GRPR_MOUSE
ID GRPR_MOUSE Reviewed; 384 AA.
AC P21729; Q53WV4;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Gastrin-releasing peptide receptor;
DE Short=GRP-R;
DE AltName: Full=GRP-preferring bombesin receptor;
GN Name=Grpr;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J; TISSUE=Fibroblast;
RX PubMed=1671171; DOI=10.1073/pnas.88.2.395;
RA Battey J.F., Way J.M., Corjay M.H., Shapira H., Kusano K., Harkins R.,
RA Wu J.M., Slattery T., Mann E., Feldman R.I.;
RT "Molecular cloning of the bombesin/gastrin-releasing peptide receptor from
RT Swiss 3T3 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:395-399(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SWR/J; TISSUE=Fibroblast;
RX PubMed=1707129; DOI=10.1210/mend-4-12-1956;
RA Spindel E.R., Giladi E., Brehm P., Goodman R.H., Segerson T.P.;
RT "Cloning and functional characterization of a complementary DNA encoding
RT the murine fibroblast bombesin/gastrin-releasing peptide receptor.";
RL Mol. Endocrinol. 4:1956-1963(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8391296; DOI=10.1007/bf02736689;
RA Giladi E., Nagalla S.R., Spindel E.R.;
RT "Molecular cloning and characterization of receptors for the mammalian
RT bombesin-like peptides.";
RL J. Mol. Neurosci. 4:41-54(1993).
RN [4] {ECO:0000312|EMBL:AAD00557.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10689196; DOI=10.1016/s0378-1119(99)00563-6;
RA Weber H.C., Jensen R.T., Battey J.F.;
RT "Molecular organization of the mouse gastrin-releasing peptide receptor
RT gene and its promoter.";
RL Gene 244:137-149(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28307.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAC28307.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9345264; DOI=10.1080/02500169708537815;
RA Wada E., Watase K., Yamada K., Ogura H., Yamano M., Inomata Y., Eguchi J.,
RA Yamamoto K., Sunday M.E., Maeno H., Mikoshiba K., Ohki-Hamazaki H.,
RA Wada K.;
RT "Generation and characterization of mice lacking gastrin-releasing peptide
RT receptor.";
RL Biochem. Biophys. Res. Commun. 239:28-33(1997).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12526815; DOI=10.1016/s0092-8674(02)01116-9;
RA Shumyatsky G.P., Tsvetkov E., Malleret G., Vronskaya S., Hatton M.,
RA Hampton L., Battey J.F., Dulac C., Kandel E.R., Bolshakov V.Y.;
RT "Identification of a signaling network in lateral nucleus of amygdala
RT important for inhibiting memory specifically related to learned fear.";
RL Cell 111:905-918(2002).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12176666; DOI=10.1677/joe.0.1740273;
RA Ladenheim E.E., Hampton L.L., Whitney A.C., White W.O., Battey J.F.,
RA Moran T.H.;
RT "Disruptions in feeding and body weight control in gastrin-releasing
RT peptide receptor deficient mice.";
RL J. Endocrinol. 174:273-281(2002).
RN [11]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17653196; DOI=10.1038/nature06029;
RA Sun Y.G., Chen Z.F.;
RT "A gastrin-releasing peptide receptor mediates the itch sensation in the
RT spinal cord.";
RL Nature 448:700-703(2007).
RN [12]
RP FUNCTION.
RX PubMed=26658875; DOI=10.1523/jneurosci.2310-15.2015;
RA Pereira P.J., Machado G.D., Danesi G.M., Canevese F.F., Reddy V.B.,
RA Pereira T.C., Bogo M.R., Cheng Y.C., Laedermann C., Talbot S., Lerner E.A.,
RA Campos M.M.;
RT "GRPR/PI3Kgamma: partners in central transmission of itch.";
RL J. Neurosci. 35:16272-16281(2015).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26855425; DOI=10.1038/nature16964;
RA Li P., Janczewski W.A., Yackle K., Kam K., Pagliardini S., Krasnow M.A.,
RA Feldman J.L.;
RT "The peptidergic control circuit for sighing.";
RL Nature 530:293-297(2016).
RN [14]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28280205; DOI=10.1126/science.aak9748;
RA Yu Y.Q., Barry D.M., Hao Y., Liu X.T., Chen Z.F.;
RT "Molecular and neural basis of contagious itch behavior in mice.";
RL Science 355:1072-1076(2017).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=34610277; DOI=10.1016/j.cell.2021.09.013;
RA Melzer S., Newmark E.R., Mizuno G.O., Hyun M., Philson A.C., Quiroli E.,
RA Righetti B., Gregory M.R., Huang K.W., Levasseur J., Tian L.,
RA Sabatini B.L.;
RT "Bombesin-like peptide recruits disinhibitory cortical circuits and
RT enhances fear memories.";
RL Cell 184:5622-5634(2021).
CC -!- FUNCTION: Receptor for gastrin-releasing peptide (GRP) (PubMed:1671171,
CC PubMed:1707129, PubMed:9345264, PubMed:12526815, PubMed:26658875).
CC Signals via association with G proteins that activate a
CC phosphatidylinositol-calcium second messenger system, resulting in Akt
CC phosphorylation (PubMed:26658875). Contributes to the regulation of
CC food intake (PubMed:12176666). Contributes to the perception of
CC prurient stimuli and transmission of itch signals in the spinal cord
CC that promote scratching behavior, but does not play a role in the
CC perception of pain (PubMed:28280205, PubMed:17653196, PubMed:26658875).
CC Contributes primarily to nonhistaminergic itch sensation
CC (PubMed:28280205). In one study, shown to act in the amygdala as part
CC of an inhibitory network which inhibits memory specifically related to
CC learned fear (PubMed:12526815). In another study, shown to contribute
CC to disinhibition of glutamatergic cells in the auditory cortex via
CC signaling on vasoactive intestinal peptide-expressing cells which leads
CC to enhanced auditory fear memories (PubMed:34610277). Contributes to
CC the induction of sighing through signaling in the pre-Botzinger
CC complex, a cluster of several thousand neurons in the ventrolateral
CC medulla responsible for inspiration during respiratory activity
CC (PubMed:26855425). {ECO:0000269|PubMed:12176666,
CC ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:1671171,
CC ECO:0000269|PubMed:1707129, ECO:0000269|PubMed:17653196,
CC ECO:0000269|PubMed:26658875, ECO:0000269|PubMed:26855425,
CC ECO:0000269|PubMed:34610277, ECO:0000269|PubMed:9345264}.
CC -!- INTERACTION:
CC P21729; P42866-9: Oprm1; NbExp=4; IntAct=EBI-6049651, EBI-6049667;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1671171,
CC ECO:0000269|PubMed:1707129}; Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in pancreas and brain (PubMed:1671171,
CC PubMed:9345264). Detected in suprachaismatic nucleus neurons
CC (PubMed:28280205). Detected in neurons in the dorsal horn of the spinal
CC cord (PubMed:17653196). Detected in inhibitory GABAergic interneurons
CC in the lateral nucleus of the amygdala (PubMed:12526815). Detected in
CC approximately 160 neurons of the pre-Botzinger complex
CC (PubMed:26855425). Within the pre-Botzinger complex, there is some
CC overlap with neurons expressing Nmbr with some cells expressing only
CC Grpr or Nmbr while some cells express both (PubMed:26855425). Detected
CC in cells throughout the cortex where it is coexpressed in most of these
CC cells with vasointestinal peptide (VIP) (PubMed:34610277).
CC {ECO:0000269|PubMed:12526815, ECO:0000269|PubMed:1671171,
CC ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:26855425,
CC ECO:0000269|PubMed:28280205, ECO:0000269|PubMed:34610277,
CC ECO:0000269|PubMed:9345264}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, are
CC viable and fertile (PubMed:9345264). They do not decrease their food
CC intake in response to gastrin-releasing peptide (PubMed:12176666). Mice
CC consume more food per meal, but the overall food intake per day remains
CC unchanged (PubMed:12176666). Still, they display increased body weight
CC relative to wild-type (PubMed:12176666). Contrary to wild-type mice,
CC their body temperature remains nearly constant when exposed to cold (4
CC degrees Celsius) after intracerebroventricular injection of gastrin-
CC releasing peptide (PubMed:9345264). Mutant mice show increased
CC locomotor activity and increased social interactions (PubMed:9345264).
CC They do not show any change in the perception of painful stimuli, but
CC show reduced scratching in response to pruritogenic treatments
CC (PubMed:17653196). Contrary to wild-type, mutant mice do not display
CC imitative scratching after observing spontaneous scratching behavior in
CC another mouse (PubMed:28280205). In one study, mutant mice display
CC normal performance in a water maze, but show decreased inhibition of
CC principal neurons by the interneurons, enhanced long-term potentiation
CC (LTP), and greater and more persistent long-term fear memory
CC (PubMed:12526815). Another study showed that mutants display reduced
CC long-term fear memory (PubMed:34610277). Reduced basal sigh rate
CC (PubMed:26855425). Conditional knockout in the auditory cortex results
CC in diminished auditory fear memories with no significant effect on
CC auditory discrimination (PubMed:34610277).
CC {ECO:0000269|PubMed:12176666, ECO:0000269|PubMed:12526815,
CC ECO:0000269|PubMed:17653196, ECO:0000269|PubMed:26855425,
CC ECO:0000269|PubMed:28280205, ECO:0000269|PubMed:34610277,
CC ECO:0000269|PubMed:9345264}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M57922; AAA75650.1; -; mRNA.
DR EMBL; M61000; AAA37744.1; -; mRNA.
DR EMBL; AH007139; AAD00557.1; -; Genomic_DNA.
DR EMBL; U84263; AAD00557.1; JOINED; Genomic_DNA.
DR EMBL; AK033473; BAC28307.1; -; mRNA.
DR EMBL; CH466571; EDL40772.1; -; Genomic_DNA.
DR EMBL; BC113145; AAI13146.1; -; mRNA.
DR CCDS; CCDS30512.1; -.
DR PIR; A39003; A39003.
DR RefSeq; NP_032203.1; NM_008177.3.
DR AlphaFoldDB; P21729; -.
DR SMR; P21729; -.
DR IntAct; P21729; 1.
DR STRING; 10090.ENSMUSP00000033730; -.
DR BindingDB; P21729; -.
DR ChEMBL; CHEMBL3596; -.
DR GuidetoPHARMACOLOGY; 39; -.
DR GlyGen; P21729; 3 sites.
DR PhosphoSitePlus; P21729; -.
DR SwissPalm; P21729; -.
DR jPOST; P21729; -.
DR PaxDb; P21729; -.
DR PRIDE; P21729; -.
DR ProteomicsDB; 271459; -.
DR Antibodypedia; 23994; 283 antibodies from 29 providers.
DR DNASU; 14829; -.
DR Ensembl; ENSMUST00000033730; ENSMUSP00000033730; ENSMUSG00000031364.
DR GeneID; 14829; -.
DR KEGG; mmu:14829; -.
DR UCSC; uc009uuu.1; mouse.
DR CTD; 2925; -.
DR MGI; MGI:95836; Grpr.
DR VEuPathDB; HostDB:ENSMUSG00000031364; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR HOGENOM; CLU_009579_6_2_1; -.
DR InParanoid; P21729; -.
DR OMA; TMINGRQ; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; P21729; -.
DR TreeFam; TF331292; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 14829; 0 hits in 74 CRISPR screens.
DR PRO; PR:P21729; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P21729; protein.
DR Bgee; ENSMUSG00000031364; Expressed in lung mesenchyme and 37 other tissues.
DR Genevisible; P21729; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004946; F:bombesin receptor activity; TAS:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0042923; F:neuropeptide binding; ISO:MGI.
DR GO; GO:0008188; F:neuropeptide receptor activity; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0061744; P:motor behavior; IMP:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; IMP:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; IMP:UniProtKB.
DR GO; GO:0036343; P:psychomotor behavior; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0043207; P:response to external biotic stimulus; IMP:UniProtKB.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR InterPro; IPR001556; Bombsn_rcpt-like.
DR InterPro; IPR001966; Gastrin_pep_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00358; BOMBESINR.
DR PRINTS; PR00640; GASTRINRELPR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..384
FT /note="Gastrin-releasing peptide receptor"
FT /id="PRO_0000069663"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54799"
FT LIPID 340
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 309
FT /note="R -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43215 MW; BF6D60387AA09A2C CRC64;
MAPNNCSHLN LDVDPFLSCN DTFNQSLSPP KMDNWFHPGF IYVIPAVYGL IIVIGLIGNI
TLIKIFCTVK SMRNVPNLFI SSLALGDLLL LVTCAPVDAS KYLADRWLFG RIGCKLIPFI
QLTSVGVSVF TLTALSADRY KAIVRPMDIQ ASHALMKICL KAALIWIVSM LLAIPEAVFS
DLHPFHVKDT NQTFISCAPY PHSNELHPKI HSMASFLVFY VIPLAIISVY YYFIARNLIQ
SAYNLPVEGN IHVKKQIESR KRLAKTVLVF VGLFAFCWLP NHVIYLYRSY HYSEVDTSML
HFVTSICARL LAFTNSCVNP FALYLLSKSF RKQFNTQLLC CQPGLMNRSH STGRSTTCMT
SFKSTNPSAT FSLINRNICH EGYV
