ID HEMA_I34A1 Reviewed; 565 AA. AC P03452; A4GXH4; Q20N38; Q83964; Q8JUU5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 2. DT 02-SEP-2026, entry version 168. 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/Puerto Rico/8/1934 H1N1). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=211044; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=7278968; DOI=10.1038/292072a0; RA Winter G., Fields S., Brownlee G.G.; RT "Nucleotide sequence of the haemagglutinin gene of a human influenza virus RT H1 subtype."; RL Nature 292:72-75(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=11779399; DOI=10.1098/rstb.2001.0979; RA Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L., RA Garcia-Sastre A., Palese P.; RT "Plasmid-only rescue of influenza A virus vaccine candidates."; RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS. RX PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028; RA de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F., RA Osterhaus A.D.M.E., Fouchier R.A.M.; RT "Efficient generation and growth of influenza virus A/PR/8/34 from eight RT cDNA fragments."; RL Virus Res. 103:155-161(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RC STRAIN=Isolate EE12/E1; RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V., RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H., RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y., RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.; RT "The NIAID influenza genome sequencing project."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 18-343. RX PubMed=6186384; DOI=10.1016/0092-8674(82)90135-0; RA Caton A.J., Brownlee G.G., Yewdell J.W., Gerhard W.; RT "The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 RT subtype)."; RL Cell 31:417-427(1982). RN [6] RP INTERACTION WITH HUMAN CACNA1C. RX PubMed=29779930; DOI=10.1016/j.chom.2018.04.015; RA Fujioka Y., Nishide S., Ose T., Suzuki T., Kato I., Fukuhara H., RA Fujioka M., Horiuchi K., Satoh A.O., Nepal P., Kashiwagi S., Wang J., RA Horiguchi M., Sato Y., Paudel S., Nanbo A., Miyazaki T., Hasegawa H., RA Maenaka K., Ohba Y.; RT "Channel Binds Hemagglutinin and Mediates Influenza A Virus Entry into RT Mammalian Cells."; RL Cell Host Microbe 23:809-818(2018). 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. Interacts with human CC CACNA1C (PubMed:29779930). {ECO:0000255|HAMAP-Rule:MF_04072, CC ECO:0000269|PubMed:29779930}. CC -!- INTERACTION: CC P03452; PRO_0000000092 [P05067]: APP; Xeno; NbExp=2; IntAct=EBI-2548105, EBI-821758; CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072, CC ECO:0000305}; Single-pass type I membrane protein {ECO:0000255|HAMAP- CC Rule:MF_04072, ECO:0000305}. Host apical cell membrane CC {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}. Note=Targeted to the CC apical plasma membrane in epithelial polarized cells through a signal CC present in the transmembrane domain. Associated with CC glycosphingolipid- and cholesterol-enriched detergent-resistant lipid CC rafts. {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 club cells. {ECO:0000255|HAMAP-Rule:MF_04072}. 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 consists 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V01088; CAA24272.1; -; Genomic_RNA. DR EMBL; AF389118; AAM75158.1; -; Genomic_RNA. DR EMBL; EF467821; ABO21709.1; -; Genomic_RNA. DR EMBL; CY009444; ABD77675.1; -; Genomic_RNA. DR EMBL; J02144; AAA43194.1; -; Genomic_RNA. DR RefSeq; NP_040980.1; NC_002017.1. DR PDB; 1RU7; X-ray; 2.30 A; A/C/E/G/I/K=18-338, B/D/F/H/J/L=344-503. DR PDB; 1RVX; X-ray; 2.20 A; A/C/E/G/I/K=14-338, B/D/F/H/J/L=344-503. DR PDB; 1RVZ; X-ray; 2.25 A; A/C/E/G/I/K=14-338, B/D/F/H/J/L=344-503. DR PDB; 5VLI; X-ray; 1.80 A; A=17-343, B=344-519. DR PDB; 5W5S; X-ray; 2.28 A; A=18-343, B=344-519. DR PDB; 5W5U; X-ray; 2.46 A; A=18-343, B=344-519. DR PDB; 5W6I; X-ray; 3.10 A; A=18-343, B=344-519. DR PDB; 5W6R; X-ray; 2.73 A; A/C/E/G=18-343, B/D/F/H=344-519. DR PDB; 5W6T; X-ray; 2.59 A; A=18-343, B=344-519. DR PDB; 5W6U; X-ray; 2.88 A; A=18-343, B=344-519. DR PDB; 6WCR; X-ray; 2.68 A; A=18-343, B=344-519. DR PDB; 8SD2; X-ray; 2.81 A; A=18-343, B=344-519. DR PDB; 8SD4; X-ray; 3.11 A; A=18-343, B=344-519. DR PDB; 8VQL; X-ray; 2.29 A; A=18-339, B=344-565. DR PDB; 8VQM; X-ray; 2.21 A; A=18-339, B=344-565. DR PDB; 8VQN; X-ray; 2.21 A; A=18-339, B=344-565. DR PDB; 8VQQ; X-ray; 2.05 A; A=18-338, B=344-565. DR PDB; 9DXX; X-ray; 2.37 A; A=18-343, B=344-519. DR PDB; 9N8P; EM; 9.00 A; A/C/E/G/I/K=17-338, B/D/F/H/J/L=345-503. DR PDB; 9PHD; X-ray; 1.59 A; C=18-343, D=344-519. DR PDB; 9PHQ; X-ray; 2.87 A; A=18-343, B=344-519. DR PDB; 9PHS; X-ray; 2.02 A; A/C/E=18-343, B/D/F=344-519. DR PDB; 9PIB; X-ray; 2.35 A; A/C/E/G=18-343, B/D/F/H=344-519. DR MDRepo; P03452; -. DR SMR; P03452; -. DR IntAct; P03452; 38. DR MINT; P03452; -. DR BindingDB; P03452; -. DR ChEMBL; CHEMBL1075313; -. DR DrugCentral; P03452; -. DR UniLectin; P03452; -. DR GlyCosmos; P03452; 6 sites, No reported glycans. DR ABCD; P03452; 63 sequenced antibodies. DR GeneID; 956529; -. DR KEGG; vg:956529; -. DR OrthoDB; 2813at10239; -. DR Reactome; R-HSA-168255; Influenza Infection. DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis. DR Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome. DR Reactome; R-HSA-168298; Release. DR Reactome; R-HSA-168302; Budding. DR Reactome; R-HSA-168303; Packaging of Eight RNA Segments. DR Reactome; R-HSA-168316; Assembly of Viral Components at the Budding Site. DR Reactome; R-HSA-168336; Uncoating of the Influenza Virion. DR Reactome; R-HSA-168874; Transport of HA trimer, NA tetramer and M2 tetramer from the endoplasmic reticulum to the Golgi Apparatus. DR Reactome; R-HSA-192823; Viral mRNA Translation. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR EvolutionaryTrace; P03452; -. DR PRO; PR:P03452; -. DR Proteomes; UP000009255; Genome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; TAS:Reactome. 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; IDA:UniProtKB. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR FunFam; 3.90.20.10:FF:000002; Hemagglutinin; 1. DR Gene3D; 3.90.20.10; -; 1. DR Gene3D; 3.90.209.20; -; 1. DR Gene3D; 2.10.77.10; Hemagglutinin Chain A, Domain 2; 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; SSF58064; Influenza hemagglutinin (stalk); 1. DR SUPFAM; SSF49818; Viral protein domain; 1. DR PDBsum; 1RU7; -. DR PDBsum; 1RVX; -. DR PDBsum; 1RVZ; -. DR PDBsum; 5VLI; -. DR PDBsum; 5W5S; -. DR PDBsum; 5W5U; -. DR PDBsum; 5W6I; -. DR PDBsum; 5W6R; -. DR PDBsum; 5W6T; -. DR PDBsum; 5W6U; -. DR PDBsum; 6WCR; -. DR PDBsum; 8SD2; -. DR PDBsum; 8SD4; -. DR PDBsum; 8VQL; -. DR PDBsum; 8VQM; -. DR PDBsum; 8VQN; -. DR PDBsum; 8VQQ; -. DR PDBsum; 9DXX; -. DR PDBsum; 9N8P; -. DR PDBsum; 9PHD; -. DR PDBsum; 9PHQ; -. DR PDBsum; 9PHS; -. DR PDBsum; 9PIB; -. 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; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; 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..17 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CHAIN 18..565 FT /note="Hemagglutinin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT /id="PRO_0000440377" FT CHAIN 18..342 FT /note="Hemagglutinin HA1 chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT /id="PRO_0000039034" FT CHAIN 344..565 FT /note="Hemagglutinin HA2 chain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT /id="PRO_0000039035" FT TOPO_DOM 18..528 FT /note="Extracellular" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT TRANSMEM 529..549 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT TOPO_DOM 550..565 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT SITE 343..344 FT /note="Cleavage; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT LIPID 554 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT LIPID 561 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT LIPID 564 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 27 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 28 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 285 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 303 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CARBOHYD 497 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 21..480 FT /note="Interchain (between HA1 and HA2 chains)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 59..291 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 72..84 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 107..152 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 295..319 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT DISULFID 487..491 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04072" FT CONFLICT 10 FT /note="C -> S (in Ref. 2; AAM75158)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="N -> TK (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="E -> A (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="P -> S (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="E -> D (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="L -> I (in Ref. 1; CAA24272 and 2; AAM75158)" FT /evidence="ECO:0000305" FT CONFLICT 268 FT /note="M -> R (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 308 FT /note="Y -> F (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="I -> N (in Ref. 3; ABO21709)" FT /evidence="ECO:0000305" FT CONFLICT 397 FT /note="T -> S (in Ref. 1; CAA24272)" FT /evidence="ECO:0000305" FT STRAND 19..25 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:8VQM" FT STRAND 39..48 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 67..70 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 74..79 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 82..87 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:8VQQ" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:1RVX" FT HELIX 115..122 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 125..134 FT /evidence="ECO:0007829|PDB:5VLI" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 143..145 FT /evidence="ECO:0007829|PDB:9DXX" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 162..166 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:1RVX" FT STRAND 177..182 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 185..187 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 189..197 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 201..208 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:5W5S" FT STRAND 239..250 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 255..262 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 269..275 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 287..297 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 315..319 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:5VLI" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 357..359 FT /evidence="ECO:0007829|PDB:5W6I" FT STRAND 364..371 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 374..379 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 381..401 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 405..408 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 418..469 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 473..477 FT /evidence="ECO:0007829|PDB:5VLI" FT STRAND 480..485 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 489..496 FT /evidence="ECO:0007829|PDB:5VLI" FT HELIX 502..512 FT /evidence="ECO:0007829|PDB:5VLI" SQ SEQUENCE 565 AA; 63353 MW; 47F34821748F494E CRC64; MKANLLVLLC ALAAADADTI CIGYHANNST DTVDTVLEKN VTVTHSVNLL EDSHNGKLCR LKGIAPLQLG KCNIAGWLLG NPECDPLLPV RSWSYIVETP NSENGICYPG DFIDYEELRE QLSSVSSFER FEIFPKESSW PNHNTNGVTA ACSHEGKSSF YRNLLWLTEK EGSYPKLKNS YVNKKGKEVL VLWGIHHPPN SKEQQNLYQN ENAYVSVVTS NYNRRFTPEI AERPKVRDQA GRMNYYWTLL KPGDTIIFEA NGNLIAPMYA FALSRGFGSG IITSNASMHE CNTKCQTPLG AINSSLPYQN IHPVTIGECP KYVRSAKLRM VTGLRNIPSI QSRGLFGAIA GFIEGGWTGM IDGWYGYHHQ NEQGSGYAAD QKSTQNAING ITNKVNTVIE KMNIQFTAVG KEFNKLEKRM ENLNKKVDDG FLDIWTYNAE LLVLLENERT LDFHDSNVKN LYEKVKSQLK NNAKEIGNGC FEFYHKCDNE CMESVRNGTY DYPKYSEESK LNREKVDGVK LESMGIYQIL AIYSTVASSL VLLVSLGAIS FWMCSNGSLQ CRICI //