ID   PAQR2_MOUSE             Reviewed;         386 AA.
AC   Q8BQS5; Q8CA45; Q8CID6;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Adiponectin receptor protein 2 {ECO:0000303|PubMed:12802337};
DE   AltName: Full=Progestin and adipoQ receptor family member 2 {ECO:0000250|UniProtKB:Q86V24};
DE   AltName: Full=Progestin and adipoQ receptor family member II;
GN   Name=Adipor2 {ECO:0000312|MGI:MGI:93830};
GN   Synonyms=D6Ucla1e, Parq2 {ECO:0000250|UniProtKB:Q86V24};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Spinal cord;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12802337; DOI=10.1038/nature01705;
RA   Yamauchi T., Kamon J., Ito Y., Tsuchida A., Yokomizo T., Kita S.,
RA   Sugiyama T., Miyagishi M., Hara K., Tsunoda M., Murakami K., Ohteki T.,
RA   Uchida S., Takekawa S., Waki H., Tsuno N.H., Shibata Y., Terauchi Y.,
RA   Froguel P., Tobe K., Koyasu S., Taira K., Kitamura T., Shimizu T.,
RA   Nagai R., Kadowaki T.;
RT   "Cloning of adiponectin receptors that mediate antidiabetic metabolic
RT   effects.";
RL   Nature 423:762-769(2003).
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17327425; DOI=10.2337/db06-1432;
RA   Bjursell M., Ahnmark A., Bohlooly-Y M., William-Olsson L., Rhedin M.,
RA   Peng X.R., Ploj K., Gerdin A.K., Arnerup G., Elmgren A., Berg A.L.,
RA   Oscarsson J., Linden D.;
RT   "Opposing effects of adiponectin receptors 1 and 2 on energy metabolism.";
RL   Diabetes 56:583-593(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17068142; DOI=10.1210/en.2006-0708;
RA   Liu Y., Michael M.D., Kash S., Bensch W.R., Monia B.P., Murray S.F.,
RA   Otto K.A., Syed S.K., Bhanot S., Sloop K.W., Sullivan J.M.,
RA   Reifel-Miller A.;
RT   "Deficiency of adiponectin receptor 2 reduces diet-induced insulin
RT   resistance but promotes type 2 diabetes.";
RL   Endocrinology 148:683-692(2007).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17268472; DOI=10.1038/nm1557;
RA   Yamauchi T., Nio Y., Maki T., Kobayashi M., Takazawa T., Iwabu M.,
RA   Okada-Iwabu M., Kawamoto S., Kubota N., Kubota T., Ito Y., Kamon J.,
RA   Tsuchida A., Kumagai K., Kozono H., Hada Y., Ogata H., Tokuyama K.,
RA   Tsunoda M., Ide T., Murakami K., Awazawa M., Takamoto I., Froguel P.,
RA   Hara K., Tobe K., Nagai R., Ueki K., Kadowaki T.;
RT   "Targeted disruption of AdipoR1 and AdipoR2 causes abrogation of
RT   adiponectin binding and metabolic actions.";
RL   Nat. Med. 13:332-339(2007).
RN   [7]
RP   INTERACTION WITH APPL2.
RX   PubMed=19661063; DOI=10.1074/jbc.m109.010355;
RA   Wang C., Xin X., Xiang R., Ramos F.J., Liu M., Lee H.J., Chen H., Mao X.,
RA   Kikani C.K., Liu F., Dong L.Q.;
RT   "Yin-Yang regulation of adiponectin signaling by APPL isoforms in muscle
RT   cells.";
RL   J. Biol. Chem. 284:31608-31615(2009).
RN   [8]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=24742672; DOI=10.1074/jbc.m114.548115;
RA   Parker-Duffen J.L., Nakamura K., Silver M., Zuriaga M.A., MacLauchlan S.,
RA   Aprahamian T.R., Walsh K.;
RT   "Divergent roles for adiponectin receptor 1 (AdipoR1) and AdipoR2 in
RT   mediating revascularization and metabolic dysfunction in vivo.";
RL   J. Biol. Chem. 289:16200-16213(2014).
CC   -!- FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by
CC       adipocytes that regulates glucose and lipid metabolism
CC       (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672).
CC       Required for normal body fat and glucose homeostasis (PubMed:17327425,
CC       PubMed:17068142, PubMed:17268472, PubMed:24742672). ADIPOQ-binding
CC       activates a signaling cascade that leads to increased PPARA activity,
CC       and ultimately to increased fatty acid oxidation and glucose uptake
CC       (PubMed:12802337, PubMed:17268472, PubMed:24742672). Has intermediate
CC       affinity for globular and full-length adiponectin (PubMed:12802337).
CC       Required for normal revascularization after chronic ischemia caused by
CC       severing of blood vessels (PubMed:24742672).
CC       {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:17068142,
CC       ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425,
CC       ECO:0000269|PubMed:24742672}.
CC   -!- SUBUNIT: May form homooligomers and heterooligomers with ADIPOR1 (By
CC       similarity). Interacts with APPL2 (via BAR domain); ADIPOQ dissociates
CC       this interaction (PubMed:19661063). {ECO:0000250|UniProtKB:Q86V24,
CC       ECO:0000269|PubMed:19661063}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86V24};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86V24}.
CC       Note=Localized to the cell membrane and intracellular organelles.
CC       {ECO:0000250|UniProtKB:Q86V24}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BQS5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BQS5-2; Sequence=VSP_008887, VSP_008888;
CC   -!- TISSUE SPECIFICITY: Detected in liver and quadriceps muscle (at protein
CC       level) (PubMed:17327425). Highly expressed in liver (PubMed:12802337).
CC       Highly expressed in white adipose tissue, and at intermediate levels in
CC       brown adipose tissue (PubMed:24742672). Expressed at intermediate level
CC       in heart, kidney, lung and skeletal muscle. Weakly expressed in brain,
CC       spleen and testis. {ECO:0000269|PubMed:12802337,
CC       ECO:0000269|PubMed:17327425, ECO:0000269|PubMed:24742672}.
CC   -!- DOMAIN: The N-terminus is cytoplasmic and the C-terminus is
CC       extracellular, contrary to what is observed for G-protein coupled
CC       receptors. Unlike G-protein coupled receptors, transmembrane helices
CC       are not kinked or tilted relative to the plane of the membrane.
CC       {ECO:0000250|UniProtKB:Q86V24}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice are viable and fertile, and display
CC       increased glucose tolerance (PubMed:17327425, PubMed:17068142,
CC       PubMed:17268472, PubMed:24742672). On a high fat diet, they have lower
CC       fasting insulin levels than wild-type (PubMed:17327425,
CC       PubMed:24742672). Mutant mice have lower plasma cholesterol levels on a
CC       high fat diet, and possibly also on normal chow (PubMed:17327425,
CC       PubMed:17068142). The precise phenotype may depend on the experimental
CC       details and on genotype. Male and female mutant mice are somewhat
CC       leaner than wild-type on standard chow and do not display increased
CC       weight gain on a high fat diet (PubMed:17327425, PubMed:24742672).
CC       Mutant mice have normal body weight on standard chow, but decreased
CC       weight gain on a high-fat diet (PubMed:17068142). Female mutant mice
CC       display lower total body fat than wild-type on a high fat diet
CC       (PubMed:17327425). Both male and female mice have reduced levels of
CC       white and brown adipose tissue relative to wild-type (PubMed:17327425).
CC       Mutant male mice display decreased testis weight, atrophy of the
CC       seminiferous tubules and aspermia (PubMed:17327425). Both male and
CC       female mice display increased brain weight relative to wild-type
CC       (PubMed:17327425). Mutant mice have increased locomotor activity and
CC       increased energy expenditure on a high fat diet (PubMed:17327425).
CC       Mutant mice display impaired revascularization, limb retraction,
CC       atrophy and necrosis in response to limb ischemia caused by severing
CC       the femoral artery (PubMed:24742672). Hepatocytes from mice lacking
CC       both Adipor1 and Adipor2 show loss of adiponectin binding and lack of
CC       adiponectin-mediated activation of AMPK and Ppara (PubMed:17268472).
CC       Mice lacking both Adipor1 and Adipor2 display elevated glucose and
CC       insulin levels in blood plasma, indicative of glucose intolerance and
CC       insulin resistance (PubMed:17268472). {ECO:0000269|PubMed:17068142,
CC       ECO:0000269|PubMed:17268472, ECO:0000269|PubMed:17327425,
CC       ECO:0000269|PubMed:24742672}.
CC   -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
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DR   EMBL; AK039667; BAC30412.1; -; mRNA.
DR   EMBL; AK046591; BAC32799.1; -; mRNA.
DR   EMBL; BC024094; AAH24094.2; -; mRNA.
DR   EMBL; BC064109; AAH64109.1; -; mRNA.
DR   CCDS; CCDS20473.1; -. [Q8BQS5-1]
DR   RefSeq; NP_932102.2; NM_197985.3. [Q8BQS5-1]
DR   RefSeq; XP_006506601.1; XM_006506538.2.
DR   RefSeq; XP_011239750.1; XM_011241448.2.
DR   AlphaFoldDB; Q8BQS5; -.
DR   SMR; Q8BQS5; -.
DR   BioGRID; 212865; 6.
DR   STRING; 10090.ENSMUSP00000032272; -.
DR   iPTMnet; Q8BQS5; -.
DR   PhosphoSitePlus; Q8BQS5; -.
DR   MaxQB; Q8BQS5; -.
DR   PaxDb; 10090-ENSMUSP00000032272; -.
DR   ProteomicsDB; 287946; -. [Q8BQS5-1]
DR   ProteomicsDB; 287947; -. [Q8BQS5-2]
DR   Antibodypedia; 22097; 314 antibodies from 30 providers.
DR   DNASU; 68465; -.
DR   Ensembl; ENSMUST00000032272.13; ENSMUSP00000032272.7; ENSMUSG00000030168.14. [Q8BQS5-1]
DR   Ensembl; ENSMUST00000169744.8; ENSMUSP00000126138.2; ENSMUSG00000030168.14. [Q8BQS5-1]
DR   GeneID; 68465; -.
DR   KEGG; mmu:68465; -.
DR   UCSC; uc009dmd.1; mouse. [Q8BQS5-1]
DR   UCSC; uc009dmf.1; mouse. [Q8BQS5-2]
DR   AGR; MGI:93830; -.
DR   CTD; 79602; -.
DR   MGI; MGI:93830; Adipor2.
DR   VEuPathDB; HostDB:ENSMUSG00000030168; -.
DR   eggNOG; KOG0748; Eukaryota.
DR   GeneTree; ENSGT00940000156451; -.
DR   HOGENOM; CLU_023075_1_0_1; -.
DR   InParanoid; Q8BQS5; -.
DR   OMA; CLGMSGT; -.
DR   OrthoDB; 373478at2759; -.
DR   PhylomeDB; Q8BQS5; -.
DR   TreeFam; TF313640; -.
DR   Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
DR   BioGRID-ORCS; 68465; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Adipor2; mouse.
DR   PRO; PR:Q8BQS5; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8BQS5; Protein.
DR   Bgee; ENSMUSG00000030168; Expressed in small intestine Peyer's patch and 275 other cell types or tissues.
DR   ExpressionAtlas; Q8BQS5; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0097003; F:adipokinetic hormone receptor activity; ISS:UniProtKB.
DR   GO; GO:0055100; F:adiponectin binding; IPI:MGI.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR   GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:MGI.
DR   GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR   GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR   GO; GO:0061871; P:negative regulation of hepatic stellate cell migration; ISO:MGI.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0009750; P:response to fructose; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0061042; P:vascular wound healing; IMP:UniProtKB.
DR   InterPro; IPR004254; AdipoR/HlyIII-related.
DR   PANTHER; PTHR20855:SF33; ADIPONECTIN RECEPTOR PROTEIN 2; 1.
DR   PANTHER; PTHR20855; ADIPOR/PROGESTIN RECEPTOR-RELATED; 1.
DR   Pfam; PF03006; HlyIII; 1.
DR   Genevisible; Q8BQS5; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Fatty acid metabolism;
KW   Lipid metabolism; Membrane; Metal-binding; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..386
FT                   /note="Adiponectin receptor protein 2"
FT                   /id="PRO_0000218830"
FT   TOPO_DOM        1..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        148..168
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        169..181
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        182..202
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        203..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        235..245
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        246..266
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        267..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        274..294
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        295..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        310..330
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        331..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TRANSMEM        349..369
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   TOPO_DOM        370..386
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q86V24"
FT   VAR_SEQ         281..283
FT                   /note="VFV -> ECM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008887"
FT   VAR_SEQ         284..386
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_008888"
FT   CONFLICT        92
FT                   /note="E -> G (in Ref. 1; BAC32799)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   386 AA;  43981 MW;  7760178D3A52E9CA CRC64;
     MNEPAKHRLG CTRTPEPDIR LRKGHQLDDT RGSNNDNYQG DLEPSLETPV CSSYYENSPE
     EPECHDDNSQ EDEGFMGMSP LLQAHHAMER MEEFVCKVWE GRWRVIPHDV LPDWLKDNDF
     LLHGHRPPMP SFRACFKSIF RIHTETGNIW THLLGCVFFL CLGIFYMFRP NISFVAPLQE
     KVVFGLFFLG AILCLSFSWL FHTVYCHSEG VSRLFSKLDY SGIALLIMGS FVPWLYYSFY
     CNPQPCFIYL IVICVLGIAA IIVSQWDMFA TPQYRGVRAG VFVGLGLSGI IPTLHYVISE
     GFLKAATIGQ IGWLMLMASL YITGAALYAA RIPERFFPGK CDIWFHSHQL FHIFVVAGAF
     VHFHGVSNLQ EFRFMIGGGC TEEDAL
//