HEMA_I68A0
ID HEMA_I68A0 Reviewed; 566 AA.
AC P03437; A0PC85; Q67132;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 29-SEP-2021, entry version 154.
DE RecName: Full=Hemagglutinin {ECO:0000255|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA1 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE Contains:
DE RecName: Full=Hemagglutinin HA2 chain {ECO:0000255|HAMAP-Rule:MF_04072};
DE Flags: Precursor;
GN Name=HA {ECO:0000255|HAMAP-Rule:MF_04072};
OS Influenza A virus (strain A/Aichi/2/1968 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=387139;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7402351; DOI=10.1038/286771a0;
RA Verhoeyen M., Fang R., Jou W.M., Devos R., Huylebroeck D., Saman E.,
RA Fiers W.;
RT "Antigenic drift between the haemagglutinin of the Hong Kong influenza
RT strains A/Aichi/2/68 and A/Victoria/3/75.";
RL Nature 286:771-776(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Min J.W., Verhoeyen M., Fang R.-X., Devos R., Huylebroeck D., Fiers W.;
RT "Shift and drift in influenza viruses.";
RL (In) Carlile M.J., Collins J.F., Moseley B.E.B. (eds.);
RL Symposium of the Society for General Microbiology, pp.285-311, Cambridge
RL University Press, New York (1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15331693; DOI=10.1128/jvi.78.18.9605-9611.2004;
RA Abe Y., Takashita E., Sugawara K., Matsuzaki Y., Muraki Y., Hongo S.;
RT "Effect of the addition of oligosaccharides on the biological activities
RT and antigenicity of influenza A/H3N2 virus hemagglutinin.";
RL J. Virol. 78:9605-9611(2004).
RN [4]
RP CLEAVAGE.
RX PubMed=9089405; DOI=10.1093/oxfordjournals.jbchem.a021588;
RA Beppu Y., Imamura Y., Tashiro M., Towatari T., Ariga H., Kido H.;
RT "Human mucus protease inhibitor in airway fluids is a potential defensive
RT compound against infection with influenza A and Sendai viruses.";
RL J. Biochem. 121:309-316(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=7464906; DOI=10.1038/289366a0;
RA Wilson I.A., Skehel J.J., Wiley D.C.;
RT "Structure of the haemagglutinin membrane glycoprotein of influenza virus
RT at 3-A resolution.";
RL Nature 289:366-373(1981).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=3374584; DOI=10.1038/333426a0;
RA Weis W.I., Brown J.H., Cusack S.C., Paulson J.C., Skehel J.J., Wiley D.C.;
RT "Structure of the influenza virus haemagglutinin complexed with its
RT receptor, sialic acid.";
RL Nature 333:426-431(1988).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF A MUTANT WITH GLY-457.
RX PubMed=2295311; DOI=10.1002/j.1460-2075.1990.tb08075.x;
RA Weis W.I., Cusack S.C., Brown J.H., Daniels R.S., Skehel J.J., Wiley D.C.;
RT "The structure of a membrane fusion mutant of the influenza virus
RT haemagglutinin.";
RL EMBO J. 9:17-24(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=2329580; DOI=10.1016/0022-2836(90)90234-d;
RA Weis W.I., Bruenger A.T., Skehel J.J., Wiley D.C.;
RT "Refinement of the influenza virus hemagglutinin by simulated annealing.";
RL J. Mol. Biol. 212:737-761(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8072525; DOI=10.1038/371037a0;
RA Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C.;
RT "Structure of influenza haemagglutinin at the pH of membrane fusion.";
RL Nature 371:37-43(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
RX PubMed=9461077; DOI=10.1038/nsb0298-119;
RA Fleury D., Wharton S.A., Skehel J.J., Knossow M., Bizebard T.;
RT "Antigen distortion allows influenza virus to escape neutralization.";
RL Nat. Struct. Biol. 5:119-123(1998).
CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC surface, bringing about the attachment of the virus particle to the
CC cell. This attachment induces virion internalization of about two third
CC of the virus particles through clathrin-dependent endocytosis and about
CC one third through a clathrin- and caveolin-independent pathway. Plays a
CC major role in the determination of host range restriction and
CC virulence. Class I viral fusion protein. Responsible for penetration of
CC the virus into the cell cytoplasm by mediating the fusion of the
CC membrane of the endocytosed virus particle with the endosomal membrane.
CC Low pH in endosomes induces an irreversible conformational change in
CC HA2, releasing the fusion hydrophobic peptide. Several trimers are
CC required to form a competent fusion pore.
CC -!- FUNCTION: Binds to sialic acid-containing receptors on the cell
CC surface, bringing about the attachment of the virus particle to the
CC cell. This attachment induces virion internalization either through
CC clathrin-dependent endocytosis or through clathrin- and caveolin-
CC independent pathway. Plays a major role in the determination of host
CC range restriction and virulence. Class I viral fusion protein.
CC Responsible for penetration of the virus into the cell cytoplasm by
CC mediating the fusion of the membrane of the endocytosed virus particle
CC with the endosomal membrane. Low pH in endosomes induces an
CC irreversible conformational change in HA2, releasing the fusion
CC hydrophobic peptide. Several trimers are required to form a competent
CC fusion pore. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked HA1-HA2. {ECO:0000255|HAMAP-
CC Rule:MF_04072}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04072}. Note=Targeted to the apical plasma membrane in
CC epithelial polarized cells through a signal present in the
CC transmembrane domain. Associated with glycosphingolipid- and
CC cholesterol-enriched detergent-resistant lipid rafts.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.
CC -!- PTM: In natural infection, inactive HA is matured into HA1 and HA2
CC outside the cell by one or more trypsin-like, arginine-specific
CC endoprotease secreted by the bronchial epithelial cells. One identified
CC protease that may be involved in this process is secreted in lungs by
CC Clara cells. {ECO:0000255|HAMAP-Rule:MF_04072,
CC ECO:0000269|PubMed:9089405}.
CC -!- MISCELLANEOUS: Major glycoprotein, comprises over 80% of the envelope
CC proteins present in virus particle.
CC -!- MISCELLANEOUS: The extent of infection into host organism is determined
CC by HA. Influenza viruses bud from the apical surface of polarized
CC epithelial cells (e.g. bronchial epithelial cells) into lumen of lungs
CC and are therefore usually pneumotropic. The reason is that HA is
CC cleaved by tryptase clara which is restricted to lungs. However, HAs of
CC H5 and H7 pantropic avian viruses subtypes can be cleaved by furin and
CC subtilisin-type enzymes, allowing the virus to grow in other organs
CC than lungs.
CC -!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
CC Genetic variation of hemagglutinin and/or neuraminidase genes results
CC in the emergence of new influenza strains. The mechanism of variation
CC can be the result of point mutations or the result of genetic
CC reassortment between segments of two different strains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the influenza viruses hemagglutinin family.
CC {ECO:0000255|HAMAP-Rule:MF_04072}.
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DR EMBL; J02090; AAA43178.1; -; Genomic_RNA.
DR EMBL; V01085; CAA24269.1; -; Genomic_RNA.
DR EMBL; M55059; AAA43239.1; -; Genomic_RNA.
DR EMBL; AB284320; BAF37221.1; -; Genomic_RNA.
DR PIR; A93231; HMIVHA.
DR PDB; 1EO8; X-ray; 2.80 A; A=17-344, B=346-520.
DR PDB; 1FYT; X-ray; 2.60 A; C=322-334.
DR PDB; 1HA0; X-ray; 2.80 A; A=25-518.
DR PDB; 1HGG; X-ray; 2.90 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 1HTM; X-ray; 2.50 A; A/C/E=17-43, B/D/F=383-520.
DR PDB; 1J8H; X-ray; 2.40 A; C=322-334.
DR PDB; 1KEN; X-ray; 3.50 A; B/D/F=346-520.
DR PDB; 1KG0; X-ray; 2.65 A; D=322-334.
DR PDB; 1PYW; X-ray; 2.10 A; C=324-332.
DR PDB; 1QFU; X-ray; 2.80 A; B=346-520.
DR PDB; 1QU1; X-ray; 1.90 A; A/B/C/D/E/F=376-530.
DR PDB; 2HMG; X-ray; 3.00 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 2VIR; X-ray; 3.25 A; C=44-325.
DR PDB; 2VIS; X-ray; 3.25 A; C=44-325.
DR PDB; 2VIT; X-ray; 3.25 A; C=44-325.
DR PDB; 2VIU; X-ray; 2.50 A; A=17-344, B=346-520.
DR PDB; 2YPG; X-ray; 2.85 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 3EYM; X-ray; 2.80 A; A/C/E=25-345, B/D/F=346-517.
DR PDB; 3HMG; X-ray; 2.90 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 3S4S; X-ray; 2.40 A; C/F=322-334.
DR PDB; 3S5L; X-ray; 2.10 A; C/F=322-334.
DR PDB; 3VUN; X-ray; 3.00 A; A/C/E=17-345, B/D/F=346-520.
DR PDB; 4C56; X-ray; 2.90 A; F/L=322-334.
DR PDB; 4HMG; X-ray; 3.00 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 5HMG; X-ray; 3.20 A; A/C/E=17-344, B/D/F=346-520.
DR PDB; 6E56; X-ray; 2.00 A; A/D=53-335.
DR PDB; 6N5D; X-ray; 3.00 A; A/B/K=53-334.
DR PDB; 6N5E; X-ray; 3.00 A; A/B/C=53-334.
DR PDB; 6XPX; X-ray; 2.60 A; A=53-335.
DR PDB; 6Y5L; EM; 3.60 A; B/D/F=346-517.
DR PDBsum; 1EO8; -.
DR PDBsum; 1FYT; -.
DR PDBsum; 1HA0; -.
DR PDBsum; 1HGG; -.
DR PDBsum; 1HTM; -.
DR PDBsum; 1J8H; -.
DR PDBsum; 1KEN; -.
DR PDBsum; 1KG0; -.
DR PDBsum; 1PYW; -.
DR PDBsum; 1QFU; -.
DR PDBsum; 1QU1; -.
DR PDBsum; 2HMG; -.
DR PDBsum; 2VIR; -.
DR PDBsum; 2VIS; -.
DR PDBsum; 2VIT; -.
DR PDBsum; 2VIU; -.
DR PDBsum; 2YPG; -.
DR PDBsum; 3EYM; -.
DR PDBsum; 3HMG; -.
DR PDBsum; 3S4S; -.
DR PDBsum; 3S5L; -.
DR PDBsum; 3VUN; -.
DR PDBsum; 4C56; -.
DR PDBsum; 4HMG; -.
DR PDBsum; 5HMG; -.
DR PDBsum; 6E56; -.
DR PDBsum; 6N5D; -.
DR PDBsum; 6N5E; -.
DR PDBsum; 6XPX; -.
DR PDBsum; 6Y5L; -.
DR BMRB; P03437; -.
DR SMR; P03437; -.
DR DIP; DIP-45342N; -.
DR IntAct; P03437; 1.
DR BindingDB; P03437; -.
DR ChEMBL; CHEMBL1932897; -.
DR DrugBank; DB07726; t-Butylhydroquinone.
DR UniLectin; P03437; -.
DR PRIDE; P03437; -.
DR ABCD; P03437; 15 sequenced antibodies.
DR EvolutionaryTrace; P03437; -.
DR Proteomes; UP000137932; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:InterPro.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.90.209.20; -; 1.
DR HAMAP; MF_04072; INFV_HEMA; 1.
DR InterPro; IPR008980; Capsid_hemagglutn.
DR InterPro; IPR013828; Hemagglutn_HA1_a/b_dom_sf.
DR InterPro; IPR000149; Hemagglutn_influenz_A.
DR InterPro; IPR001364; Hemagglutn_influenz_A/B.
DR Pfam; PF00509; Hemagglutinin; 1.
DR PRINTS; PR00330; HEMAGGLUTN1.
DR PRINTS; PR00329; HEMAGGLUTN12.
DR SUPFAM; SSF49818; SSF49818; 1.
PE 1: Evidence at protein level;
KW 3D-structure;
KW Clathrin- and caveolin-independent endocytosis of virus by host;
KW Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; Hemagglutinin;
KW Host cell membrane; Host membrane; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CHAIN 17..566
FT /note="Hemagglutinin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000440411"
FT CHAIN 17..344
FT /note="Hemagglutinin HA1 chain"
FT /id="PRO_0000038885"
FT CHAIN 346..566
FT /note="Hemagglutinin HA2 chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT /id="PRO_0000038886"
FT TOPO_DOM 17..530
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT TOPO_DOM 552..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT SITE 345..346
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 555
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 562
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT LIPID 565
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 30..482
FT /note="Interchain (between HA1 and HA2 chains)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 68..293
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 80..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 113..155
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 297..321
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT DISULFID 489..493
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072"
FT CONFLICT 14
FT /note="A -> P (in Ref. 2; AAA43239)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="L -> I (in Ref. 3; BAF37221)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="G -> S (in Ref. 3; BAF37221)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="I -> V (in Ref. 3; BAF37221)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="R -> G (in Ref. 3; BAF37221)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="E -> D (in Ref. 3; BAF37221)"
FT /evidence="ECO:0000305"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6E56"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:6E56"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6E56"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6E56"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1HA0"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:6E56"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:6N5E"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 258..265
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6E56"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1HA0"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:2VIU"
FT HELIX 383..449
FT /evidence="ECO:0007829|PDB:1QU1"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:1HTM"
FT HELIX 458..470
FT /evidence="ECO:0007829|PDB:1QU1"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:2VIU"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:1QU1"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:1KEN"
FT HELIX 491..499
FT /evidence="ECO:0007829|PDB:1QU1"
FT HELIX 504..515
FT /evidence="ECO:0007829|PDB:2VIU"
FT TURN 516..519
FT /evidence="ECO:0007829|PDB:1HGG"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:1QU1"
SQ SEQUENCE 566 AA; 63416 MW; E395659C23CAFECA CRC64;
MKTIIALSYI FCLALGQDLP GNDNSTATLC LGHHAVPNGT LVKTITDDQI EVTNATELVQ
SSSTGKICNN PHRILDGIDC TLIDALLGDP HCDVFQNETW DLFVERSKAF SNCYPYDVPD
YASLRSLVAS SGTLEFITEG FTWTGVTQNG GSNACKRGPG SGFFSRLNWL TKSGSTYPVL
NVTMPNNDNF DKLYIWGIHH PSTNQEQTSL YVQASGRVTV STRRSQQTII PNIGSRPWVR
GLSSRISIYW TIVKPGDVLV INSNGNLIAP RGYFKMRTGK SSIMRSDAPI DTCISECITP
NGSIPNDKPF QNVNKITYGA CPKYVKQNTL KLATGMRNVP EKQTRGLFGA IAGFIENGWE
GMIDGWYGFR HQNSEGTGQA ADLKSTQAAI DQINGKLNRV IEKTNEKFHQ IEKEFSEVEG
RIQDLEKYVE DTKIDLWSYN AELLVALENQ HTIDLTDSEM NKLFEKTRRQ LRENAEEMGN
GCFKIYHKCD NACIESIRNG TYDHDVYRDE ALNNRFQIKG VELKSGYKDW ILWISFAISC
FLLCVVLLGF IMWACQRGNI RCNICI
