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Database: UniProt
Entry: P08637
LinkDB: P08637
Original site: P08637 
ID   FCG3A_HUMAN             Reviewed;         254 AA.
AC   P08637; A2N6W9; Q53FJ0; Q53FL6; Q5EBR4; Q65ZM6; Q6PIJ0;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   26-NOV-2014, entry version 166.
DE   RecName: Full=Low affinity immunoglobulin gamma Fc region receptor III-A;
DE   AltName: Full=CD16a antigen;
DE   AltName: Full=Fc-gamma RIII-alpha;
DE            Short=Fc-gamma RIII;
DE            Short=Fc-gamma RIIIa;
DE            Short=FcRIII;
DE            Short=FcRIIIa;
DE   AltName: Full=FcR-10;
DE   AltName: Full=IgG Fc receptor III-2;
DE   AltName: CD_antigen=CD16a;
DE   Flags: Precursor;
GN   Name=FCGR3A; Synonyms=CD16A, FCG3, FCGR3, IGFR3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2526846; DOI=10.1084/jem.170.2.481;
RA   Ravetch J.V., Perussia B.;
RT   "Alternative membrane forms of Fc gamma RIII(CD16) on human natural
RT   killer cells and neutrophils. Cell type-specific expression of two
RT   genes that differ in single nucleotide substitutions.";
RL   J. Exp. Med. 170:481-497(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RX   PubMed=16951347; DOI=10.4049/jimmunol.177.6.3848;
RA   Rogers K.A., Scinicariello F., Attanasio R.;
RT   "IgG Fc receptor III homologues in nonhuman primate species: genetic
RT   characterization and ligand interactions.";
RL   J. Immunol. 177:3848-3856(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC   TISSUE=Synovium;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-176.
RC   TISSUE=Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC   TISSUE=Placenta;
RX   PubMed=7836402; DOI=10.1074/jbc.270.3.1350;
RA   Gessner J.E., Grussenmeyer T., Kolanus W., Schmidt R.E.;
RT   "The human low affinity immunoglobulin G Fc receptor III-A and III-B
RT   genes. Molecular characterization of the promoter regions.";
RL   J. Biol. Chem. 270:1350-1361(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-254, AND VARIANT VAL-176.
RX   PubMed=7700021; DOI=10.1038/ki.1994.462;
RA   Morcos M., Hansch G.M., Schonermark M., Ellwanger S., Harle M.,
RA   Heckl-Ostreicher B.;
RT   "Human glomerular mesangial cells express CD16 and may be stimulated
RT   via this receptor.";
RL   Kidney Int. 46:1627-1634(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-254.
RC   TISSUE=Lung;
RX   PubMed=2525780; DOI=10.1073/pnas.86.13.5079;
RA   Scallon B.J., Scigliano E., Freedman V.H., Miedel M.C., Pan Y.C.,
RA   Unkeless J.C., Kochan J.P.;
RT   "A human immunoglobulin G receptor exists in both polypeptide-anchored
RT   and phosphatidylinositol-glycan-anchored forms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5079-5083(1989).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-193 IN COMPLEX WITH IGHG1,
RP   FUNCTION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-63 AND ASN-180.
RX   PubMed=22023369; DOI=10.1111/j.1365-2443.2011.01552.x;
RA   Mizushima T., Yagi H., Takemoto E., Shibata-Koyama M., Isoda Y.,
RA   Iida S., Masuda K., Satoh M., Kato K.;
RT   "Structural basis for improved efficacy of therapeutic antibodies on
RT   defucosylation of their Fc glycans.";
RL   Genes Cells 16:1071-1080(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-208 IN COMPLEX WITH IGHG1,
RP   FUNCTION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-63 AND ASN-180.
RX   PubMed=21768335; DOI=10.1073/pnas.1108455108;
RA   Ferrara C., Grau S., Jager C., Sondermann P., Brunker P.,
RA   Waldhauer I., Hennig M., Ruf A., Rufer A.C., Stihle M., Umana P.,
RA   Benz J.;
RT   "Unique carbohydrate-carbohydrate interactions are required for high
RT   affinity binding between FcgammaRIII and antibodies lacking core
RT   fucose.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12669-12674(2011).
RN   [11]
RP   VARIANT IMD20 HIS-66, AND VARIANT ARG-66.
RX   PubMed=8609432;
RA   de Haas M., Koene H.R., Kleijer M., de Vries E., Simsek S.,
RA   van Tol M.J.D., Roos D., von dem Borne A.E.G.K.;
RT   "A triallelic Fc gamma receptor type IIIA polymorphism influences the
RT   binding of human IgG by NK cell Fc gamma RIIIa.";
RL   J. Immunol. 156:2948-2955(1996).
RN   [12]
RP   VARIANT VAL-176.
RX   PubMed=9242542;
RA   Koene H.R., Kleijer M., Algra J., Roos D., von dem Borne A.E.G.K.,
RA   de Haas M.;
RT   "Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by
RT   natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-
RT   48L/R/H phenotype.";
RL   Blood 90:1109-1114(1997).
RN   [13]
RP   VARIANT VAL-176.
RX   PubMed=9276722; DOI=10.1172/JCI119616;
RA   Wu J., Edberg J.C., Redecha P.B., Bansal V., Guyre P.M., Coleman K.,
RA   Salmon J.E., Kimberly R.P.;
RT   "A novel polymorphism of FcgammaRIIIa (CD16) alters receptor function
RT   and predisposes to autoimmune disease.";
RL   J. Clin. Invest. 100:1059-1070(1997).
RN   [14]
RP   RP VARIANT IMD20 HIS-66.
RX   PubMed=8874200;
RA   de Vries E., Koene H.R., Vossen J.M., Gratama J.W.,
RA   von dem Borne A.E., Waaijer J.L., Haraldsson A., de Haas M.,
RA   van Tol M.J.;
RT   "Identification of an unusual Fc gamma receptor IIIa (CD16) on natural
RT   killer cells in a patient with recurrent infections.";
RL   Blood 88:3022-3027(1996).
RN   [15]
RP   RP VARIANT IMD20 HIS-66.
RX   PubMed=8608639; DOI=10.1111/j.1365-2249.1996.tb08295.x;
RA   Jawahar S., Moody C., Chan M., Finberg R., Geha R., Chatila T.;
RT   "Natural Killer (NK) cell deficiency associated with an epitope-
RT   deficient Fc receptor type IIIA (CD16-II).";
RL   Clin. Exp. Immunol. 103:408-413(1996).
RN   [16]
RP   RP VARIANT IMD20 HIS-66.
RX   PubMed=23006327; DOI=10.1172/JCI64837;
RA   Grier J.T., Forbes L.R., Monaco-Shawver L., Oshinsky J.,
RA   Atkinson T.P., Moody C., Pandey R., Campbell K.S., Orange J.S.;
RT   "Human immunodeficiency-causing mutation defines CD16 in spontaneous
RT   NK cell cytotoxicity.";
RL   J. Clin. Invest. 122:3769-3780(2012).
CC   -!- FUNCTION: Receptor for the Fc region of IgG. Binds complexed or
CC       aggregated IgG and also monomeric IgG. Mediates antibody-dependent
CC       cellular cytotoxicity (ADCC) and other antibody-dependent
CC       responses, such as phagocytosis. {ECO:0000269|PubMed:21768335,
CC       ECO:0000269|PubMed:22023369}.
CC   -!- SUBUNIT: Exists as a heterooligomeric receptor complex with Fc
CC       epsilon receptor I gamma subunit and / or the CD3 zeta subunit.
CC       Interacts with INPP5D/SHIP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
CC       type I membrane protein {ECO:0000305}. Secreted. Note=Exists also
CC       as a soluble receptor.
CC   -!- TISSUE SPECIFICITY: Expressed on natural killer cells,
CC       macrophages, subpopulation of T-cells, immature thymocytes and
CC       placental trophoblasts.
CC   -!- PTM: Glycosylated. Contains high mannose- and complex-type
CC       oligosaccharides. Glycosylation at Asn-180 is mandatory for high
CC       affinity binding to the Fc and for discrimination between
CC       fucosylated and afucosylated IgG glycoforms.
CC       {ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369}.
CC   -!- PTM: The soluble form is produced by a proteolytic cleavage.
CC   -!- DISEASE: Immunodeficiency 20 (IMD20) [MIM:615707]: A rare
CC       autosomal recessive primary immunodeficiency characterized by
CC       functional deficiency of NK cells. Affected individuals typically
CC       present with severe herpes viral infections, particularly Epstein
CC       Barr virus (EBV), and human papillomavirus (HPV). Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry. {ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:8608639,
CC       ECO:0000269|PubMed:8609432, ECO:0000269|PubMed:8874200}.
CC   -!- MISCELLANEOUS: Encoded by one of two nearly indentical genes:
CC       FCGR3A (Shown here) and FCGR3B which are expressed in a tissue-
CC       specific manner. The Phe-203 in III-A determines the transmembrane
CC       domains whereas the 'Ser-203' in III-B determines the GPI-
CC       anchoring.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD96988.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Evidence={ECO:0000305};
CC       Sequence=BAD97015.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=FCGR3Abase; Note=FCGR3A mutation db;
CC       URL="http://bioinf.uta.fi/FCGR3Abase/";
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DR   EMBL; X52645; CAA36870.1; -; mRNA.
DR   EMBL; AK223268; BAD96988.1; ALT_INIT; mRNA.
DR   EMBL; AK223295; BAD97015.1; ALT_INIT; mRNA.
DR   EMBL; AL590385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017865; AAH17865.1; -; mRNA.
DR   EMBL; BC033678; AAH33678.1; -; mRNA.
DR   EMBL; Z46222; CAA86295.1; -; Genomic_DNA.
DR   EMBL; S76824; AAB33925.2; -; mRNA.
DR   EMBL; M24853; AAA53506.1; -; mRNA.
DR   CCDS; CCDS44266.1; -.
DR   PIR; JL0107; JL0107.
DR   RefSeq; NP_000560.5; NM_000569.6.
DR   RefSeq; NP_001121064.1; NM_001127592.1.
DR   RefSeq; NP_001121065.1; NM_001127593.1.
DR   RefSeq; NP_001121067.1; NM_001127595.1.
DR   RefSeq; NP_001121068.1; NM_001127596.1.
DR   UniGene; Hs.372679; -.
DR   PDB; 3AY4; X-ray; 2.20 A; C=21-193.
DR   PDB; 3SGJ; X-ray; 2.20 A; C=19-208.
DR   PDB; 3SGK; X-ray; 2.40 A; C=19-208.
DR   PDBsum; 3AY4; -.
DR   PDBsum; 3SGJ; -.
DR   PDBsum; 3SGK; -.
DR   ProteinModelPortal; P08637; -.
DR   SMR; P08637; 24-231.
DR   BioGrid; 108508; 8.
DR   IntAct; P08637; 3.
DR   STRING; 9606.ENSP00000356946; -.
DR   DrugBank; DB00054; Abciximab.
DR   DrugBank; DB00051; Adalimumab.
DR   DrugBank; DB00092; Alefacept.
DR   DrugBank; DB00087; Alemtuzumab.
DR   DrugBank; DB00074; Basiliximab.
DR   DrugBank; DB00112; Bevacizumab.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB00111; Daclizumab.
DR   DrugBank; DB00095; Efalizumab.
DR   DrugBank; DB00005; Etanercept.
DR   DrugBank; DB00056; Gemtuzumab ozogamicin.
DR   DrugBank; DB00078; Ibritumomab.
DR   DrugBank; DB00028; Intravenous Immunoglobulin.
DR   DrugBank; DB00075; Muromonab.
DR   DrugBank; DB00108; Natalizumab.
DR   DrugBank; DB00110; Palivizumab.
DR   DrugBank; DB00073; Rituximab.
DR   DrugBank; DB00081; Tositumomab.
DR   DrugBank; DB00072; Trastuzumab.
DR   MEROPS; I43.001; -.
DR   PhosphoSite; P08637; -.
DR   DMDM; 119876; -.
DR   PaxDb; P08637; -.
DR   PRIDE; P08637; -.
DR   DNASU; 2214; -.
DR   Ensembl; ENST00000367967; ENSP00000356944; ENSG00000203747.
DR   Ensembl; ENST00000436743; ENSP00000416607; ENSG00000203747.
DR   Ensembl; ENST00000443193; ENSP00000392047; ENSG00000203747.
DR   GeneID; 2214; -.
DR   KEGG; hsa:2214; -.
DR   UCSC; uc001gar.3; human.
DR   CTD; 2214; -.
DR   GeneCards; GC01M161511; -.
DR   HGNC; HGNC:3619; FCGR3A.
DR   HPA; CAB032435; -.
DR   HPA; HPA055431; -.
DR   MIM; 146740; gene.
DR   MIM; 615707; phenotype.
DR   neXtProt; NX_P08637; -.
DR   PharmGKB; PA28065; -.
DR   eggNOG; NOG47725; -.
DR   GeneTree; ENSGT00760000119130; -.
DR   HOVERGEN; HBG051602; -.
DR   InParanoid; P08637; -.
DR   KO; K06463; -.
DR   PhylomeDB; P08637; -.
DR   Reactome; REACT_11152; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; REACT_160086; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; REACT_160158; Role of phospholipids in phagocytosis.
DR   Reactome; REACT_160274; FCGR activation.
DR   ChiTaRS; FCGR3A; human.
DR   EvolutionaryTrace; P08637; -.
DR   GeneWiki; FCGR3A; -.
DR   GenomeRNAi; 2214; -.
DR   NextBio; 8979; -.
DR   PRO; PR:P08637; -.
DR   Bgee; P08637; -.
DR   CleanEx; HS_FCGR3A; -.
DR   ExpressionAtlas; P08637; baseline.
DR   Genevestigator; P08637; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   SMART; SM00409; IG; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; IgG-binding protein; Immunoglobulin domain; Membrane;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17    254       Low affinity immunoglobulin gamma Fc
FT                                region receptor III-A.
FT                                /FTId=PRO_0000015150.
FT   TOPO_DOM     17    208       Extracellular. {ECO:0000255}.
FT   TRANSMEM    209    229       Helical. {ECO:0000255}.
FT   TOPO_DOM    230    254       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       24    105       Ig-like C2-type 1.
FT   DOMAIN      107    189       Ig-like C2-type 2.
FT   CARBOHYD     56     56       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     63     63       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:21768335,
FT                                ECO:0000269|PubMed:22023369}.
FT   CARBOHYD     92     92       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    180    180       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:21768335,
FT                                ECO:0000269|PubMed:22023369}.
FT   CARBOHYD    187    187       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     47     89
FT   DISULFID    128    172
FT   VARIANT      66     66       L -> H (in IMD20; dbSNP:rs10127939).
FT                                {ECO:0000269|PubMed:23006327,
FT                                ECO:0000269|PubMed:8608639,
FT                                ECO:0000269|PubMed:8609432,
FT                                ECO:0000269|PubMed:8874200}.
FT                                /FTId=VAR_008800.
FT   VARIANT      66     66       L -> R (in dbSNP:rs10127939).
FT                                {ECO:0000269|PubMed:8609432}.
FT                                /FTId=VAR_008799.
FT   VARIANT     147    147       G -> D (in dbSNP:rs443082).
FT                                /FTId=VAR_058398.
FT   VARIANT     158    158       Y -> H (in dbSNP:rs396716).
FT                                /FTId=VAR_058399.
FT   VARIANT     176    176       F -> V (shows a higher binding capacity
FT                                of IgG1, IgG3 and IgG4; dbSNP:rs396991).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7700021,
FT                                ECO:0000269|PubMed:9242542,
FT                                ECO:0000269|PubMed:9276722,
FT                                ECO:0000269|Ref.3}.
FT                                /FTId=VAR_003960.
FT   VARIANT     203    203       F -> S (in dbSNP:rs1042206).
FT                                /FTId=VAR_058400.
FT   CONFLICT    106    106       I -> V (in Ref. 3; BAD96988/BAD97015).
FT                                {ECO:0000305}.
FT   CONFLICT    195    195       A -> S (in Ref. 5; AAH33678).
FT                                {ECO:0000305}.
FT   STRAND       28     33       {ECO:0000244|PDB:3AY4}.
FT   STRAND       35     38       {ECO:0000244|PDB:3AY4}.
FT   STRAND       43     47       {ECO:0000244|PDB:3AY4}.
FT   STRAND       51     54       {ECO:0000244|PDB:3SGJ}.
FT   STRAND       60     65       {ECO:0000244|PDB:3AY4}.
FT   STRAND       71     78       {ECO:0000244|PDB:3AY4}.
FT   HELIX        81     83       {ECO:0000244|PDB:3AY4}.
FT   STRAND       85     89       {ECO:0000244|PDB:3AY4}.
FT   STRAND      100    105       {ECO:0000244|PDB:3AY4}.
FT   STRAND      107    112       {ECO:0000244|PDB:3AY4}.
FT   STRAND      116    119       {ECO:0000244|PDB:3AY4}.
FT   STRAND      124    130       {ECO:0000244|PDB:3AY4}.
FT   HELIX       131    133       {ECO:0000244|PDB:3AY4}.
FT   STRAND      137    143       {ECO:0000244|PDB:3AY4}.
FT   STRAND      146    153       {ECO:0000244|PDB:3AY4}.
FT   STRAND      157    161       {ECO:0000244|PDB:3AY4}.
FT   HELIX       164    166       {ECO:0000244|PDB:3AY4}.
FT   STRAND      168    176       {ECO:0000244|PDB:3AY4}.
FT   STRAND      179    182       {ECO:0000244|PDB:3AY4}.
FT   STRAND      186    191       {ECO:0000244|PDB:3AY4}.
SQ   SEQUENCE   254 AA;  29089 MW;  D38D178D32C67337 CRC64;
     MWQLLLPTAL LLLVSAGMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA YSPEDNSTQW
     FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE
     EDPIHLRCHS WKNTALHKVT YLQNGKGRKY FHHNSDFYIP KATLKDSGSY FCRGLFGSKN
     VSSETVNITI TQGLAVSTIS SFFPPGYQVS FCLVMVLLFA VDTGLYFSVK TNIRSSTRDW
     KDHKFKWRKD PQDK
//
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