VGF_RAT
ID VGF_RAT Reviewed; 617 AA.
AC P20156;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Neurosecretory protein VGF;
DE AltName: Full=VGF8a protein;
DE Contains:
DE RecName: Full=VGF(24-63);
DE Contains:
DE RecName: Full=VGF(180-194);
DE Contains:
DE RecName: Full=VGF(375-407);
DE Contains:
DE RecName: Full=Neuroendocrine regulatory peptide-1;
DE Short=NERP-1;
DE Contains:
DE RecName: Full=Neuroendocrine regulatory peptide-2;
DE Short=NERP-2;
DE Contains:
DE RecName: Full=VGF-derived peptide TLQP-11;
DE Contains:
DE RecName: Full=VGF-derived peptide TLQP-21;
DE Contains:
DE RecName: Full=VGF-derived peptide TLQP-30;
DE Contains:
DE RecName: Full=VGF-derived peptide TLQP-62;
DE Contains:
DE RecName: Full=VGF-derived peptide HFHH-10;
DE Contains:
DE RecName: Full=VGF-derived peptide AQEE-30;
DE Contains:
DE RecName: Full=VGF-derived peptide LQEQ-19;
DE Flags: Precursor;
GN Name=Vgf;
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].
RX PubMed=2676516; DOI=10.1002/j.1460-2075.1989.tb08345.x;
RA Possenti R., Eldridge J.D., Paterson B.M., Grasso A., Levi A.;
RT "A protein induced by NGF in PC12 cells is stored in secretory vesicles and
RT released through the regulated pathway.";
RL EMBO J. 8:2217-2223(1989).
RN [2]
RP SEQUENCE REVISION.
RA Possenti R.;
RL Submitted (OCT-1995) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2017159; DOI=10.1128/mcb.11.5.2335-2349.1991;
RA Salton S.R.J., Fischberg D.J., Dong K.-W.;
RT "Structure of the gene encoding VGF, a nervous system-specific mRNA that is
RT rapidly and selectively induced by nerve growth factor in PC12 cells.";
RL Mol. Cell. Biol. 11:2335-2349(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1377233; DOI=10.1523/jneurosci.12-07-02573.1992;
RA Hawley R.J., Scheibe R.J., Wagner J.A.;
RT "NGF induces the expression of the VGF gene through a cAMP response
RT element.";
RL J. Neurosci. 12:2573-2581(1992).
RN [5]
RP FUNCTION (NEUROSECRETORY PROTEIN VGF).
RX PubMed=7595538; DOI=10.1046/j.1471-4159.1995.65062441.x;
RA Trani E., Ciotti T., Rinaldi A.M., Canu N., Ferri G.L., Levi A.,
RA Possenti R.;
RT "Tissue-specific processing of the neuroendocrine protein VGF.";
RL J. Neurochem. 65:2441-2449(1995).
RN [6]
RP FUNCTION (NEUROSECRETORY PROTEIN VGF), AND TISSUE SPECIFICITY.
RX PubMed=12065665; DOI=10.1046/j.1471-4159.2002.00842.x;
RA Trani E., Giorgi A., Canu N., Amadoro G., Rinaldi A.M., Halban P.A.,
RA Ferri G.L., Possenti R., Schinina M.E., Levi A.;
RT "Isolation and characterization of VGF peptides in rat brain. Role of PC1/3
RT and PC2 in the maturation of VGF precursor.";
RL J. Neurochem. 81:565-574(2002).
RN [7]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-21).
RX PubMed=16983076; DOI=10.1073/pnas.0606102103;
RA Bartolomucci A., La Corte G., Possenti R., Locatelli V., Rigamonti A.E.,
RA Torsello A., Bresciani E., Bulgarelli I., Rizzi R., Pavone F.,
RA D'Amato F.R., Severini C., Mignogna G., Giorgi A., Schinina M.E., Elia G.,
RA Brancia C., Ferri G.L., Conti R., Ciani B., Pascucci T., Dell'Omo G.,
RA Muller E.E., Levi A., Moles A.;
RT "TLQP-21, a VGF-derived peptide, increases energy expenditure and prevents
RT the early phase of diet-induced obesity.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14584-14589(2006).
RN [8]
RP PROTEIN SEQUENCE OF 24-63; 180-194 AND 375-407, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-180.
RC STRAIN=Wistar; TISSUE=Corpus striatum;
RX PubMed=19164277; DOI=10.1074/mcp.m800501-mcp200;
RA Bernay B., Gaillard M.-C., Guryca V., Emadali A., Kuhn L., Bertrand A.,
RA Detraz I., Carcenac C., Savasta M., Brouillet E., Garin J., Elalouf J.-M.;
RT "Discovering new bioactive neuropeptides in the striatum secretome using in
RT vivo microdialysis and versatile proteomics.";
RL Mol. Cell. Proteomics 8:946-958(2009).
RN [9]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-21).
RX PubMed=19466987; DOI=10.1111/j.1476-5381.2009.00192.x;
RA Severini C., La Corte G., Improta G., Broccardo M., Agostini S.,
RA Petrella C., Sibilia V., Pagani F., Guidobono F., Bulgarelli I.,
RA Ferri G.L., Brancia C., Rinaldi A.M., Levi A., Possenti R.;
RT "In vitro and in vivo pharmacological role of TLQP-21, a VGF-derived
RT peptide, in the regulation of rat gastric motor functions.";
RL Br. J. Pharmacol. 157:984-993(2009).
RN [10]
RP FUNCTION (NEUROENDOCRINE REGULATORY PEPTIDE-1), FUNCTION (NEUROENDOCRINE
RP REGULATORY PEPTIDE-2), PYROGLUTAMATE FORMATION AT GLN-313, AND TISSUE
RP SPECIFICITY.
RX PubMed=19194657; DOI=10.1007/s00018-009-8796-0;
RA Toshinai K., Nakazato M.;
RT "Neuroendocrine regulatory peptide-1 and -2: novel bioactive peptides
RT processed from VGF.";
RL Cell. Mol. Life Sci. 66:1939-1945(2009).
RN [11]
RP FUNCTION (NEUROENDOCRINE REGULATORY PEPTIDE-2).
RX PubMed=20551287; DOI=10.1152/ajpendo.00768.2009;
RA Toshinai K., Yamaguchi H., Kageyama H., Matsuo T., Koshinaka K., Sasaki K.,
RA Shioda S., Minamino N., Nakazato M.;
RT "Neuroendocrine regulatory peptide-2 regulates feeding behavior via the
RT orexin system in the hypothalamus.";
RL Am. J. Physiol. 299:E394-E401(2010).
RN [12]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-21), AND INTERACTION WITH C3AR1
RP (VGF-DERIVED PEPTIDE TLQP-21).
RX PubMed=23940034; DOI=10.1074/jbc.m113.497214;
RA Hannedouche S., Beck V., Leighton-Davies J., Beibel M., Roma G.,
RA Oakeley E.J., Lannoy V., Bernard J., Hamon J., Barbieri S., Preuss I.,
RA Lasbennes M.C., Sailer A.W., Suply T., Seuwen K., Parker C.N.,
RA Bassilana F.;
RT "Identification of the C3a receptor (C3AR1) as the target of the VGF-
RT derived peptide TLQP-21 in rodent cells.";
RL J. Biol. Chem. 288:27434-27443(2013).
RN [13]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-21), AND INTERACTION WITH C1QBP
RP (VGF-DERIVED PEPTIDE TLQP-21).
RX PubMed=24106277; DOI=10.1074/jbc.m113.510917;
RA Chen Y.C., Pristera A., Ayub M., Swanwick R.S., Karu K., Hamada Y.,
RA Rice A.S., Okuse K.;
RT "Identification of a receptor for neuropeptide VGF and its role in
RT neuropathic pain.";
RL J. Biol. Chem. 288:34638-34646(2013).
RN [14]
RP FUNCTION (NEUROENDOCRINE REGULATORY PEPTIDE-1), AND FUNCTION
RP (NEUROENDOCRINE REGULATORY PEPTIDE-2).
RX PubMed=24704271; DOI=10.1016/j.brainres.2014.03.038;
RA Toshinai K., Saito T., Yamaguchi H., Sasaki K., Tsuchimochi W.,
RA Minamino N., Ueta Y., Nakazato M.;
RT "Neuroendocrine regulatory peptide-1 and -2 (NERPs) inhibit the
RT excitability of magnocellular neurosecretory cells in the hypothalamus.";
RL Brain Res. 1563:52-60(2014).
RN [15]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-62).
RX PubMed=25917832; DOI=10.1530/jme-14-0313;
RA Petrocchi-Passeri P., Cero C., Cutarelli A., Frank C., Severini C.,
RA Bartolomucci A., Possenti R.;
RT "The VGF-derived peptide TLQP-62 modulates insulin secretion and glucose
RT homeostasis.";
RL J. Mol. Endocrinol. 54:227-239(2015).
RN [16]
RP FUNCTION (NEUROENDOCRINE REGULATORY PEPTIDE-2).
RX PubMed=28213131; DOI=10.1016/j.bbrc.2017.02.064;
RA Namkoong C., Toshinai K., Waise T.M.Z., Sakoda H., Sasaki K., Ueta Y.,
RA Kim M.S., Minamino N., Nakazato M.;
RT "NERP-2 regulates gastric acid secretion and gastric emptying via the
RT orexin pathway.";
RL Biochem. Biophys. Res. Commun. 485:409-413(2017).
RN [17]
RP FUNCTION (VGF-DERIVED PEPTIDE TLQP-21).
RX PubMed=28123945; DOI=10.1016/j.molmet.2016.10.005;
RA Cero C., Razzoli M., Han R., Sahu B.S., Patricelli J., Guo Z.,
RA Zaidman N.A., Miles J.M., O'Grady S.M., Bartolomucci A.;
RT "The neuropeptide TLQP-21 opposes obesity via C3aR1-mediated enhancement of
RT adrenergic-induced lipolysis.";
RL Mol. Metab. 6:148-158(2017).
CC -!- FUNCTION: [Neurosecretory protein VGF]: Secreted polyprotein that is
CC packaged and proteolytically processed by prohormone convertases PCSK1
CC and PCSK2 in a cell-type-specific manner (PubMed:12065665,
CC PubMed:7595538). VGF and peptides derived from its processing play many
CC roles in neurogenesis and neuroplasticity associated with learning,
CC memory, depression and chronic pain (By similarity).
CC {ECO:0000250|UniProtKB:Q0VGU4, ECO:0000269|PubMed:12065665,
CC ECO:0000269|PubMed:7595538}.
CC -!- FUNCTION: [Neuroendocrine regulatory peptide-1]: Plays a role in the
CC control of body fluid homeostasis by regulating vasopressin release.
CC Suppresses presynaptic glutamatergic neurons connected to vasopressin
CC neurons. {ECO:0000269|PubMed:24704271}.
CC -!- FUNCTION: [Neuroendocrine regulatory peptide-2]: Plays a role in the
CC control of body fluid homeostasis by regulating vasopressin release.
CC Activates GABAergic interneurons which are inhibitory neurons of the
CC nervous system and thereby suppresses presynaptic glutamatergic neurons
CC (PubMed:24704271). Stimulates also feeding behavior in an orexin-
CC dependent manner in the hypothalamus (PubMed:20551287). Functions as a
CC positive regulator for the activation of orexin neurons resulting in
CC elevated gastric acid secretion and gastric emptying (PubMed:28213131).
CC {ECO:0000269|PubMed:20551287, ECO:0000269|PubMed:24704271,
CC ECO:0000269|PubMed:28213131}.
CC -!- FUNCTION: [VGF-derived peptide TLQP-21]: Secreted multifunctional
CC neuropeptide that binds to different cell receptors and thereby plays
CC multiple physiological roles including modulation of energy
CC expenditure, pain, response to stress, gastric regulation, glucose
CC homeostasis as well as lipolysis (PubMed:28123945, PubMed:16983076).
CC Activates the G-protein-coupled receptor C3AR1 via a folding-upon-
CC binding mechanism leading to enhanced lipolysis in adipocytes
CC (PubMed:23940034, PubMed:28123945). Interacts with C1QBP receptor in
CC macrophages and microglia causing increased levels of intracellular
CC calcium and hypersensitivity (PubMed:24106277, PubMed:19466987).
CC {ECO:0000269|PubMed:16983076, ECO:0000269|PubMed:19466987,
CC ECO:0000269|PubMed:23940034, ECO:0000269|PubMed:24106277,
CC ECO:0000269|PubMed:28123945}.
CC -!- FUNCTION: [VGF-derived peptide TLQP-62]: Plays a role in the regulation
CC of memory formation and depression-related behaviors potentially by
CC influencing synaptic plasticity and neurogenesis. Induces acute and
CC transient activation of the NTRK2/TRKB receptor and subsequent CREB
CC phosphorylation (By similarity). Induces also insulin secretion in
CC insulinoma cells by increasing intracellular calcium mobilization
CC (PubMed:25917832). {ECO:0000250|UniProtKB:Q0VGU4,
CC ECO:0000269|PubMed:25917832}.
CC -!- SUBUNIT: [VGF-derived peptide TLQP-21]: Interacts with HSPA8 on cell
CC membrane (By similarity). Interacts with C3AR1 (By similarity).
CC Interacts with C1QBP (PubMed:24106277). {ECO:0000250|UniProtKB:O15240,
CC ECO:0000250|UniProtKB:Q0VGU4, ECO:0000269|PubMed:24106277}.
CC -!- SUBCELLULAR LOCATION: [Neurosecretory protein VGF]: Secreted
CC {ECO:0000250|UniProtKB:O15240}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:O15240}. Note=Stored in secretory vesicles and
CC then secreted, NERP peptides colocalize with vasopressin in the storage
CC granules of hypothalamus. {ECO:0000250|UniProtKB:O15240}.
CC -!- TISSUE SPECIFICITY: Central and peripheral nervous systems, synthesized
CC exclusively in neuronal and neuroendocrine cells. VGF and several of
CC the derived peptides are present in the brain.
CC {ECO:0000269|PubMed:12065665, ECO:0000269|PubMed:19194657}.
CC -!- INDUCTION: By nerve growth factor.
CC -!- PTM: Multiple peptides are derived from VGF, with activities in
CC synaptic plasticity, antidepression, penile erection, autonomic
CC activation, and increases in energy expenditure.
CC -!- MASS SPECTROMETRY: [VGF(24-63)]: Mass=4164.694; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19164277};
CC -!- MASS SPECTROMETRY: [VGF(180-194)]: Mass=1655.730; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19164277};
CC -!- MASS SPECTROMETRY: [VGF(375-407)]: Mass=3470.868; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19164277};
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DR EMBL; M60522; AAA41700.1; -; Genomic_DNA.
DR EMBL; M60525; AAA86428.1; -; mRNA.
DR EMBL; M74223; AAA42336.1; -; mRNA.
DR PIR; I56530; I56530.
DR PIR; S05381; S05381.
DR RefSeq; NP_112259.1; NM_030997.1.
DR AlphaFoldDB; P20156; -.
DR SMR; P20156; -.
DR BioGRID; 248104; 1.
DR IntAct; P20156; 1.
DR MINT; P20156; -.
DR STRING; 10116.ENSRNOP00000050024; -.
DR CarbonylDB; P20156; -.
DR iPTMnet; P20156; -.
DR PhosphoSitePlus; P20156; -.
DR jPOST; P20156; -.
DR PaxDb; P20156; -.
DR PRIDE; P20156; -.
DR Ensembl; ENSRNOT00000041808; ENSRNOP00000050024; ENSRNOG00000001416.
DR GeneID; 29461; -.
DR KEGG; rno:29461; -.
DR UCSC; RGD:69399; rat.
DR CTD; 7425; -.
DR RGD; 69399; Vgf.
DR eggNOG; ENOG502S5N4; Eukaryota.
DR GeneTree; ENSGT00390000017745; -.
DR InParanoid; P20156; -.
DR OrthoDB; 1064302at2759; -.
DR PhylomeDB; P20156; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P20156; -.
DR Proteomes; UP000002494; Chromosome 12.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISO:RGD.
DR GO; GO:0033500; P:carbohydrate homeostasis; IBA:GO_Central.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; TAS:RGD.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0043084; P:penile erection; IDA:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IDA:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; ISO:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0019953; P:sexual reproduction; ISO:RGD.
DR InterPro; IPR026128; VGF.
DR PANTHER; PTHR15159; PTHR15159; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Growth factor; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..617
FT /note="Neurosecretory protein VGF"
FT /id="PRO_0000022656"
FT PEPTIDE 24..63
FT /note="VGF(24-63)"
FT /id="PRO_0000375995"
FT PEPTIDE 180..194
FT /note="VGF(180-194)"
FT /id="PRO_0000375996"
FT PEPTIDE 285..309
FT /note="Neuroendocrine regulatory peptide-1"
FT /id="PRO_0000403366"
FT PEPTIDE 313..350
FT /note="Neuroendocrine regulatory peptide-2"
FT /id="PRO_0000403367"
FT PEPTIDE 375..407
FT /note="VGF(375-407)"
FT /id="PRO_0000375997"
FT PEPTIDE 556..617
FT /note="VGF-derived peptide TLQP-62"
FT /id="PRO_0000403368"
FT PEPTIDE 556..587
FT /note="VGF-derived peptide TLQP-30"
FT /id="PRO_0000403369"
FT PEPTIDE 556..576
FT /note="VGF-derived peptide TLQP-21"
FT /id="PRO_0000403370"
FT PEPTIDE 556..566
FT /note="VGF-derived peptide TLQP-11"
FT /id="PRO_0000403371"
FT PEPTIDE 567..576
FT /note="VGF-derived peptide HFHH-10"
FT /id="PRO_0000403372"
FT PEPTIDE 588..617
FT /note="VGF-derived peptide AQEE-30"
FT /id="PRO_0000403373"
FT PEPTIDE 599..617
FT /note="VGF-derived peptide LQEQ-19"
FT /id="PRO_0000403374"
FT REGION 29..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 180
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:19164277"
FT MOD_RES 313
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:19194657"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15240"
FT CONFLICT 342
FT /note="G -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 68179 MW; 5E23E47DF460C7B4 CRC64;
MKTFTLPASV LFCFLLLIRG LGAAPPGRSD VYPPPLGSEH NGQVAEDAVS RPKDDSVPEV
RAARNSEPQD QGELFQGVDP RALAAVLLQA LDRPASPPAV PAGSQQGTPE EAAEALLTES
VRSQTHSLPA SEIQASAVAP PRPQTQDNDP EADDRSEELE ALASLLQELR DFSPSNAKRQ
QETAAAETET RTHTLTRVNL ESPGPERVWR ASWGEFQARV PERAPLPPSV PSQFQARMSE
NVPLPETHQF GEGVSSPKTH LGETLTPLSK AYQSLSAPFP KVRRLEGSFL GGSEAGERLL
QQGLAQVEAG RRQAEATRQA AAQEERLADL ASDLLLQYLL QGGARQRDLG GRGLQETQQE
RENEREEEAE QERRGGGEDE VGEEDEEAAE AEAEAEEAER ARQNALLFAE EEDGEAGAED
KRSQEEAPGH RRKDAEGTEE GGEEDDDDEE MDPQTIDSLI ELSTKLHLPA DDVVSIIEEV
EEKRKRKKNA PPEPVPPPRA APAPTHVRSP QPPPPAPARD ELPDWNEVLP PWDREEDEVF
PPGPYHPFPN YIRPRTLQPP ASSRRRHFHH ALPPARHHPD LEAQARRAQE EADAEERRLQ
EQEELENYIE HVLLHRP
