NTRK3_CHICK
ID NTRK3_CHICK Reviewed; 827 AA.
AC Q91044; Q91011; Q92022;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=NT-3 growth factor receptor;
DE EC=2.7.10.1;
DE AltName: Full=Neurotrophic tyrosine kinase receptor type 3;
DE AltName: Full=TrkC tyrosine kinase;
DE Short=Trk-C;
DE Flags: Precursor;
GN Name=NTRK3; Synonyms=TRKC;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-FL; ALPHA-KT; ALPHA-KD; BETA-KD
RP AND KI25), AND FUNCTION.
RC TISSUE=Embryonic brain;
RX PubMed=8060621; DOI=10.1016/0896-6273(94)90360-3;
RA Garner A.S., Large T.H.;
RT "Isoforms of the avian TrkC receptor: a novel kinase insertion dissociates
RT transformation and process outgrowth from survival.";
RL Neuron 13:457-472(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-FL AND TRKC-3).
RX PubMed=8394830; DOI=10.1016/0014-5793(93)80216-h;
RA Okazawa H., Kamei M., Kanazawa I.;
RT "Molecular cloning and expression of a novel truncated form of chicken
RT trkC.";
RL FEBS Lett. 329:171-177(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 378-513.
RC TISSUE=Embryo;
RX PubMed=8261614; DOI=10.1016/0165-3806(93)90028-9;
RA Williams R., Backstrom A., Ebendal T., Hallboeoek F.;
RT "Molecular cloning and cellular localization of trkC in the chicken
RT embryo.";
RL Brain Res. Dev. Brain Res. 75:235-252(1993).
RN [4]
RP INTERACTION WITH PTPRS.
RX PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
RA Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S., Stoker A.;
RT "PTPsigma binds and dephosphorylates neurotrophin receptors and can
RT suppress NGF-dependent neurite outgrowth from sensory neurons.";
RL Biochim. Biophys. Acta 1773:1689-1700(2007).
RN [5] {ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 32-302 IN COMPLEX WITH PTPRS,
RP GLYCOSYLATION AT ASN-79; ASN-203 AND ASN-272, AND DISULFIDE BONDS.
RX PubMed=25385546; DOI=10.1038/ncomms6209;
RA Coles C.H., Mitakidis N., Zhang P., Elegheert J., Lu W., Stoker A.W.,
RA Nakagawa T., Craig A.M., Jones E.Y., Aricescu A.R.;
RT "Structural basis for extracellular cis and trans RPTPsigma signal
RT competition in synaptogenesis.";
RL Nat. Commun. 5:5209-5209(2014).
CC -!- FUNCTION: Receptor tyrosine kinase involved in nervous system and
CC probably heart development. Upon binding of its ligand
CC NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different
CC signaling pathways, including the phosphatidylinositol 3-kinase/AKT and
CC the MAPK pathways, that control cell survival and differentiation (By
CC similarity). The KT and KD isoforms fail to stimulate transformation,
CC process outgrowth or survival. Isoform KI25 exhibits tyrosine
CC phosphorylation in the absence of ligand and is unable to mediate
CC survival of neuronal cells (PubMed:8060621).
CC {ECO:0000250|UniProtKB:Q16288, ECO:0000269|PubMed:8060621}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC affinity) and dimeric (high affinity) structures (By similarity).
CC Interacts with PTPRS (PubMed:17967490, PubMed:25385546). {ECO:0000250,
CC ECO:0000269|PubMed:17967490, ECO:0000269|PubMed:25385546}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha-FL;
CC IsoId=Q91044-1; Sequence=Displayed;
CC Name=Alpha-KT;
CC IsoId=Q91044-2; Sequence=VSP_002943, VSP_002944;
CC Name=Alpha-KD;
CC IsoId=Q91044-3; Sequence=VSP_002939, VSP_002940;
CC Name=Beta-KD;
CC IsoId=Q91044-4; Sequence=VSP_002938, VSP_002939, VSP_002940;
CC Name=TRKC-3;
CC IsoId=Q91044-5; Sequence=VSP_002941, VSP_002942;
CC Name=KI25;
CC IsoId=Q91044-6; Sequence=VSP_002945;
CC -!- DEVELOPMENTAL STAGE: Expression occurs in the embryonal day 2 (E2)
CC embryo with increasing levels later in development. In the E9 embryo
CC highest levels are found in brain and spinal cord with intermediate
CC levels in eye, heart, gut and muscle. Low levels are found in kidney,
CC liver, skin and yolk sac.
CC -!- PTM: Ligand-mediated auto-phosphorylation. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform TRKC-3]: The kinase domain is of 19 aa instead
CC of 39aa in the isoform alpha-KD due to a frameshift. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S74248; AAB31699.1; -; mRNA.
DR EMBL; X59669; CAA42202.1; -; mRNA.
DR EMBL; Z30091; CAA82907.1; -; mRNA.
DR PIR; I51222; I51222.
DR PIR; I51259; I51259.
DR PIR; S35695; S35695.
DR RefSeq; NP_990500.1; NM_205169.1. [Q91044-6]
DR RefSeq; XP_015147467.1; XM_015291981.1. [Q91044-1]
DR PDB; 4PBV; X-ray; 2.50 A; A/B=32-302.
DR PDB; 4PBW; X-ray; 3.05 A; A/B/C=32-302.
DR PDBsum; 4PBV; -.
DR PDBsum; 4PBW; -.
DR AlphaFoldDB; Q91044; -.
DR SMR; Q91044; -.
DR STRING; 9031.ENSGALP00000010970; -.
DR Ensembl; ENSGALT00000056594; ENSGALP00000052783; ENSGALG00000040241. [Q91044-1]
DR Ensembl; ENSGALT00000072944; ENSGALP00000049680; ENSGALG00000040241. [Q91044-6]
DR Ensembl; ENSGALT00000095819; ENSGALP00000069877; ENSGALG00000040241. [Q91044-2]
DR GeneID; 396081; -.
DR KEGG; gga:396081; -.
DR CTD; 4916; -.
DR VEuPathDB; HostDB:geneid_396081; -.
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000155645; -.
DR InParanoid; Q91044; -.
DR OMA; RXVGGHT; -.
DR OrthoDB; 295510at2759; -.
DR PhylomeDB; Q91044; -.
DR BRENDA; 2.7.10.1; 1306.
DR Reactome; R-GGA-170984; ARMS-mediated activation.
DR Reactome; R-GGA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-GGA-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:Q91044; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000040241; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; Q91044; baseline and differential.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043121; F:neurotrophin binding; IBA:GO_Central.
DR GO; GO:0005030; F:neurotrophin receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR020777; NTRK.
DR InterPro; IPR020446; NTRK3.
DR InterPro; IPR031635; NTRK_LRRCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF16920; LRRCT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01939; NTKRECEPTOR.
DR PRINTS; PR01942; NTKRECEPTOR3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Leucine-rich repeat; Membrane; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..827
FT /note="NT-3 growth factor receptor"
FT /id="PRO_0000016736"
FT TOPO_DOM 32..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..125
FT /note="LRR 1"
FT REPEAT 128..149
FT /note="LRR 2"
FT DOMAIN 160..209
FT /note="LRRCT"
FT DOMAIN 210..300
FT /note="Ig-like C2-type 1"
FT DOMAIN 319..382
FT /note="Ig-like C2-type 2"
FT DOMAIN 540..812
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 681
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 546..554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 518
FT /note="Interaction with SHC1"
FT /evidence="ECO:0000250"
FT SITE 822
FT /note="Interaction with PLC-gamma-1"
FT /evidence="ECO:0000250"
FT MOD_RES 518
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 707
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 711
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 712
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 822
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4PBW"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4PBV"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4PBV"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..38
FT /evidence="ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW"
FT DISULFID 36..45
FT /evidence="ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW"
FT DISULFID 164..189
FT /evidence="ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW"
FT DISULFID 166..207
FT /evidence="ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW"
FT DISULFID 231..284
FT /evidence="ECO:0007744|PDB:4PBV, ECO:0007744|PDB:4PBW"
FT DISULFID 320..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform Beta-KD)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002938"
FT VAR_SEQ 581..619
FT /note="LAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVF -> CFREIMLNP
FT ISLPGHSKPLNQGIYVEDVSVYFSKGRHGF (in isoform Alpha-KD and
FT isoform Beta-KD)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002939"
FT VAR_SEQ 581..599
FT /note="LAARKDFQREAELLTNLQH -> CFREIMLNPISLPGHCQTS (in
FT isoform TRKC-3)"
FT /evidence="ECO:0000303|PubMed:8394830"
FT /id="VSP_002941"
FT VAR_SEQ 600..827
FT /note="Missing (in isoform TRKC-3)"
FT /evidence="ECO:0000303|PubMed:8394830"
FT /id="VSP_002942"
FT VAR_SEQ 620..827
FT /note="Missing (in isoform Alpha-KD and isoform Beta-KD)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002940"
FT VAR_SEQ 633..664
FT /note="AHGPDAMILVDGQPRQAKGELGLSQMLHIASQ -> LEDTPCCLSAGCLRRA
FT SCTGSSQRRVTSGASG (in isoform Alpha-KT)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002943"
FT VAR_SEQ 665..827
FT /note="Missing (in isoform Alpha-KT)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002944"
FT VAR_SEQ 713
FT /note="R -> REGPRPKGQLSTAWQRHRLAPPAAAT (in isoform KI25)"
FT /evidence="ECO:0000303|PubMed:8060621"
FT /id="VSP_002945"
FT CONFLICT 1..39
FT /note="MDVSLCPTKCTFWRVFLLWSIWGDYLLSVLACPANCLCS -> MHFICWRIF
FT ASDRLKVLF (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="A -> G (in Ref. 2; CAA42202)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="I -> F (in Ref. 3; CAA82907)"
FT /evidence="ECO:0000305"
FT CONFLICT 481..496
FT /note="SPLHHINHGITTPSSL -> ATHTSTTDTRFVT (in Ref. 2;
FT CAA42202)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="W -> C (in Ref. 2; CAA42202)"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:4PBW"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4PBV"
FT TURN 120..125
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:4PBV"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:4PBV"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:4PBV"
SQ SEQUENCE 827 AA; 93181 MW; AB97373113DCB28A CRC64;
MDVSLCPTKC TFWRVFLLWS IWGDYLLSVL ACPANCLCSK TDINCKKPDD GNLFPLLEGQ
DSGSSNGNTS INITDISRNI TSIHIENWKN LQTLNAVDME LYTGLQRLTI RNSGLRNIQP
RAFAKNPHLR YIDLSGNRLT TLSWQLFQTL RLFDLRLERN PFNCSCDIRW IQLWQEKGEA
NLQSQQLHCM NLDTAVILLR NMNITQCDLP EISVSHVNLT VREGENAVIT CNGSGSPLPD
VDWTVADLHS INTHQTNLNW TNVHAINLTL VNVTSEDNGF LLTCIAENVV GMSNASVLLT
VYYPPRILTL EEPVLHLEHC IAFAVHGNPA PTLHWLHNGQ VLRETEIIHM EFYQQGEVSE
GCLLFNKPTH YNNGNYTIVA TNQLGSANQT IKGHFLEKPF PESTDNFVSI GDYEVSPTPP
ITVTHKPEED TFGVSIAVGL AAFACVLLVV LFIMINKYGR RSKFGMKGPV AVISGEEDSA
SPLHHINHGI TTPSSLDAGP DTVVIGMTRI PVIENPQYFR QGHNCHKPDT YVQHIKRRDI
VLKRELGEGA FGKVFLAECY NLSPTNDKML VAVKALKDPT LAARKDFQRE AELLTNLQHE
HIVKFYGVCG DGDPLIMVFE YMKHGDLNKF LRAHGPDAMI LVDGQPRQAK GELGLSQMLH
IASQIASGMV YLASQHFVHR DLATRNCLVG ANLLVKIGDF GMSRDVYSTD YYRVGGHTML
PIRWMPPESI MYRKFTTESD VWSFGVILWE IFTYGKQPWF QLSNTEVIEC ITQGRVLERP
RVCPKEVYDI MLGCWQREPQ QRLNIKEIYK ILHALGKATP IYLDILG
