CD226_HUMAN
ID CD226_HUMAN Reviewed; 336 AA.
AC Q15762; B2R818;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=CD226 antigen;
DE AltName: Full=DNAX accessory molecule 1;
DE Short=DNAM-1;
DE AltName: CD_antigen=CD226;
DE Flags: Precursor;
GN Name=CD226; Synonyms=DNAM1;
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], PROTEIN SEQUENCE OF 19-39; 54-72; 204-221 AND
RP 285-294, FUNCTION, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND
RP VARIANT GLY-307.
RX PubMed=8673704; DOI=10.1016/s1074-7613(00)70060-4;
RA Shibuya A., Campbell D., Hannum C., Yssel H., Franz-Bacon K.,
RA McClanahan T., Kitamura T., Nicholl J., Sutherland G.R., Lanier L.L.,
RA Phillips J.H.;
RT "DNAM-1, a novel adhesion molecule involved in the cytolytic function of T
RT lymphocytes.";
RL Immunity 4:573-581(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-307.
RC TISSUE=Natural killer cell;
RA Biassoni R.;
RT "Receptor involved in the NK cell triggering.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-307.
RC TISSUE=Brain;
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 [7]
RP INTERACTION WITH PVR AND NECTIN2.
RX PubMed=15039383; DOI=10.1093/intimm/dxh059;
RA Tahara-Hanaoka S., Shibuya K., Onoda Y., Zhang H., Yamazaki S.,
RA Miyamoto A., Honda S., Lanier L.L., Shibuya A.;
RT "Functional characterization of DNAM-1 (CD226) interaction with its ligands
RT PVR (CD155) and nectin-2 (PRR-2/CD112).";
RL Int. Immunol. 16:533-538(2004).
RN [8]
RP INTERACTION WITH PVR AND NECTIN2.
RX PubMed=15607800; DOI=10.1016/j.molimm.2004.07.028;
RA Pende D., Bottino C., Castriconi R., Cantoni C., Marcenaro S., Rivera P.,
RA Spaggiari G.M., Dondero A., Carnemolla B., Reymond N., Mingari M.C.,
RA Lopez M., Moretta L., Moretta A.;
RT "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226)
RT activating receptor: involvement in tumor cell lysis.";
RL Mol. Immunol. 42:463-469(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-322, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-322, VARIANT [LARGE SCALE
RP ANALYSIS] GLY-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP FUNCTION AS NECTIN2 RECEPTOR.
RX PubMed=26755705; DOI=10.1084/jem.20150785;
RA Zhu Y., Paniccia A., Schulick A.C., Chen W., Koenig M.R., Byers J.T.,
RA Yao S., Bevers S., Edil B.H.;
RT "Identification of CD112R as a novel checkpoint for human T cells.";
RL J. Exp. Med. 213:167-176(2016).
CC -!- FUNCTION: Involved in intercellular adhesion, lymphocyte signaling,
CC cytotoxicity and lymphokine secretion mediated by cytotoxic T-
CC lymphocyte (CTL) and NK cell (PubMed:8673704). Cell surface receptor
CC for NECTIN2. Upon ligand binding, stimulates T-cell proliferation and
CC cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG.
CC Competes with PVRIG for NECTIN2-binding (PubMed:26755705).
CC {ECO:0000269|PubMed:26755705, ECO:0000269|PubMed:8673704}.
CC -!- SUBUNIT: Interacts with PVR and NECTIN2. Competes with PVRIG for
CC NECTIN2-binding. {ECO:0000269|PubMed:15039383,
CC ECO:0000269|PubMed:15607800, ECO:0000269|PubMed:26755705}.
CC -!- INTERACTION:
CC Q15762; Q15762: CD226; NbExp=2; IntAct=EBI-4314442, EBI-4314442;
CC Q15762; Q92692: NECTIN2; NbExp=2; IntAct=EBI-4314442, EBI-718419;
CC Q15762; P15151: PVR; NbExp=3; IntAct=EBI-4314442, EBI-3919694;
CC Q15762; Q495A1: TIGIT; NbExp=4; IntAct=EBI-4314442, EBI-4314807;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by peripheral blood T-lymphocytes.
CC {ECO:0000269|PubMed:8673704}.
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DR EMBL; U56102; AAC50560.1; -; mRNA.
DR EMBL; AJ537553; CAD61184.1; -; mRNA.
DR EMBL; AK313199; BAG36015.1; -; mRNA.
DR EMBL; AC011930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471117; EAW66515.1; -; Genomic_DNA.
DR EMBL; BC074787; AAH74787.1; -; mRNA.
DR CCDS; CCDS11997.1; -.
DR RefSeq; NP_001290547.1; NM_001303618.1.
DR RefSeq; NP_006557.2; NM_006566.3.
DR RefSeq; XP_005266699.1; XM_005266642.3.
DR PDB; 6ISB; X-ray; 2.50 A; A/B/C=19-250.
DR PDB; 6O3O; X-ray; 2.80 A; A/B=19-250.
DR PDBsum; 6ISB; -.
DR PDBsum; 6O3O; -.
DR AlphaFoldDB; Q15762; -.
DR SMR; Q15762; -.
DR BioGRID; 115908; 76.
DR IntAct; Q15762; 3.
DR STRING; 9606.ENSP00000280200; -.
DR GlyGen; Q15762; 8 sites.
DR iPTMnet; Q15762; -.
DR PhosphoSitePlus; Q15762; -.
DR BioMuta; CD226; -.
DR DMDM; 317373338; -.
DR jPOST; Q15762; -.
DR MassIVE; Q15762; -.
DR PaxDb; Q15762; -.
DR PeptideAtlas; Q15762; -.
DR PRIDE; Q15762; -.
DR ProteomicsDB; 60748; -.
DR Antibodypedia; 2514; 815 antibodies from 38 providers.
DR DNASU; 10666; -.
DR Ensembl; ENST00000280200.8; ENSP00000280200.4; ENSG00000150637.9.
DR Ensembl; ENST00000582621.6; ENSP00000461947.1; ENSG00000150637.9.
DR GeneID; 10666; -.
DR KEGG; hsa:10666; -.
DR MANE-Select; ENST00000582621.6; ENSP00000461947.1; NM_001303618.2; NP_001290547.1.
DR UCSC; uc002lkm.6; human.
DR CTD; 10666; -.
DR DisGeNET; 10666; -.
DR GeneCards; CD226; -.
DR HGNC; HGNC:16961; CD226.
DR HPA; ENSG00000150637; Group enriched (lymphoid tissue, parathyroid gland).
DR MIM; 605397; gene.
DR neXtProt; NX_Q15762; -.
DR OpenTargets; ENSG00000150637; -.
DR PharmGKB; PA134911130; -.
DR VEuPathDB; HostDB:ENSG00000150637; -.
DR eggNOG; ENOG502RY5X; Eukaryota.
DR GeneTree; ENSGT00500000044993; -.
DR HOGENOM; CLU_069157_0_0_1; -.
DR InParanoid; Q15762; -.
DR OMA; DAREDIY; -.
DR OrthoDB; 843835at2759; -.
DR PhylomeDB; Q15762; -.
DR TreeFam; TF336260; -.
DR PathwayCommons; Q15762; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q15762; -.
DR SIGNOR; Q15762; -.
DR BioGRID-ORCS; 10666; 9 hits in 1075 CRISPR screens.
DR ChiTaRS; CD226; human.
DR GeneWiki; CD226; -.
DR GenomeRNAi; 10666; -.
DR Pharos; Q15762; Tbio.
DR PRO; PR:Q15762; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q15762; protein.
DR Bgee; ENSG00000150637; Expressed in monocyte and 104 other tissues.
DR ExpressionAtlas; Q15762; baseline and differential.
DR Genevisible; Q15762; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0045121; C:membrane raft; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0008037; P:cell recognition; TAS:BHF-UCL.
DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; IDA:BHF-UCL.
DR GO; GO:0002891; P:positive regulation of immunoglobulin mediated immune response; IDA:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IBA:GO_Central.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IDA:BHF-UCL.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; IBA:GO_Central.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:BHF-UCL.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:BHF-UCL.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042842; CD226.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR47011; PTHR47011; 1.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8673704"
FT CHAIN 19..336
FT /note="CD226 antigen"
FT /id="PRO_0000014665"
FT TOPO_DOM 19..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..239
FT /note="Ig-like C2-type 2"
FT REGION 297..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 307
FT /note="S -> G (in dbSNP:rs763361)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8673704, ECO:0000269|Ref.2,
FT ECO:0007744|PubMed:19690332"
FT /id="VAR_018632"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6ISB"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6ISB"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6ISB"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6ISB"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6ISB"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:6ISB"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6O3O"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6ISB"
FT TURN 200..205
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:6ISB"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 218..229
FT /evidence="ECO:0007829|PDB:6ISB"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:6ISB"
SQ SEQUENCE 336 AA; 38614 MW; 5379182CC4695097 CRC64;
MDYPTLLLAL LHVYRALCEE VLWHTSVPFA ENMSLECVYP SMGILTQVEW FKIGTQQDSI
AIFSPTHGMV IRKPYAERVY FLNSTMASNN MTLFFRNASE DDVGYYSCSL YTYPQGTWQK
VIQVVQSDSF EAAVPSNSHI VSEPGKNVTL TCQPQMTWPV QAVRWEKIQP RQIDLLTYCN
LVHGRNFTSK FPRQIVSNCS HGRWSVIVIP DVTVSDSGLY RCYLQASAGE NETFVMRLTV
AEGKTDNQYT LFVAGGTVLL LLFVISITTI IVIFLNRRRR RERRDLFTES WDTQKAPNNY
RSPISTSQPT NQSMDDTRED IYVNYPTFSR RPKTRV
