in response to growth factor treatment stabilizes the protein, possibly
CC       by preventing proteasomal degradation. Phosphorylation at Ser-289, Ser-
CC       296, Ser-301, Ser-338 and Ser-621 are somehow linked to the methylation
CC       potential of cells. Treatment of cells with HGF in the presence of the
CC       methylation inhibitor 5'-methylthioadenosine (MTA) results in increased
CC       phosphorylation at Ser-338 and Ser-621 and decreased phosphorylation at
CC       Ser-296, Ser-301 and Ser-338. Dephosphorylation at Ser-338 by PPP5C
CC       results in a decreased of activity (By similarity). {ECO:0000250}.
CC   -!- PTM: Methylated at Arg-563 in response to EGF treatment. This
CC       modification leads to destabilization of the protein, possibly through
CC       proteasomal degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000305}.
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DR   EMBL; CR860830; CAH92939.1; -; mRNA.
DR   RefSeq; NP_001126730.1; NM_001133258.1.
DR   AlphaFoldDB; Q5R5M7; -.
DR   BMRB; Q5R5M7; -.
DR   SMR; Q5R5M7; -.
DR   STRING; 9601.ENSPPYP00000014975; -.
DR   Ensembl; ENSPPYT00000015575.2; ENSPPYP00000014975.1; ENSPPYG00000013388.2.
DR   GeneID; 100173732; -.
DR   KEGG; pon:100173732; -.
DR   CTD; 5894; -.
DR   eggNOG; KOG0193; Eukaryota.
DR   GeneTree; ENSGT00940000156084; -.
DR   HOGENOM; CLU_023684_1_1_1; -.
DR   InParanoid; Q5R5M7; -.
DR   OrthoDB; 4560496at2759; -.
DR   TreeFam; TF317006; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd20870; C1_A_C-Raf; 1.
DR   CDD; cd17135; RBD_CRAF; 1.
DR   CDD; cd14149; STKc_C-Raf; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; RBD_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23257:SF763; RAF PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Cytoplasm; Kinase; Membrane; Metal-binding;
KW   Methylation; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..648
FT                   /note="RAF proto-oncogene serine/threonine-protein kinase"
FT                   /id="PRO_0000260304"
FT   DOMAIN          56..131
FT                   /note="RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT   DOMAIN          349..609
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ZN_FING         138..184
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          220..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..349
FT                   /note="Interaction with PEBP1/RKIP"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        222..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        468
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         29
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99N57"
FT   MOD_RES         43
FT                   /note="Phosphoserine; by PKA and MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         233
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         259
FT                   /note="Phosphoserine; by PKA, PKC and PKB/AKT1"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         268
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         269
FT                   /note="Phosphothreonine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         289
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         296
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99N57"
FT   MOD_RES         301
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         338
FT                   /note="Phosphoserine; by PAK1, PAK2, PAK3 and PAK5"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         339
FT                   /note="Phosphoserine; by PAK1, PAK2 and PAK3"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         340
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         341
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         491
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         494
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         497
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         499
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         563
FT                   /note="Symmetric dimethylarginine; by PRMT5"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         621
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
FT   MOD_RES         642
FT                   /note="Phosphoserine; by MAPK1"
FT                   /evidence="ECO:0000250|UniProtKB:P04049"
SQ   SEQUENCE   648 AA;  73052 MW;  EF821B5349711BC3 CRC64;
     MEHIQGAWKT ISNGFGFKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD PSKTSNTIRV
     FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR LLHEHKGKKA RLDWNTDAAS
     LIGEELQVDF LDHVPLTTHN FARKTFLKLA FCDICQKFLL NGFRCQTCGY KFHEHCSTKV
     PTMCVDWSNI RQLLLFPNST IGDSGVPALP SLTMRRMRES VSRMPVSSQH RYSTPHAFTF
     NTSSPSSEGS LSQRQRSTST PNVHMVSTTL PVDSRMIEDA IRSHSESASP SALSSSPNNL
     SPTGWSQPKT PVPAQRERAP VSGTQEKNKI RPRGQRDSSY YWEIEASEVM LSTRIGSGSF
     GTVYKGKWHG DVAVKILKVV DPTPEQFQAF RNEVAVLRKT RHVNILLFMG YMTKDNLAIV
     TQWCEGSSLY KHLHVQETKF QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
     TVKIGDFGLA TVKSRWSGSQ QVEQPTGSVL WMAPEVIRMQ DNNPFSFQSD VYSYGIVLYE
     LMTGELPYSH INNRDQIIFM VGRGYASPDL SKLYKNCPKA MKRLVADCVK KVKEERPLFP
     QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
//
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