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   24-JAN-2024, entry version 175.
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.ENSP00000461947; -.
DR   GlyCosmos; Q15762; 8 sites, No reported glycans.
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; 9606-ENSP00000280200; -.
DR   PeptideAtlas; Q15762; -.
DR   ProteomicsDB; 60748; -.
DR   Antibodypedia; 2514; 922 antibodies from 39 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   AGR; HGNC:16961; -.
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; IREPYAD; -.
DR   OrthoDB; 5354047at2759; -.
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 1155 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 105 other cell types or tissues.
DR   ExpressionAtlas; Q15762; baseline and differential.
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: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: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:0032729; P:positive regulation of type II interferon production; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd05889; IgV_1_DNAM-1_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; CD226 ANTIGEN; 1.
DR   PANTHER; PTHR47011:SF1; CD226 ANTIGEN; 1.
DR   Pfam; PF07686; V-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   Genevisible; Q15762; HS.
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
//