BT3A2_HUMAN
ID BT3A2_HUMAN Reviewed; 334 AA.
AC P78410; B4DRT7; B4E103; F5H791; F8W6E0; O00477; O15338; O75658; Q76PA0;
AC Q9BU81; Q9NR44;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Butyrophilin subfamily 3 member A2;
DE Flags: Precursor;
GN Name=BTN3A2; Synonyms=BT3.2, BTF3, BTF4;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9382921; DOI=10.1007/s002510050326;
RA Tazi-Ahnini R., Henry J., Offer C., Bouissou-Bouchouata C., Mather I.H.,
RA Pontarotti P.;
RT "Cloning, localization, and structure of new members of the butyrophilin
RT gene family in the juxta-telomeric region of the major histocompatibility
RT complex.";
RL Immunogenetics 47:55-63(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11170752; DOI=10.1006/geno.2000.6406;
RA Rhodes D.A., Stammers M., Malcherek G., Beck S., Trowsdale J.;
RT "The cluster of BTN genes in the extended major histocompatibility
RT complex.";
RL Genomics 71:351-362(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASP-181;
RP THR-182 AND ASN-307.
RC TISSUE=Thymus, and Tongue;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282 AND SER-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [8]
RP GLYCOSYLATION.
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 30-239, 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. Inhibits the release of IFNG from activated T-cells.
CC {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22846996}.
CC -!- INTERACTION:
CC P78410; O00481: BTN3A1; NbExp=3; IntAct=EBI-17564670, EBI-2809309;
CC P78410; P57739: CLDN2; NbExp=3; IntAct=EBI-17564670, EBI-751440;
CC P78410; Q96CV9: OPTN; NbExp=3; IntAct=EBI-17564670, EBI-748974;
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=3;
CC Name=1;
CC IsoId=P78410-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78410-2; Sequence=VSP_045907;
CC Name=3;
CC IsoId=P78410-3; Sequence=VSP_045906;
CC -!- TISSUE SPECIFICITY: Detected in T-cells and natural killer cells.
CC {ECO:0000269|PubMed:21918970}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20610803}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53424.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC02652.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC02655.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U90546; AAB53424.1; ALT_FRAME; mRNA.
DR EMBL; U90144; AAC02652.1; ALT_FRAME; mRNA.
DR EMBL; U97499; AAC02655.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U97498; AAC02655.1; JOINED; Genomic_DNA.
DR EMBL; AF257505; AAF76140.1; -; mRNA.
DR EMBL; AK299417; BAG61399.1; -; mRNA.
DR EMBL; AK303600; BAG64615.1; -; mRNA.
DR EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002832; AAH02832.3; -; mRNA.
DR EMBL; BC020214; AAH20214.3; -; mRNA.
DR CCDS; CCDS4605.1; -. [P78410-1]
DR CCDS; CCDS56399.1; -. [P78410-2]
DR CCDS; CCDS56400.1; -. [P78410-3]
DR RefSeq; NP_001184175.1; NM_001197246.2. [P78410-1]
DR RefSeq; NP_001184176.1; NM_001197247.2. [P78410-1]
DR RefSeq; NP_001184177.1; NM_001197248.2. [P78410-2]
DR RefSeq; NP_001184178.1; NM_001197249.2. [P78410-3]
DR RefSeq; NP_008978.2; NM_007047.4. [P78410-1]
DR RefSeq; XP_005248884.1; XM_005248827.3. [P78410-1]
DR RefSeq; XP_016865700.1; XM_017010211.1. [P78410-1]
DR RefSeq; XP_016865701.1; XM_017010212.1. [P78410-1]
DR RefSeq; XP_016865703.1; XM_017010214.1. [P78410-3]
DR PDB; 4F8Q; X-ray; 2.38 A; A=30-239.
DR PDBsum; 4F8Q; -.
DR AlphaFoldDB; P78410; -.
DR SMR; P78410; -.
DR BioGRID; 116293; 31.
DR IntAct; P78410; 8.
DR STRING; 9606.ENSP00000348751; -.
DR GlyConnect; 1049; 1 N-Linked glycan (1 site).
DR GlyGen; P78410; 1 site.
DR iPTMnet; P78410; -.
DR PhosphoSitePlus; P78410; -.
DR BioMuta; BTN3A2; -.
DR DMDM; 67462189; -.
DR EPD; P78410; -.
DR jPOST; P78410; -.
DR MassIVE; P78410; -.
DR MaxQB; P78410; -.
DR PaxDb; P78410; -.
DR PeptideAtlas; P78410; -.
DR PRIDE; P78410; -.
DR ProteomicsDB; 27417; -.
DR ProteomicsDB; 29764; -.
DR ProteomicsDB; 57615; -. [P78410-1]
DR Antibodypedia; 25604; 122 antibodies from 18 providers.
DR DNASU; 11118; -.
DR Ensembl; ENST00000356386.6; ENSP00000348751.2; ENSG00000186470.14. [P78410-1]
DR Ensembl; ENST00000377708.7; ENSP00000366937.2; ENSG00000186470.14. [P78410-1]
DR Ensembl; ENST00000396934.7; ENSP00000380140.3; ENSG00000186470.14. [P78410-2]
DR Ensembl; ENST00000396948.5; ENSP00000380152.1; ENSG00000186470.14. [P78410-1]
DR Ensembl; ENST00000508906.6; ENSP00000442687.1; ENSG00000186470.14. [P78410-3]
DR Ensembl; ENST00000527422.5; ENSP00000432138.1; ENSG00000186470.14. [P78410-1]
DR GeneID; 11118; -.
DR KEGG; hsa:11118; -.
DR MANE-Select; ENST00000377708.7; ENSP00000366937.2; NM_007047.5; NP_008978.2.
DR UCSC; uc003nhp.5; human. [P78410-1]
DR CTD; 11118; -.
DR DisGeNET; 11118; -.
DR GeneCards; BTN3A2; -.
DR HGNC; HGNC:1139; BTN3A2.
DR HPA; ENSG00000186470; Tissue enhanced (lymphoid).
DR MIM; 613594; gene.
DR neXtProt; NX_P78410; -.
DR OpenTargets; ENSG00000186470; -.
DR PharmGKB; PA25460; -.
DR VEuPathDB; HostDB:ENSG00000186470; -.
DR eggNOG; ENOG502QSRZ; Eukaryota.
DR GeneTree; ENSGT00940000162723; -.
DR InParanoid; P78410; -.
DR OMA; LHTPCSA; -.
DR OrthoDB; 522383at2759; -.
DR PhylomeDB; P78410; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; P78410; -.
DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR SignaLink; P78410; -.
DR BioGRID-ORCS; 11118; 16 hits in 1062 CRISPR screens.
DR ChiTaRS; BTN3A2; human.
DR GenomeRNAi; 11118; -.
DR Pharos; P78410; Tbio.
DR PRO; PR:P78410; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P78410; protein.
DR Bgee; ENSG00000186470; Expressed in granulocyte and 192 other tissues.
DR ExpressionAtlas; P78410; baseline and differential.
DR Genevisible; P78410; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
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 Gene3D; 2.60.40.10; -; 2.
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 Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Coiled coil; Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..334
FT /note="Butyrophilin subfamily 3 member A2"
FT /id="PRO_0000014533"
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..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..139
FT /note="Ig-like V-type"
FT COILED 272..319
FT /evidence="ECO:0000255"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_045906"
FT VAR_SEQ 1..28
FT /note="MKMASSLAFLLLNFHVSLLLVQLLTPCS -> MGIPR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045907"
FT VARIANT 167
FT /note="R -> T (in dbSNP:rs9379861)"
FT /id="VAR_049833"
FT VARIANT 181
FT /note="N -> D (in dbSNP:rs9358936)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_026211"
FT VARIANT 182
FT /note="A -> T (in dbSNP:rs12205731)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049834"
FT VARIANT 211
FT /note="R -> K (in dbSNP:rs35183513)"
FT /id="VAR_049835"
FT VARIANT 307
FT /note="S -> N (in dbSNP:rs13216828)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_049836"
FT CONFLICT 63
FT /note="M -> L (in Ref. 4; BAG64615)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="S -> G (in Ref. 3; AAF76140)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..212
FT /note="RG -> KS (in Ref. 3; AAF76140)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="S -> L (in Ref. 2; AAC02655)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:4F8Q"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4F8Q"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4F8Q"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4F8Q"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4F8Q"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:4F8Q"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 133..145
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 161..173
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4F8Q"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:4F8Q"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:4F8Q"
SQ SEQUENCE 334 AA; 36428 MW; 940519D57F95EEE4 CRC64;
MKMASSLAFL LLNFHVSLLL VQLLTPCSAQ FSVLGPSGPI LAMVGEDADL PCHLFPTMSA
ETMELKWVSS SLRQVVNVYA DGKEVEDRQS APYRGRTSIL RDGITAGKAA LRIHNVTASD
SGKYLCYFQD GDFYEKALVE LKVAALGSNL HVEVKGYEDG GIHLECRSTG WYPQPQIQWS
NAKGENIPAV EAPVVADGVG LYEVAASVIM RGGSGEGVSC IIRNSLLGLE KTASISIADP
FFRSAQPWIA ALAGTLPILL LLLAGASYFL WRQQKEITAL SSEIESEQEM KEMGYAATER
EISLRESLQE ELKRKKIQYL TRGEESSSDT NKSA
