CNR2_MOUSE
ID CNR2_MOUSE Reviewed; 347 AA.
AC P47936; Q544H5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cannabinoid receptor 2;
DE Short=CB-2;
DE Short=CB2;
DE Short=mCB2;
GN Name=Cnr2;
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], AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=8679694; DOI=10.1016/0167-4781(96)00047-4;
RA Shire D., Calandra B., Rinaldi-Carmona M., Oustric D., Pessegue B.,
RA Cabanne O., le Fur G., Caput D., Ferrara P.;
RT "Molecular cloning, expression and function of the murine CB2 peripheral
RT cannabinoid receptor.";
RL Biochim. Biophys. Acta 1307:132-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NFS/N;
RX PubMed=9261404; DOI=10.1128/jvi.71.9.6796-6804.1997;
RA Valk P.J.M., Hol S., Vankan Y., Ihle J.N., Askew D., Jenkins N.A.,
RA Gilbert D.J., Copeland N.G., de Both N.J., Loewenberg B., Delwel R.;
RT "The genes encoding the peripheral cannabinoid receptor and alpha-L-
RT fucosidase are located near a newly identified common virus integration
RT site, Evi11.";
RL J. Virol. 71:6796-6804(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Buckley N.E., Bonner T.I.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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].
RC STRAIN=FVB/N; TISSUE=Liver;
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, AND FUNCTION.
RX PubMed=10822068; DOI=10.1016/s0014-2999(00)00211-9;
RA Buckley N.E., McCoy K.L., Mezey E., Bonner T., Zimmer A., Felder C.C.,
RA Glass M., Zimmer A.;
RT "Immunomodulation by cannabinoids is absent in mice deficient for the
RT cannabinoid CB(2) receptor.";
RL Eur. J. Pharmacol. 396:141-149(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11929767; DOI=10.1182/blood.v99.8.2786;
RA Jorda M.A., Verbakel S.E., Valk P.J.M., Vankan-Berkhoudt Y.V.,
RA Maccarrone M., Finazzi-Agro A., Loewenberg B., Delwel R.;
RT "Hematopoietic cells expressing the peripheral cannabinoid receptor migrate
RT in response to the endocannabinoid 2-arachidonoylglycerol.";
RL Blood 99:2786-2793(2002).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=12511587; DOI=10.1172/jci200316116;
RA Casanova M.L., Blazquez C., Martinez-Palacio J., Villanueva C.,
RA Fernandez-Acenero M.J., Huffman J.W., Jorcano J.L., Guzman M.;
RT "Inhibition of skin tumor growth and angiogenesis in vivo by activation of
RT cannabinoid receptors.";
RL J. Clin. Invest. 111:43-50(2003).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16924491; DOI=10.1007/s00251-006-0138-x;
RA Ziring D., Wei B., Velazquez P., Schrage M., Buckley N.E., Braun J.;
RT "Formation of B and T cell subsets require the cannabinoid receptor CB2.";
RL Immunogenetics 58:714-725(2006).
RN [12]
RP FUNCTION.
RX PubMed=16563625; DOI=10.1016/j.pain.2005.12.018;
RA Ibrahim M.M., Rude M.L., Stagg N.J., Mata H.P., Lai J., Vanderah T.W.,
RA Porreca F., Buckley N.E., Makriyannis A., Malan T.P. Jr.;
RT "CB2 cannabinoid receptor mediation of antinociception.";
RL Pain 122:36-42(2006).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16407142; DOI=10.1073/pnas.0504187103;
RA Ofek O., Karsak M., Leclerc N., Fogel M., Frenkel B., Wright K., Tam J.,
RA Attar-Namdar M., Kram V., Shohami E., Mechoulam R., Zimmer A., Bab I.;
RT "Peripheral cannabinoid receptor, CB2, regulates bone mass.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:696-701(2006).
RN [14]
RP FUNCTION.
RX PubMed=17401376; DOI=10.1038/nm1561;
RA Maresz K., Pryce G., Ponomarev E.D., Marsicano G., Croxford J.L.,
RA Shriver L.P., Ledent C., Cheng X., Carrier E.J., Mann M.K., Giovannoni G.,
RA Pertwee R.G., Yamamura T., Buckley N.E., Hillard C.J., Lutz B., Baker D.,
RA Dittel B.N.;
RT "Direct suppression of CNS autoimmune inflammation via the cannabinoid
RT receptor CB1 on neurons and CB2 on autoreactive T cells.";
RL Nat. Med. 13:492-497(2007).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18286196; DOI=10.1371/journal.pone.0001640;
RA Onaivi E.S., Ishiguro H., Gong J.-P., Patel S., Meozzi P.A., Myers L.,
RA Perchuk A., Mora Z., Tagliaferro P.A., Gardner E., Brusco A.,
RA Akinshola B.E., Hope B., Lujilde J., Inada T., Iwasaki S., Macharia D.,
RA Teasenfitz L., Arinami T., Uhl G.R.;
RT "Brain neuronal CB2 cannabinoid receptors in drug abuse and depression:
RT from mice to human subjects.";
RL PLoS ONE 3:E1640-E1640(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336 AND THR-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Heterotrimeric G protein-coupled receptor for endocannabinoid
CC 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May
CC function in inflammatory response, nociceptive transmission and bone
CC homeostasis. {ECO:0000269|PubMed:10822068, ECO:0000269|PubMed:11929767,
CC ECO:0000269|PubMed:16407142, ECO:0000269|PubMed:16563625,
CC ECO:0000269|PubMed:16924491, ECO:0000269|PubMed:17401376,
CC ECO:0000269|PubMed:18286196, ECO:0000269|PubMed:8679694}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
CC Perikaryon {ECO:0000250}. Note=Localizes to apical dendrite of
CC pyramidal neurons. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by cells of hematopoietic origin.
CC Expressed in skin in suprabasal layers and hair follicles, in brain by
CC neurons and glial cells and by osteoblasts, osteocytes, osteoclasts (at
CC protein level). {ECO:0000269|PubMed:11929767,
CC ECO:0000269|PubMed:12511587, ECO:0000269|PubMed:16407142,
CC ECO:0000269|PubMed:16924491, ECO:0000269|PubMed:18286196}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are responsive to the psychotropic
CC effects of cannabinoid but not to the cannabinoid-induced
CC immunomodulation. They also show accelerated age-related trabecular
CC bone loss and cortical expansion. {ECO:0000269|PubMed:10822068}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X86405; CAA60159.1; -; mRNA.
DR EMBL; X93168; CAA63655.1; -; mRNA.
DR EMBL; U21681; AAA63757.1; -; Genomic_DNA.
DR EMBL; AK036658; BAC29520.1; -; mRNA.
DR EMBL; AK037898; BAC29894.1; -; mRNA.
DR EMBL; AK134109; BAE22017.1; -; mRNA.
DR EMBL; AL672076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL29965.1; -; Genomic_DNA.
DR EMBL; BC024052; AAH24052.1; -; mRNA.
DR CCDS; CCDS18793.1; -.
DR PIR; S70364; S70364.
DR RefSeq; NP_001292207.1; NM_001305278.1.
DR RefSeq; NP_034054.3; NM_009924.4.
DR AlphaFoldDB; P47936; -.
DR SMR; P47936; -.
DR BioGRID; 198794; 1.
DR IntAct; P47936; 2.
DR STRING; 10090.ENSMUSP00000095454; -.
DR BindingDB; P47936; -.
DR ChEMBL; CHEMBL5373; -.
DR DrugCentral; P47936; -.
DR GuidetoPHARMACOLOGY; 57; -.
DR GlyGen; P47936; 1 site.
DR iPTMnet; P47936; -.
DR PhosphoSitePlus; P47936; -.
DR MaxQB; P47936; -.
DR PaxDb; P47936; -.
DR PRIDE; P47936; -.
DR ProteomicsDB; 283658; -.
DR Antibodypedia; 4047; 491 antibodies from 41 providers.
DR DNASU; 12802; -.
DR Ensembl; ENSMUST00000068830; ENSMUSP00000069957; ENSMUSG00000062585.
DR Ensembl; ENSMUST00000097843; ENSMUSP00000095454; ENSMUSG00000062585.
DR GeneID; 12802; -.
DR KEGG; mmu:12802; -.
DR UCSC; uc008vhh.3; mouse.
DR CTD; 1269; -.
DR MGI; MGI:104650; Cnr2.
DR VEuPathDB; HostDB:ENSMUSG00000062585; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_7_0_1; -.
DR InParanoid; P47936; -.
DR OMA; CNFVNFH; -.
DR OrthoDB; 822074at2759; -.
DR PhylomeDB; P47936; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 12802; 2 hits in 59 CRISPR screens.
DR ChiTaRS; Cnr2; mouse.
DR PRO; PR:P47936; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P47936; protein.
DR Bgee; ENSMUSG00000062585; Expressed in granulocyte and 75 other tissues.
DR Genevisible; P47936; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004949; F:cannabinoid receptor activity; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038171; P:cannabinoid signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR GO; GO:0045759; P:negative regulation of action potential; ISO:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0033004; P:negative regulation of mast cell activation; ISO:MGI.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISO:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR InterPro; IPR001551; Canbinoid_rcpt_2.
DR InterPro; IPR002230; Cnbnoid_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR22750:SF10; PTHR22750:SF10; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00523; CANABINOID2R.
DR PRINTS; PR00362; CANNABINOIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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; Cell projection; G-protein coupled receptor; Glycoprotein;
KW Inflammatory response; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Cannabinoid receptor 2"
FT /id="PRO_0000069324"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..301
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 326..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 64
FT /note="L -> V (in Ref. 2; CAA63655)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="L -> V (in Ref. 2; CAA63655)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> M (in Ref. 3; AAA63757)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="G -> A (in Ref. 3; AAA63757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38213 MW; 10747611D41FF442 CRC64;
MEGCRETEVT NGSNGGLEFN PMKEYMILSS GQQIAVAVLC TLMGLLSALE NMAVLYIILS
SRRLRRKPSY LFISSLAGAD FLASVIFACN FVIFHVFHGV DSNAIFLLKI GSVTMTFTAS
VGSLLLTAVD RYLCLCYPPT YKALVTRGRA LVALCVMWVL SALISYLPLM GWTCCPSPCS
ELFPLIPNDY LLGWLLFIAI LFSGIIYTYG YVLWKAHRHV ATLAEHQDRQ VPGIARMRLD
VRLAKTLGLV LAVLLICWFP ALALMGHSLV TTLSDQVKEA FAFCSMLCLV NSMVNPIIYA
LRSGEIRSAA QHCLIGWKKY LQGLGPEGKE EGPRSSVTET EADVKTT
