ID   BT3A3_HUMAN             Reviewed;         584 AA.
AC   O00478; B4DWI7; E9PCP5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 194.
DE   RecName: Full=Butyrophilin subfamily 3 member A3;
DE   Flags: Precursor;
GN   Name=BTN3A3; Synonyms=BTF3;
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] (ISOFORM 1).
RX   PubMed=9149941; DOI=10.1101/gr.7.5.441;
RA   Ruddy D.A., Kronmal G.S., Lee V.K., Mintier G.A., Quintana L.,
RA   Domingo R. Jr., Meyer N.C., Irrinki A., McClelland E.E., Fullan A.,
RA   Mapa F.A., Moore T., Thomas W., Loeb D.B., Harmon C., Tsuchihashi Z.,
RA   Wolff R.K., Schatzman R.C., Feder J.N.;
RT   "A 1.1-Mb transcript map of the hereditary hemochromatosis locus.";
RL   Genome Res. 7:441-456(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
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=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph;
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   [6]
RP   PROTEIN SEQUENCE OF 30-44.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX   PubMed=20610803; DOI=10.1189/jlb.0309156;
RA   Yamashiro H., Yoshizaki S., Tadaki T., Egawa K., Seo N.;
RT   "Stimulation of human butyrophilin 3 molecules results in negative
RT   regulation of cellular immunity.";
RL   J. Leukoc. Biol. 88:757-767(2010).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=21918970; DOI=10.1002/eji.201141404;
RA   Messal N., Mamessier E., Sylvain A., Celis-Gutierrez J., Thibult M.L.,
RA   Chetaille B., Firaguay G., Pastor S., Guillaume Y., Wang Q., Hirsch I.,
RA   Nunes J.A., Olive D.;
RT   "Differential role for CD277 as a co-regulator of the immune signal in T
RT   and NK cells.";
RL   Eur. J. Immunol. 41:3443-3454(2011).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22767497; DOI=10.1182/blood-2012-05-430470;
RA   Harly C., Guillaume Y., Nedellec S., Peigne C.M., Monkkonen H.,
RA   Monkkonen J., Li J., Kuball J., Adams E.J., Netzer S.,
RA   Dechanet-Merville J., Leger A., Herrmann T., Breathnach R., Olive D.,
RA   Bonneville M., Scotet E.;
RT   "Key implication of CD277/butyrophilin-3 (BTN3A) in cellular stress sensing
RT   by a major human gammadelta T-cell subset.";
RL   Blood 120:2269-2279(2012).
RN   [11]
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   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 30-246, SUBUNIT, AND DISULFIDE
RP   BONDS.
RX   PubMed=22846996; DOI=10.1074/jbc.m112.384354;
RA   Palakodeti A., Sandstrom A., Sundaresan L., Harly C., Nedellec S.,
RA   Olive D., Scotet E., Bonneville M., Adams E.J.;
RT   "The molecular basis for modulation of human Vgamma9Vdelta2 T cell
RT   responses by CD277/butyrophilin-3 (BTN3A)-specific antibodies.";
RL   J. Biol. Chem. 287:32780-32790(2012).
CC   -!- FUNCTION: Plays a role in T-cell responses in the adaptive immune
CC       response. {ECO:0000269|PubMed:22767497}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21918970,
CC       ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00478-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O00478-2; Sequence=VSP_045063, VSP_045064;
CC   -!- TISSUE SPECIFICITY: Detected in peripheral blood mononuclear cells and
CC       in T-cells (at protein level). Detected in spleen and lymphocytes.
CC       {ECO:0000269|PubMed:20610803}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19349973,
CC       ECO:0000269|PubMed:20610803}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000305}.
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DR   EMBL; U90548; AAB53426.1; -; mRNA.
DR   EMBL; BT007251; AAP35915.1; -; mRNA.
DR   EMBL; AK301553; BAG63049.1; -; mRNA.
DR   EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC015815; AAH15815.1; -; mRNA.
DR   CCDS; CCDS4611.1; -. [O00478-1]
DR   CCDS; CCDS4612.2; -. [O00478-2]
DR   RefSeq; NP_001229732.1; NM_001242803.1.
DR   RefSeq; NP_008925.1; NM_006994.4. [O00478-1]
DR   RefSeq; NP_932078.2; NM_197974.2. [O00478-2]
DR   PDB; 4F8T; X-ray; 2.38 A; A=30-246.
DR   PDB; 5ZZ3; X-ray; 3.00 A; A=328-584.
DR   PDB; 6J0G; X-ray; 1.60 A; A/B/C/D=328-515.
DR   PDB; 6J0K; X-ray; 2.00 A; A/B=328-515.
DR   PDB; 6J0L; X-ray; 1.95 A; A/B=328-515.
DR   PDBsum; 4F8T; -.
DR   PDBsum; 5ZZ3; -.
DR   PDBsum; 6J0G; -.
DR   PDBsum; 6J0K; -.
DR   PDBsum; 6J0L; -.
DR   AlphaFoldDB; O00478; -.
DR   SMR; O00478; -.
DR   BioGRID; 115657; 34.
DR   IntAct; O00478; 7.
DR   STRING; 9606.ENSP00000244519; -.
DR   GlyConnect; 1050; 1 N-Linked glycan (1 site).
DR   GlyCosmos; O00478; 1 site, No reported glycans.
DR   GlyGen; O00478; 1 site.
DR   iPTMnet; O00478; -.
DR   PhosphoSitePlus; O00478; -.
DR   BioMuta; BTN3A3; -.
DR   EPD; O00478; -.
DR   jPOST; O00478; -.
DR   MassIVE; O00478; -.
DR   MaxQB; O00478; -.
DR   PaxDb; 9606-ENSP00000244519; -.
DR   PeptideAtlas; O00478; -.
DR   ProteomicsDB; 19486; -.
DR   ProteomicsDB; 47923; -. [O00478-1]
DR   Pumba; O00478; -.
DR   Antibodypedia; 2341; 145 antibodies from 21 providers.
DR   DNASU; 10384; -.
DR   Ensembl; ENST00000244519.7; ENSP00000244519.2; ENSG00000111801.16. [O00478-1]
DR   Ensembl; ENST00000361232.7; ENSP00000355238.3; ENSG00000111801.16. [O00478-2]
DR   GeneID; 10384; -.
DR   KEGG; hsa:10384; -.
DR   MANE-Select; ENST00000244519.7; ENSP00000244519.2; NM_006994.5; NP_008925.1.
DR   UCSC; uc003nhz.3; human. [O00478-1]
DR   AGR; HGNC:1140; -.
DR   CTD; 10384; -.
DR   DisGeNET; 10384; -.
DR   GeneCards; BTN3A3; -.
DR   HGNC; HGNC:1140; BTN3A3.
DR   HPA; ENSG00000111801; Low tissue specificity.
DR   MIM; 613595; gene.
DR   neXtProt; NX_O00478; -.
DR   OpenTargets; ENSG00000111801; -.
DR   PharmGKB; PA25461; -.
DR   VEuPathDB; HostDB:ENSG00000111801; -.
DR   eggNOG; ENOG502QSRZ; Eukaryota.
DR   GeneTree; ENSGT00940000162723; -.
DR   HOGENOM; CLU_013137_22_2_1; -.
DR   InParanoid; O00478; -.
DR   OMA; WVKMIPE; -.
DR   OrthoDB; 2943983at2759; -.
DR   PhylomeDB; O00478; -.
DR   TreeFam; TF331083; -.
DR   PathwayCommons; O00478; -.
DR   Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR   SignaLink; O00478; -.
DR   BioGRID-ORCS; 10384; 14 hits in 1152 CRISPR screens.
DR   GeneWiki; BTN3A3; -.
DR   GenomeRNAi; 10384; -.
DR   Pharos; O00478; Tbio.
DR   PRO; PR:O00478; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O00478; Protein.
DR   Bgee; ENSG00000111801; Expressed in granulocyte and 203 other cell types or tissues.
DR   ExpressionAtlas; O00478; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0002456; P:T cell mediated immunity; IMP:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd05713; IgV_MOG_like; 1.
DR   CDD; cd15820; SPRY_PRY_BTN3; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; IPR013106; Ig_V-set.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR037954; SPRY_PRY_BTN3.
DR   PANTHER; PTHR24100; BUTYROPHILIN; 1.
DR   PANTHER; PTHR24100:SF56; BUTYROPHILIN SUBFAMILY 3 MEMBER A3; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   Genevisible; O00478; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           30..584
FT                   /note="Butyrophilin subfamily 3 member A3"
FT                   /id="PRO_0000014534"
FT   TOPO_DOM        30..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..584
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..139
FT                   /note="Ig-like V-type 1"
FT   DOMAIN          145..236
FT                   /note="Ig-like V-type 2"
FT   DOMAIN          322..518
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          519..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   DISULFID        52..126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:22846996"
FT   DISULFID        166..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:22846996"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045063"
FT   VAR_SEQ         307..313
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045064"
FT   CONFLICT        229
FT                   /note="L -> P (in Ref. 3; BAG63049)"
FT                   /evidence="ECO:0000305"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          48..56
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   TURN            70..73
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          108..115
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          122..130
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          133..145
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          151..158
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          161..173
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          176..181
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          202..210
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          218..224
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   TURN            225..228
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   STRAND          229..235
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   TURN            239..241
FT                   /evidence="ECO:0007829|PDB:4F8T"
FT   HELIX           328..336
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   TURN            346..348
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          353..355
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          359..364
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          379..381
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          383..387
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          390..400
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          407..413
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          418..421
FT                   /evidence="ECO:0007829|PDB:5ZZ3"
FT   HELIX           427..429
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          431..437
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   TURN            438..440
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          446..448
FT                   /evidence="ECO:0007829|PDB:5ZZ3"
FT   STRAND          450..452
FT                   /evidence="ECO:0007829|PDB:6J0L"
FT   STRAND          459..466
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   TURN            467..470
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          471..476
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   TURN            477..479
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          482..485
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          495..500
FT                   /evidence="ECO:0007829|PDB:6J0G"
FT   STRAND          509..511
FT                   /evidence="ECO:0007829|PDB:6J0G"
SQ   SEQUENCE   584 AA;  65002 MW;  2B279B9141E0327F CRC64;
     MKMASSLAFL LLNFHVSLFL VQLLTPCSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA
     ETMELRWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD
     SGKYLCYFQD GDFYEKALVE LKVAALGSDL HIEVKGYEDG GIHLECRSTG WYPQPQIKWS
     DTKGENIPAV EAPVVADGVG LYAVAASVIM RGSSGGGVSC IIRNSLLGLE KTASISIADP
     FFRSAQPWIA ALAGTLPISL LLLAGASYFL WRQQKEKIAL SRETEREREM KEMGYAATEQ
     EISLREKLQE ELKWRKIQYM ARGEKSLAYH EWKMALFKPA DVILDPDTAN AILLVSEDQR
     SVQRAEEPRD LPDNPERFEW RYCVLGCENF TSGRHYWEVE VGDRKEWHIG VCSKNVERKK
     GWVKMTPENG YWTMGLTDGN KYRALTEPRT NLKLPEPPRK VGIFLDYETG EISFYNATDG
     SHIYTFPHAS FSEPLYPVFR ILTLEPTALT ICPIPKEVES SPDPDLVPDH SLETPLTPGL
     ANESGEPQAE VTSLLLPAHP GAEVSPSATT NQNHKLQART EALY
//