PTN_RAT
ID PTN_RAT Reviewed; 168 AA.
AC P63090; P20935;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Pleiotrophin {ECO:0000303|PubMed:2270483};
DE Short=PTN {ECO:0000303|PubMed:2270483};
DE AltName: Full=Heparin-binding brain mitogen {ECO:0000303|PubMed:2388713};
DE Short=HBBM {ECO:0000303|PubMed:2388713};
DE AltName: Full=Heparin-binding growth factor 8 {ECO:0000250|UniProtKB:P21782};
DE Short=HBGF-8 {ECO:0000250|UniProtKB:P21782};
DE AltName: Full=Heparin-binding growth-associated molecule {ECO:0000303|PubMed:2170351};
DE Short=HB-GAM {ECO:0000303|PubMed:2170351};
DE AltName: Full=Heparin-binding neutrophic factor {ECO:0000303|PubMed:1700712};
DE Short=HBNF {ECO:0000303|PubMed:1700712};
DE AltName: Full=Osteoblast-specific factor 1 {ECO:0000250|UniProtKB:P21246};
DE Short=OSF-1 {ECO:0000250|UniProtKB:P21246};
DE Flags: Precursor;
GN Name=Ptn {ECO:0000312|RGD:3444};
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], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=2170351; DOI=10.1016/s0021-9258(17)44817-4;
RA Merenmies J., Rauvala H.;
RT "Molecular cloning of the 18-kDa growth-associated protein of developing
RT brain.";
RL J. Biol. Chem. 265:16721-16724(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2270483; DOI=10.1126/science.2270483;
RA Li Y.-S., Milner P.G., Chauhan A.K., Watson M.A., Hoffman R.M.,
RA Kodner C.M., Milbrandt J., Deuel T.F.;
RT "Cloning and expression of a developmentally regulated protein that induces
RT mitogenic and neurite outgrowth activity.";
RL Science 250:1690-1694(1990).
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 33-54.
RC TISSUE=Brain;
RX PubMed=2388713; DOI=10.1007/bf00969930;
RA Huber D., Gautschi-Sova P., Bohlen P.;
RT "Amino-terminal sequences of a novel heparin-binding protein from human,
RT bovine, rat, and chick brain: high interspecies homology.";
RL Neurochem. Res. 15:435-439(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-134.
RC STRAIN=Sprague-Dawley;
RX PubMed=1700712; DOI=10.1016/0006-291x(90)90753-a;
RA Kovesdi I., Fairhurst J.L., Kretschmer P.J., Boehlen P.;
RT "Heparin-binding neurotrophic factor (HBNF) and MK, members of a new family
RT of homologous, developmentally regulated proteins.";
RL Biochem. Biophys. Res. Commun. 172:850-854(1990).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=1768439; DOI=10.3109/08977199109000275;
RA Kretschmer P.J., Fairhurst J.L., Decker M.M., Chan C.P., Gluzman Y.,
RA Boehlen P., Kovesdi I.;
RT "Cloning, characterization and developmental regulation of two members of a
RT novel human gene family of neurite outgrowth-promoting proteins.";
RL Growth Factors 5:99-114(1991).
RN [7]
RP INTERACTION WITH SDC3.
RX PubMed=8175719; DOI=10.1016/s0021-9258(18)99975-8;
RA Raulo E., Chernousov M.A., Carey D.J., Nolo R., Rauvala H.;
RT "Isolation of a neuronal cell surface receptor of heparin binding growth-
RT associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3).";
RL J. Biol. Chem. 269:12999-13004(1994).
RN [8]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH
RP SDC3.
RX PubMed=9817766; DOI=10.1083/jcb.143.4.1113;
RA Imai S., Kaksonen M., Raulo E., Kinnunen T., Fages C., Meng X., Lakso M.,
RA Rauvala H.;
RT "Osteoblast recruitment and bone formation enhanced by cell matrix-
RT associated heparin-binding growth-associated molecule (HB-GAM).";
RL J. Cell Biol. 143:1113-1128(1998).
RN [9]
RP FUNCTION, AND INTERACTION WITH PTPRZ1.
RX PubMed=16814777; DOI=10.1016/j.febslet.2006.06.041;
RA Fukada M., Fujikawa A., Chow J.P., Ikematsu S., Sakuma S., Noda M.;
RT "Protein tyrosine phosphatase receptor type Z is inactivated by ligand-
RT induced oligomerization.";
RL FEBS Lett. 580:4051-4056(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH GPC2.
RX PubMed=27671118; DOI=10.1038/srep33916;
RA Paveliev M., Fenrich K.K., Kislin M., Kuja-Panula J., Kulesskiy E.,
RA Varjosalo M., Kajander T., Mugantseva E., Ahonen-Bishopp A., Khiroug L.,
RA Kulesskaya N., Rougon G., Rauvala H.;
RT "HB-GAM (pleiotrophin) reverses inhibition of neural regeneration by the
RT CNS extracellular matrix.";
RL Sci. Rep. 6:33916-33916(2016).
CC -!- FUNCTION: Secreted growth factor that mediates its signal through cell-
CC surface proteoglycan and non-proteoglycan receptors (PubMed:16814777,
CC PubMed:27671118, PubMed:9817766). Binds cell-surface proteoglycan
CC receptor via their chondroitin sulfate (CS) groups (By similarity).
CC Thereby regulates many processes like cell proliferation, cell
CC survival, cell growth, cell differentiation and cell migration in
CC several tissues namely neuron and bone (PubMed:27671118,
CC PubMed:9817766). Also plays a role in synaptic plasticity and learning-
CC related behavior by inhibiting long-term synaptic potentiation (By
CC similarity). Binds PTPRZ1, leading to neutralization of the negative
CC charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby
CC causing the dimerization and inactivation of its phosphatase activity
CC leading to increased tyrosine phosphorylation of each of the PTPRZ1
CC substrates like ALK or AFAP1L2 in order to activate the PI3K-AKT
CC pathway (PubMed:16814777). Through PTPRZ1 binding, regulates
CC endothelial cell migration and controls oligodendrocyte precursor cell
CC differentiation (By similarity). Forms a complex with PTPRZ1 and
CC integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell
CC migration through SRC dephosphorylation and activation that
CC consequently leads to ITGB3 'Tyr-773' phosphorylation (By similarity).
CC In adult hippocampus promotes dendritic arborization, spine
CC development, and functional integration and connectivity of newborn
CC granule neurons through ALK by activating AKT signaling pathway (By
CC similarity). Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs)
CC at the neuron surface, leading to abrogation of binding between PTPRS
CC and CSPGs and neurite outgrowth promotion (PubMed:27671118). Binds SDC3
CC and mediates bone formation by recruiting and attaching
CC osteoblasts/osteoblast precursors to the sites for new bone deposition
CC (PubMed:9817766). Binds ALK and promotes cell survival and cell
CC proliferation through MAPK pathway activation (By similarity). Inhibits
CC proliferation and enhances differentiation of neural stem cells by
CC inhibiting FGF2-induced fibroblast growth factor receptor signaling
CC pathway (By similarity). Mediates regulatory mechanisms in normal
CC hemostasis and in hematopoietic regeneration and in maintaining the
CC balance of myeloid and lymphoid regeneration (By similarity). In
CC addition may play a role in the female reproductive system, auditory
CC response and the progesterone-induced decidualization pathway (By
CC similarity). {ECO:0000250|UniProtKB:P21246,
CC ECO:0000250|UniProtKB:P63089, ECO:0000269|PubMed:16814777,
CC ECO:0000269|PubMed:27671118, ECO:0000269|PubMed:9817766}.
CC -!- SUBUNIT: Interacts with ALK and NEK6 (By similarity). Interacts with
CC PTPRZ1 (via chondroitin sulfate groups); promotes formation of
CC homooligomers; oligomerization impairs tyrosine phosphatase activity
CC (PubMed:16814777). Forms a complex with PTPRZ1 and CTNNB1; this complex
CC inactivates PTPRZ1 protein tyrosine phosphatase activity through PTN
CC interaction and stimulates tyrosine phosphorylation of CTNNB1.
CC Interacts with ITGB3 AND ITGA5. Forms a complex with PTPRZ1 and
CC integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell
CC migration through ITGB3 'Tyr-773' phosphorylation (By similarity).
CC Interacts with SDC3 (via heparan sulfate chains); this interaction
CC mediates the neurite outgrowth-promoting signal from PTN to the
CC cytoskeleton of growing neurites; this interaction mediates osteoblast
CC recruitment (PubMed:8175719, PubMed:9817766). Interacts with GPC2 (via
CC heparan sulfate); this interaction promotes neurite outgrowth through
CC binding of PTN with chondroitin sulfate of proteoglycans, thereby
CC releasing PTPRS of chondroitin sulfate proteoglycans (CSPGs) and
CC leading to binding with heparan sulfate of GPC2 (PubMed:27671118).
CC {ECO:0000250|UniProtKB:P21246, ECO:0000269|PubMed:16814777,
CC ECO:0000269|PubMed:27671118, ECO:0000269|PubMed:8175719,
CC ECO:0000269|PubMed:9817766}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:2170351). Hardly
CC expressed in bone. Abundantly expressed in the growth plate. Intensely
CC expressed in the cartilage matrix that forms the hollow for the
CC secondary ossification center. Is expressed selectively by the
CC osteocytes of the lamellar bone, whereas it is hardly expressed by
CC those of the woven bone. Is detected in the matrix surrounding the
CC osteocytes and in the canaliculi of the osteocytes. Is distributed on
CC the surface of lamellar bone (PubMed:9817766).
CC {ECO:0000269|PubMed:2170351, ECO:0000269|PubMed:9817766}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the brain in early
CC embryonic stages. Levels increase to a maximum before or just after
CC birth, and are lower in adult brain (PubMed:1768439). At E16 intensely
CC expressed in the matrix of the developing cartilage and persists in the
CC matrix of the mineralized cartilage at E20 (at protein level).
CC Localized within the unmineralized cartilage matrix (at mRNA level)
CC (PubMed:9817766). {ECO:0000269|PubMed:1768439,
CC ECO:0000269|PubMed:9817766}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P21246}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; M55601; AAA41310.1; -; mRNA.
DR EMBL; M68916; AAA41311.1; -; mRNA.
DR EMBL; BC062013; AAH62013.1; -; mRNA.
DR PIR; B37780; B37780.
DR RefSeq; NP_058762.1; NM_017066.2.
DR AlphaFoldDB; P63090; -.
DR SMR; P63090; -.
DR BioGRID; 247030; 2.
DR STRING; 10116.ENSRNOP00000016088; -.
DR PaxDb; P63090; -.
DR PRIDE; P63090; -.
DR Ensembl; ENSRNOT00000016088; ENSRNOP00000016088; ENSRNOG00000011946.
DR GeneID; 24924; -.
DR KEGG; rno:24924; -.
DR UCSC; RGD:3444; rat.
DR CTD; 5764; -.
DR RGD; 3444; Ptn.
DR eggNOG; ENOG502RXV7; Eukaryota.
DR GeneTree; ENSGT00390000007640; -.
DR HOGENOM; CLU_136864_1_0_1; -.
DR InParanoid; P63090; -.
DR OMA; PKWRERR; -.
DR OrthoDB; 1489280at2759; -.
DR PhylomeDB; P63090; -.
DR TreeFam; TF332376; -.
DR Reactome; R-RNO-201556; Signaling by ALK.
DR PRO; PR:P63090; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000011946; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P63090; RN.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISO:RGD.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IPI:RGD.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; IDA:RGD.
DR GO; GO:1904399; F:heparan sulfate binding; IPI:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; IPI:UniProtKB.
DR GO; GO:0045545; F:syndecan binding; IPI:UniProtKB.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IPI:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0034644; P:cellular response to UV; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0046697; P:decidualization; ISS:UniProtKB.
DR GO; GO:0140059; P:dendrite arborization; ISS:UniProtKB.
DR GO; GO:0031104; P:dendrite regeneration; IDA:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; IEP:RGD.
DR GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0030902; P:hindbrain development; IEP:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; IEP:RGD.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEP:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0045837; P:negative regulation of membrane potential; IDA:RGD.
DR GO; GO:0072201; P:negative regulation of mesenchymal cell proliferation; IDA:RGD.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:1904397; P:negative regulation of neuromuscular junction development; IDA:RGD.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0043932; P:ossification involved in bone remodeling; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:RGD.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IDA:RGD.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:UniProtKB.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:RGD.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
DR GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1903706; P:regulation of hemopoiesis; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0010996; P:response to auditory stimulus; ISS:UniProtKB.
DR GO; GO:1904391; P:response to ciliary neurotrophic factor; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:1904373; P:response to kainic acid; IEP:RGD.
DR GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR GO; GO:0060221; P:retinal rod cell differentiation; IMP:RGD.
DR GO; GO:1904389; P:rod bipolar cell differentiation; IEP:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0021794; P:thalamus development; IEP:RGD.
DR GO; GO:0042246; P:tissue regeneration; ISS:UniProtKB.
DR Gene3D; 2.20.60.10; -; 1.
DR Gene3D; 2.30.90.10; -; 1.
DR InterPro; IPR000762; Midkine_heparin-bd_GF.
DR InterPro; IPR020090; PTN/MK_C_dom.
DR InterPro; IPR038130; PTN/MK_C_dom_sf.
DR InterPro; IPR020091; PTN/MK_diS_sf.
DR InterPro; IPR020089; PTN/MK_N_dom.
DR InterPro; IPR037122; PTN/MK_N_dom_sf.
DR InterPro; IPR020092; PTN_MK_heparin-bd_GF_CS.
DR PANTHER; PTHR13850; PTHR13850; 1.
DR Pfam; PF01091; PTN_MK_C; 1.
DR Pfam; PF05196; PTN_MK_N; 1.
DR PRINTS; PR00269; PTNMIDKINE.
DR SMART; SM00193; PTN; 1.
DR SUPFAM; SSF57288; SSF57288; 2.
DR PROSITE; PS00619; PTN_MK_1; 1.
DR PROSITE; PS00620; PTN_MK_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Growth factor; Heparin-binding;
KW Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:2388713"
FT CHAIN 33..168
FT /note="Pleiotrophin"
FT /id="PRO_0000024661"
FT REGION 92..99
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 123..131
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 139..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..168
FT /note="Chondroitin sulfate A binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT COMPBIAS 148..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 47..76
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 55..85
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 62..89
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 99..131
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 109..141
FT /evidence="ECO:0000250|UniProtKB:P21246"
SQ SEQUENCE 168 AA; 18869 MW; 2127DA167D2DD33D CRC64;
MSSQQYQQQR RKFAAAFLAL IFILAAVDTA EAGKKEKPEK KVKKSDCGEW QWSVCVPTSG
DCGLGTREGT RTGAECKQTM KTQRCKIPCN WKKQFGAECK YQFQAWGECD LNTALKTRTG
SLKRALHNAD CQKTVTISKP CGKLTKPKPQ AESKKKKKEG KKQEKMLD
