GLRB_MOUSE
ID GLRB_MOUSE Reviewed; 496 AA.
AC P48168; Q5U5X3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glycine receptor subunit beta;
DE AltName: Full=Glycine receptor 58 kDa subunit;
DE Flags: Precursor;
GN Name=Glrb;
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], DISEASE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7920630; DOI=10.1038/ng0694-136;
RA Kingsmore S.F., Giros B., Suh D., Bieniarz M., Caron M.G., Seldin M.F.;
RT "Glycine receptor beta-subunit gene mutation in spastic mouse associated
RT with LINE-1 element insertion.";
RL Nat. Genet. 7:136-141(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS SPASTIC, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Brain, and Liver;
RX PubMed=7946325; DOI=10.1016/0896-6273(94)90265-8;
RA Muelhardt C., Fischer M., Gass P., Simon-Chazottes D., Guenet J.-L.,
RA Kuhse J., Betz H., Becker C.M.;
RT "The spastic mouse: aberrant splicing of glycine receptor beta subunit mRNA
RT caused by intronic insertion of L1 element.";
RL Neuron 13:1003-1015(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP DISEASE, AND FUNCTION.
RX PubMed=12809985; DOI=10.1016/s0304-3940(03)00499-3;
RA von Wegerer J., Becker K., Glockenhammer D., Becker C.M., Zeilhofer H.U.,
RA Swandulla D.;
RT "Spinal inhibitory synaptic transmission in the glycine receptor mouse
RT mutant spastic.";
RL Neurosci. Lett. 345:45-48(2003).
RN [7]
RP DISEASE, AND FUNCTION.
RX PubMed=16672662; DOI=10.1523/jneurosci.3991-05.2006;
RA Graham B.A., Schofield P.R., Sah P., Margrie T.W., Callister R.J.;
RT "Distinct physiological mechanisms underlie altered glycinergic synaptic
RT transmission in the murine mutants spastic, spasmodic, and oscillator.";
RL J. Neurosci. 26:4880-4890(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19723286; DOI=10.1111/j.1460-9568.2009.06903.x;
RA Eichler S.A., Foerstera B., Smolinsky B., Juettner R., Lehmann T.N.,
RA Faehling M., Schwarz G., Legendre P., Meier J.C.;
RT "Splice-specific roles of glycine receptor alpha3 in the hippocampus.";
RL Eur. J. Neurosci. 30:1077-1091(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22592841; DOI=10.1002/cne.23139;
RA Weltzien F., Puller C., O'Sullivan G.A., Paarmann I., Betz H.;
RT "Distribution of the glycine receptor beta-subunit in the mouse CNS as
RT revealed by a novel monoclonal antibody.";
RL J. Comp. Neurol. 520:3962-3981(2012).
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. GLRB
CC does not form ligand-gated ion channels by itself, but is part of
CC heteromeric ligand-gated chloride channels. Channel opening is
CC triggered by extracellular glycine (PubMed:12809985). Heteropentameric
CC channels composed of GLRB and GLRA1 are activated by lower glycine
CC levels than homopentameric GLRA1. Plays an important role in the down-
CC regulation of neuronal excitability. Contributes to the generation of
CC inhibitory postsynaptic currents (PubMed:12809985, PubMed:16672662).
CC {ECO:0000250|UniProtKB:P48167, ECO:0000269|PubMed:12809985,
CC ECO:0000269|PubMed:16672662}.
CC -!- SUBUNIT: Heteropentamer composed of GLRB and GLRA1. Heteropentamer
CC composed of GLRB and GLRA2. Heteropentamer composed of GLRB and GLRA3.
CC Heteropentamer composed of two GLRA1 and three GLRB subunits.
CC Heteropentamer composed of three GLRA1 and two GLRB subunits. Interacts
CC with GPHN. {ECO:0000250|UniProtKB:P48167}.
CC -!- INTERACTION:
CC P48168; Q8BUV3: Gphn; NbExp=4; IntAct=EBI-7069198, EBI-771218;
CC P48168; Q03555: Gphn; Xeno; NbExp=4; IntAct=EBI-7069198, EBI-349317;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:22592841}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000269|PubMed:19723286,
CC ECO:0000269|PubMed:22592841}. Cell projection, dendrite
CC {ECO:0000269|PubMed:19723286}. Cell membrane
CC {ECO:0000269|PubMed:12809985}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Cytoplasm
CC {ECO:0000250|UniProtKB:P48167}. Note=Retained in the cytoplasm upon
CC heterologous expression by itself. Coexpression with GPHN promotes
CC expression at the cell membrane. Coexpression with GLRA1, GLRA2 or
CC GLRA3 promotes expression at the cell membrane.
CC {ECO:0000250|UniProtKB:P20781}.
CC -!- TISSUE SPECIFICITY: Detected in spinal cord, brain and brain stem,
CC especially in the periolivary region, spinal nuclei, trigeminal
CC nucleus, medulla oblongata, pons and midbrain. Detected in the inner
CC plexiform layer of the retina (at protein level) (PubMed:22592841).
CC High levels of expression in cortex, hippocampus, thalamus and
CC cerebellum (PubMed:7920630). Detected in spinal cord (PubMed:7946325).
CC {ECO:0000269|PubMed:22592841, ECO:0000269|PubMed:7920630,
CC ECO:0000269|PubMed:7946325}.
CC -!- DISEASE: Note=Defects in Glrb cause the spastic condition which is
CC characterized by muscle rigidity, tremors, myoclonic jerks, pronounced
CC startle reaction, abnormal gait and impaired righting ability
CC (PubMed:7920630). Neurons from the ventral horn of the spinal cord
CC display reduced inhibitory postsynaptic currents (PubMed:12809985).
CC Likewise, hypoglossal neurons display a dramatic reduction in the
CC frequency and amplitude of postsynaptic inhibitory currents
CC (PubMed:16672662). {ECO:0000269|PubMed:12809985,
CC ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7920630}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRB sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; U09399; AAA61874.1; -; mRNA.
DR EMBL; X81202; CAA57076.1; -; mRNA.
DR EMBL; X81201; CAA57075.1; -; Genomic_DNA.
DR EMBL; L32594; AAA65966.1; -; Genomic_DNA.
DR EMBL; AK083251; BAC38831.1; -; mRNA.
DR EMBL; CH466547; EDL15445.1; -; Genomic_DNA.
DR EMBL; BC037605; AAH37605.1; -; mRNA.
DR CCDS; CCDS17424.1; -.
DR PIR; S46459; S46459.
DR RefSeq; NP_001268898.1; NM_001281969.2.
DR RefSeq; NP_001332884.1; NM_001345955.1.
DR RefSeq; NP_001332885.1; NM_001345956.1.
DR RefSeq; NP_001332886.1; NM_001345957.1.
DR RefSeq; NP_001332887.1; NM_001345958.1.
DR RefSeq; NP_001332888.1; NM_001345959.1.
DR RefSeq; NP_001332925.1; NM_001345996.1.
DR RefSeq; NP_034428.2; NM_010298.6.
DR AlphaFoldDB; P48168; -.
DR SMR; P48168; -.
DR BioGRID; 199953; 1.
DR IntAct; P48168; 5.
DR MINT; P48168; -.
DR STRING; 10090.ENSMUSP00000029654; -.
DR GlyConnect; 2356; 2 N-Linked glycans (1 site).
DR GlyGen; P48168; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P48168; -.
DR PhosphoSitePlus; P48168; -.
DR PaxDb; P48168; -.
DR PRIDE; P48168; -.
DR ProteomicsDB; 267458; -.
DR Antibodypedia; 66124; 184 antibodies from 28 providers.
DR DNASU; 14658; -.
DR Ensembl; ENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
DR GeneID; 14658; -.
DR KEGG; mmu:14658; -.
DR UCSC; uc008pog.2; mouse.
DR CTD; 2743; -.
DR MGI; MGI:95751; Glrb.
DR VEuPathDB; HostDB:ENSMUSG00000028020; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000156344; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P48168; -.
DR OMA; KFFWGIL; -.
DR OrthoDB; 614790at2759; -.
DR PhylomeDB; P48168; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 14658; 2 hits in 72 CRISPR screens.
DR PRO; PR:P48168; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P48168; protein.
DR Bgee; ENSMUSG00000028020; Expressed in lateral geniculate body and 213 other tissues.
DR ExpressionAtlas; P48168; baseline and differential.
DR Genevisible; P48168; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:MGI.
DR GO; GO:0016935; C:glycine-gated chloride channel complex; ISS:UniProtKB.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IMP:MGI.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; ISS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IMP:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IGI:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR008060; Glycine_rcpt_B.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR PANTHER; PTHR18945:SF29; PTHR18945:SF29; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01677; GLYRBETA.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Chloride; Chloride channel; Cytoplasm;
KW Disease variant; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..496
FT /note="Glycine receptor subunit beta"
FT /id="PRO_0000000424"
FT TOPO_DOM 23..268
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 269..290
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 291..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 296..316
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 317..327
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 328..348
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 349..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 475..495
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT REGION 32..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..253
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT SITE 307
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20781"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 243..255
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT VARIANT 74..83
FT /note="NFKGIPVDVV -> TTMLDIQPMI (in spastic 1)"
FT /evidence="ECO:0000269|PubMed:7946325"
FT VARIANT 84..496
FT /note="Missing (in spastic 1)"
FT /evidence="ECO:0000269|PubMed:7946325"
FT VARIANT 143..151
FT /note="LFFANEKSA -> VSMSWIYNR (in spastic 2)"
FT /evidence="ECO:0000269|PubMed:7946325"
FT VARIANT 152..496
FT /note="Missing (in spastic 2)"
FT /evidence="ECO:0000269|PubMed:7946325"
FT CONFLICT 365
FT /note="A -> R (in Ref. 1; AAA61874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 55951 MW; 554840A6DE9DE7BE CRC64;
MKFSLAISFF ILMSLLFEDA CAKEKSSKKG KGKKKQYLCP SQQSPEDLAR VPPNSTSNIL
NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD YRVNIFLRQK WNDPRLKLPS
DFRGSDALTV DPTMYKCLWK PDLFFANEKS ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT
LSCPLDLTLF PMDTQRCKMQ LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY
GNCTKYYKGT GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP
LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV QVMLNNPKRV
EAEKARIAKA EQADGKGGNA AKKNTVNGTG TPVHISTLQV GETRCKKVCT SKSDLRSNDF
SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK PQAKNKKPPP AKPVIPTAAK RIDLYARALF
PFCFLFFNVI YWSIYL
