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 Genevisible; O00478; HS.
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.
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
//
