PAQR2_HUMAN
ID PAQR2_HUMAN Reviewed; 386 AA.
AC Q86V24; Q53YY5; Q9H737;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Adiponectin receptor protein 2 {ECO:0000303|PubMed:25969726};
DE AltName: Full=Progestin and adipoQ receptor family member 2 {ECO:0000303|PubMed:16044242};
DE AltName: Full=Progestin and adipoQ receptor family member II;
GN Name=ADIPOR2 {ECO:0000312|HGNC:HGNC:24041};
GN Synonyms=PAQR2 {ECO:0000303|PubMed:16044242};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16044242; DOI=10.1007/s00239-004-0375-2;
RA Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C.,
RA Funk W.D.;
RT "PAQR proteins: a novel membrane receptor family defined by an ancient 7-
RT transmembrane pass motif.";
RL J. Mol. Evol. 61:372-380(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Hippocampus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND TOPOLOGY.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 100-386 IN COMPLEX WITH ZINC,
RP FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-202;
RP ASP-219; HIS-348 AND HIS-352.
RX PubMed=25855295; DOI=10.1038/nature14301;
RA Tanabe H., Fujii Y., Okada-Iwabu M., Iwabu M., Nakamura Y., Hosaka T.,
RA Motoyama K., Ikeda M., Wakiyama M., Terada T., Ohsawa N., Hato M.,
RA Ogasawara S., Hino T., Murata T., Iwata S., Hirata K., Kawano Y.,
RA Yamamoto M., Kimura-Someya T., Shirouzu M., Yamauchi T., Kadowaki T.,
RA Yokoyama S.;
RT "Crystal structures of the human adiponectin receptors.";
RL Nature 520:312-316(2015).
RN [8]
RP VARIANT 31-ARG--LEU-386 DEL.
RX PubMed=25969726; DOI=10.1186/s13229-015-0017-0;
RA Codina-Sola M., Rodriguez-Santiago B., Homs A., Santoyo J., Rigau M.,
RA Aznar-Lain G., Del Campo M., Gener B., Gabau E., Botella M.P.,
RA Gutierrez-Arumi A., Antinolo G., Perez-Jurado L.A., Cusco I.;
RT "Integrated analysis of whole-exome sequencing and transcriptome profiling
RT in males with autism spectrum disorders.";
RL Mol. Autism 6:21-21(2015).
CC -!- FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by
CC adipocytes that regulates glucose and lipid metabolism
CC (PubMed:12802337, PubMed:25855295). Required for normal body fat and
CC glucose homeostasis. ADIPOQ-binding activates a signaling cascade that
CC leads to increased PPARA activity, and ultimately to increased fatty
CC acid oxidation and glucose uptake. Has intermediate affinity for
CC globular and full-length adiponectin. Required for normal
CC revascularization after chronic ischemia caused by severing of blood
CC vessels (By similarity). {ECO:0000250|UniProtKB:Q8BQS5,
CC ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.
CC -!- SUBUNIT: May form homooligomers and heterooligomers with ADIPOR1
CC (PubMed:12802337). Interacts with APPL2 (via BAR domain); ADIPOQ
CC dissociates this interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q8BQS5, ECO:0000269|PubMed:12802337}.
CC -!- INTERACTION:
CC Q86V24; P55061: TMBIM6; NbExp=3; IntAct=EBI-1769445, EBI-1045825;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12802337,
CC ECO:0000269|PubMed:25855295}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:25855295}.
CC Note=Localized to the cell membrane and intracellular organelles.
CC {ECO:0000269|PubMed:12802337}.
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:16044242). Highly expressed in
CC skeletal muscle, liver and placenta (PubMed:12802337). Weakly expressed
CC in brain, heart, colon, spleen, kidney, thymus, small intestine,
CC peripheral blood leukocytes and lung (PubMed:12802337).
CC {ECO:0000269|PubMed:12802337, ECO:0000269|PubMed:16044242}.
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:0000269|PubMed:12802337}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15062.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Adiponectin entry;
CC URL="https://en.wikipedia.org/wiki/Adiponectin";
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DR EMBL; AY424280; AAR08368.1; -; mRNA.
DR EMBL; AK025085; BAB15062.1; ALT_INIT; mRNA.
DR EMBL; AK127196; BAC86881.1; -; mRNA.
DR EMBL; AK128511; BAC87473.1; -; mRNA.
DR EMBL; CH471116; EAW88924.1; -; Genomic_DNA.
DR EMBL; BC051858; AAH51858.1; -; mRNA.
DR CCDS; CCDS8511.1; -.
DR RefSeq; NP_078827.2; NM_024551.2.
DR RefSeq; XP_005253846.1; XM_005253789.1.
DR RefSeq; XP_006719081.1; XM_006719018.2.
DR RefSeq; XP_011519326.1; XM_011521024.2.
DR PDB; 5LWY; X-ray; 2.40 A; A=100-386.
DR PDB; 5LX9; X-ray; 2.40 A; A=99-386.
DR PDB; 5LXA; X-ray; 3.00 A; A=100-386.
DR PDB; 6KS1; X-ray; 2.40 A; A=100-386.
DR PDB; 6YX9; X-ray; 2.40 A; A=100-386.
DR PDB; 6YXD; X-ray; 2.90 A; A=100-386.
DR PDB; 6YXF; X-ray; 3.02 A; A=100-386.
DR PDB; 6YXG; X-ray; 3.01 A; A=100-386.
DR PDBsum; 5LWY; -.
DR PDBsum; 5LX9; -.
DR PDBsum; 5LXA; -.
DR PDBsum; 6KS1; -.
DR PDBsum; 6YX9; -.
DR PDBsum; 6YXD; -.
DR PDBsum; 6YXF; -.
DR PDBsum; 6YXG; -.
DR AlphaFoldDB; Q86V24; -.
DR SMR; Q86V24; -.
DR BioGRID; 122739; 11.
DR IntAct; Q86V24; 6.
DR STRING; 9606.ENSP00000349616; -.
DR BindingDB; Q86V24; -.
DR ChEMBL; CHEMBL3392947; -.
DR TCDB; 1.C.113.1.11; the hemolysin iii (hly iii) family.
DR iPTMnet; Q86V24; -.
DR PhosphoSitePlus; Q86V24; -.
DR BioMuta; ADIPOR2; -.
DR DMDM; 38372190; -.
DR EPD; Q86V24; -.
DR jPOST; Q86V24; -.
DR MassIVE; Q86V24; -.
DR MaxQB; Q86V24; -.
DR PaxDb; Q86V24; -.
DR PeptideAtlas; Q86V24; -.
DR PRIDE; Q86V24; -.
DR ProteomicsDB; 69953; -.
DR ABCD; Q86V24; 1 sequenced antibody.
DR Antibodypedia; 22097; 253 antibodies from 30 providers.
DR DNASU; 79602; -.
DR Ensembl; ENST00000357103.5; ENSP00000349616.4; ENSG00000006831.10.
DR Ensembl; ENST00000645126.2; ENSP00000495699.1; ENSG00000285070.2.
DR GeneID; 79602; -.
DR KEGG; hsa:79602; -.
DR MANE-Select; ENST00000357103.5; ENSP00000349616.4; NM_024551.3; NP_078827.2.
DR UCSC; uc001qjm.4; human.
DR CTD; 79602; -.
DR DisGeNET; 79602; -.
DR GeneCards; ADIPOR2; -.
DR HGNC; HGNC:24041; ADIPOR2.
DR HPA; ENSG00000006831; Low tissue specificity.
DR MIM; 607946; gene.
DR neXtProt; NX_Q86V24; -.
DR OpenTargets; ENSG00000006831; -.
DR PharmGKB; PA128394711; -.
DR VEuPathDB; HostDB:ENSG00000006831; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000156451; -.
DR HOGENOM; CLU_023075_1_0_1; -.
DR InParanoid; Q86V24; -.
DR OMA; LRKGHMP; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q86V24; -.
DR TreeFam; TF313640; -.
DR BRENDA; 3.5.1.23; 2681.
DR PathwayCommons; Q86V24; -.
DR Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
DR SignaLink; Q86V24; -.
DR SIGNOR; Q86V24; -.
DR BioGRID-ORCS; 79602; 32 hits in 1076 CRISPR screens.
DR ChiTaRS; ADIPOR2; human.
DR GeneWiki; ADIPOR2; -.
DR GenomeRNAi; 79602; -.
DR Pharos; Q86V24; Tbio.
DR PRO; PR:Q86V24; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86V24; protein.
DR Bgee; ENSG00000006831; Expressed in corpus callosum and 96 other tissues.
DR Genevisible; Q86V24; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0097003; F:adipokinetic hormone receptor activity; IDA:UniProtKB.
DR GO; GO:0055100; F:adiponectin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:UniProtKB.
DR GO; GO:0019395; P:fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0061042; P:vascular wound healing; ISS:UniProtKB.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Fatty acid metabolism; Lipid metabolism;
KW Membrane; Metal-binding; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..386
FT /note="Adiponectin receptor protein 2"
FT /id="PRO_0000218829"
FT TOPO_DOM 1..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 148..168
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 169..181
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 182..202
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 203..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 214..234
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 235..245
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 246..266
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 267..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 274..294
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 295..309
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 310..330
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 331..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TRANSMEM 349..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:25855295"
FT TOPO_DOM 370..386
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25855295"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..41
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:0000269|PubMed:25855295"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25855295"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25855295"
FT VARIANT 31..386
FT /note="Missing (found in a patient with autism spectrum
FT disorder; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25969726"
FT /id="VAR_078687"
FT VARIANT 39
FT /note="Q -> R (in dbSNP:rs12298275)"
FT /id="VAR_048203"
FT MUTAGEN 202
FT /note="H->A: Abolishes response to ADIPOQ binding; when
FT associated with A-219; A-348 and A-352."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 219
FT /note="D->A: Impairs response to ADIPOQ binding. Abolishes
FT response to ADIPOQ binding; when associated with A-202; A-
FT 348 and A-352."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 348
FT /note="H->A: Impairs response to ADIPOQ binding. Abolishes
FT response to ADIPOQ binding; when associated with A-202; A-
FT 219 and A-352."
FT /evidence="ECO:0000269|PubMed:25855295"
FT MUTAGEN 352
FT /note="H->A: Abolishes response to ADIPOQ binding; when
FT associated with A-202; A-219 and A-348."
FT /evidence="ECO:0000269|PubMed:25855295"
FT CONFLICT 158
FT /note="F -> S (in Ref. 2; BAB15062)"
FT /evidence="ECO:0000305"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 146..167
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5LWY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5LX9"
FT HELIX 177..203
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 209..238
FT /evidence="ECO:0007829|PDB:5LWY"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5LXA"
FT HELIX 243..263
FT /evidence="ECO:0007829|PDB:5LWY"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 310..330
FT /evidence="ECO:0007829|PDB:5LWY"
FT TURN 331..336
FT /evidence="ECO:0007829|PDB:5LWY"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:5LWY"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:5LWY"
FT HELIX 347..376
FT /evidence="ECO:0007829|PDB:5LWY"
SQ SEQUENCE 386 AA; 43884 MW; B3B0FF0BBF118AA1 CRC64;
MNEPTENRLG CSRTPEPDIR LRKGHQLDGT RRGDNDSHQG DLEPILEASV LSSHHKKSSE
EHEYSDEAPQ EDEGFMGMSP LLQAHHAMEK MEEFVCKVWE GRWRVIPHDV LPDWLKDNDF
LLHGHRPPMP SFRACFKSIF RIHTETGNIW THLLGCVFFL CLGIFYMFRP NISFVAPLQE
KVVFGLFFLG AILCLSFSWL FHTVYCHSEG VSRLFSKLDY SGIALLIMGS FVPWLYYSFY
CNPQPCFIYL IVICVLGIAA IIVSQWDMFA TPQYRGVRAG VFLGLGLSGI IPTLHYVISE
GFLKAATIGQ IGWLMLMASL YITGAALYAA RIPERFFPGK CDIWFHSHQL FHIFVVAGAF
VHFHGVSNLQ EFRFMIGGGC SEEDAL
