ID FETA_HUMAN Reviewed; 609 AA. AC P02771; B2RBU3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Alpha-fetoprotein; DE AltName: Full=Alpha-1-fetoprotein; DE AltName: Full=Alpha-fetoglobulin; DE Flags: Precursor; GN Name=AFP; Synonyms=HPAFP; 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]. RX PubMed=6192439; DOI=10.1073/pnas.80.15.4604; RA Morinaga T., Sakai M., Wegmann T.G., Tamaoki T.; RT "Primary structures of human alpha-fetoprotein and its mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 80:4604-4608(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2436661; DOI=10.1021/bi00379a020; RA Gibbs P.E.M., Zielinski R., Boyd C., Dugaiczyk A.; RT "Structure, polymorphism, and novel repeated DNA elements revealed by a RT complete sequence of the human alpha-fetoprotein gene."; RL Biochemistry 26:1332-1343(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-570. RC TISSUE=Heart; 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 MRNA]. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 AND 596-609, AND GENE STRUCTURE. RX PubMed=2580830; DOI=10.1016/s0021-9258(18)89178-5; RA Sakai M., Morinaga T., Urano Y., Watanabe K., Wegmann T.G., Tamaoki T.; RT "The human alpha-fetoprotein gene. Sequence organization and the 5' RT flanking region."; RL J. Biol. Chem. 260:5055-5060(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND INVOLVEMENT IN HPAFP. RX PubMed=7684942; DOI=10.1093/hmg/2.4.379; RA McVey J.H., Michaelides K., Hansen L.P., Ferguson-Smith M., Tilghman S., RA Krumlauf R., Tuddenham E.G.D.; RT "A G-->A substitution in an HNF I binding site in the human alpha- RT fetoprotein gene is associated with hereditary persistence of alpha- RT fetoprotein (HPAFP)."; RL Hum. Mol. Genet. 2:379-384(1993). RN [7] RP PROTEIN SEQUENCE OF 311-332; 348-372 AND 422-437, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 429-556. RX PubMed=6187626; DOI=10.1016/0378-1119(82)90210-4; RA Beattie W.G., Dugaiczyk A.; RT "Structure and evolution of human alpha-fetoprotein deduced from partial RT sequence of cloned cDNA."; RL Gene 20:415-422(1982). RN [9] RP PROTEIN SEQUENCE OF 19-609. RX PubMed=1709810; DOI=10.1021/bi00234a032; RA Pucci P., Siciliano R., Malorni A., Marino G., Tecce M.F., Ceccarini C., RA Terrana B.; RT "Human alpha-fetoprotein primary structure: a mass spectrometric study."; RL Biochemistry 30:5061-5066(1991). RN [10] RP PRELIMINARY PROTEIN SEQUENCE OF 19-35. RX PubMed=70228; DOI=10.1016/0005-2795(77)90198-2; RA Yachnin S., Hsu R., Heinrikson R.L., Miller J.B.; RT "Studies on human alpha-fetoprotein. Isolation and characterization of RT monomeric and polymeric forms and amino-terminal sequence analysis."; RL Biochim. Biophys. Acta 493:418-428(1977). RN [11] RP PRELIMINARY PROTEIN SEQUENCE OF 19-38. RX PubMed=71198; RA Aoyagi Y., Ikenaka T., Ichida F.; RT "Comparative chemical structures of human alpha-fetoproteins from fetal RT serum and from ascites fluid of a patient with hepatoma."; RL Cancer Res. 37:3663-3667(1977). RN [12] RP PRELIMINARY PROTEIN SEQUENCE OF 19-39. RX PubMed=4138095; RA Ruoslahti E., Pihko H., Vaheri A., Seppala M., Virolainen M., Konttinen A.; RT "Alpha fetoprotein: structure and expression in man and inbred mouse RT strains under normal conditions and liver injury."; RL Johns Hopkins Med. J. Suppl. 3:249-255(1974). RN [13] RP METAL-BINDING. RX PubMed=80265; RA Aoyagi Y., Ikenaka T., Ichida F.; RT "Copper(II)-binding ability of human alpha-fetoprotein."; RL Cancer Res. 38:3483-3486(1978). RN [14] RP BILIRUBIN-BINDING. RX PubMed=89900; RA Aoyagi Y., Ikenaka T., Ichida F.; RT "Alpha-fetoprotein as a carrier protein in plasma and its bilirubin-binding RT ability."; RL Cancer Res. 39:3571-3574(1979). RN [15] RP SULFATION. RX PubMed=2414772; DOI=10.1073/pnas.82.21.7160; RA Liu M.C., Yu S., Sy J., Redman C.M., Lipmann F.; RT "Tyrosine sulfation of proteins from the human hepatoma cell line HepG2."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7160-7164(1985). RN [16] RP INVOLVEMENT IN AFPD. RX PubMed=15280901; DOI=10.1038/sj.ejhg.5201246; RA Sharony R., Zadik I., Parvari R.; RT "Congenital deficiency of alpha feto-protein."; RL Eur. J. Hum. Genet. 12:871-874(2004). RN [17] RP INVOLVEMENT IN AFPD. RX PubMed=18854864; DOI=10.1038/ejhg.2008.186; RA Petit F.M., Hebert M., Picone O., Brisset S., Maurin M.L., Parisot F., RA Capel L., Benattar C., Senat M.V., Tachdjian G., Labrune P.; RT "A new mutation in the AFP gene responsible for a total absence of alpha RT feto-protein on second trimester maternal serum screening for Down RT syndrome."; RL Eur. J. Hum. Genet. 17:387-390(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION AT SER-111; SER-115; SER-117; SER-344; SER-444 AND SER-445. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). CC -!- FUNCTION: Binds copper, nickel, and fatty acids as well as, and CC bilirubin less well than, serum albumin. Only a small percentage (less CC than 2%) of the human AFP shows estrogen-binding properties. CC -!- SUBUNIT: Dimeric and trimeric forms have been found in addition to the CC monomeric form. CC -!- INTERACTION: CC P02771; PRO_0000045596 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-722498, EBI-6901449; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Plasma. Synthesized by the fetal liver and yolk CC sac. CC -!- DEVELOPMENTAL STAGE: Occurs in the plasma of fetuses more than 4 weeks CC old, reaches the highest levels during the 12th-16th week of gestation, CC and drops to trace amounts after birth. The serum level in adults is CC usually less than 40 ng/ml. AFP occurs also at high levels in the CC plasma and ascitic fluid of adults with hepatoma. CC -!- PTM: Independent studies suggest heterogeneity of the N-terminal CC sequence of the mature protein and of the cleavage site of the signal CC sequence. CC -!- PTM: Sulfated. {ECO:0000269|PubMed:2414772}. CC -!- DISEASE: Alpha-fetoprotein deficiency (AFPD) [MIM:615969]: A benign CC condition characterized by undetectable AFP levels in the amniotic CC fluid. Affected individuals are asymptomatic and present normal CC development. {ECO:0000269|PubMed:15280901, CC ECO:0000269|PubMed:18854864}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Alpha-fetoprotein, hereditary persistence (HPAFP) CC [MIM:615970]: A benign autosomal dominant condition characterized by CC continued expression of alpha-fetoprotein in adult life. CC {ECO:0000269|PubMed:7684942}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE- CC ProRule:PRU00769}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-fetoprotein entry; CC URL="https://en.wikipedia.org/wiki/Alpha-fetoprotein"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44248/AFP"; 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; V01514; CAA24758.1; -; mRNA. DR EMBL; M16110; AAB58754.1; -; Genomic_DNA. DR EMBL; AK314817; BAG37340.1; -; mRNA. DR EMBL; BC027881; AAH27881.1; -; mRNA. DR EMBL; M10949; AAA51674.1; -; Genomic_DNA. DR EMBL; M10950; AAA51675.1; -; Genomic_DNA. DR EMBL; Z19532; CAA79592.1; -; Genomic_DNA. DR CCDS; CCDS3556.1; -. DR PIR; A26624; FPHU. DR RefSeq; NP_001125.1; NM_001134.2. DR PDB; 3MRK; X-ray; 1.40 A; P=137-145. DR PDB; 7RE7; X-ray; 2.55 A; C/F=158-166. DR PDB; 7RE8; X-ray; 2.82 A; C/F=158-166. DR PDB; 7YIM; EM; 2.60 A; A=1-609. DR PDBsum; 3MRK; -. DR PDBsum; 7RE7; -. DR PDBsum; 7RE8; -. DR PDBsum; 7YIM; -. DR AlphaFoldDB; P02771; -. DR EMDB; EMD-33861; -. DR SMR; P02771; -. DR BioGRID; 106682; 24. DR IntAct; P02771; 11. DR STRING; 9606.ENSP00000379138; -. DR ChEMBL; CHEMBL3712864; -. DR GlyConnect; 41; 31 N-Linked glycans (2 sites). DR GlyCosmos; P02771; 2 sites, 48 glycans. DR GlyGen; P02771; 3 sites, 48 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P02771; -. DR PhosphoSitePlus; P02771; -. DR BioMuta; AFP; -. DR DMDM; 120042; -. DR jPOST; P02771; -. DR MassIVE; P02771; -. DR MaxQB; P02771; -. DR PaxDb; 9606-ENSP00000379138; -. DR PeptideAtlas; P02771; -. DR ProteomicsDB; 51589; -. DR TopDownProteomics; P02771; -. DR ABCD; P02771; 16 sequenced antibodies. DR Antibodypedia; 1359; 3835 antibodies from 58 providers. DR DNASU; 174; -. DR Ensembl; ENST00000395792.7; ENSP00000379138.2; ENSG00000081051.8. DR GeneID; 174; -. DR KEGG; hsa:174; -. DR MANE-Select; ENST00000395792.7; ENSP00000379138.2; NM_001134.3; NP_001125.1. DR UCSC; uc003hgz.3; human. DR AGR; HGNC:317; -. DR CTD; 174; -. DR DisGeNET; 174; -. DR GeneCards; AFP; -. DR HGNC; HGNC:317; AFP. DR HPA; ENSG00000081051; Tissue enriched (liver). DR MalaCards; AFP; -. DR MIM; 104150; gene. DR MIM; 615969; phenotype. DR MIM; 615970; phenotype. DR neXtProt; NX_P02771; -. DR OpenTargets; ENSG00000081051; -. DR Orphanet; 168612; Congenital deficiency in alpha-fetoprotein. DR Orphanet; 168615; Hereditary persistence of alpha-fetoprotein. DR PharmGKB; PA24614; -. DR VEuPathDB; HostDB:ENSG00000081051; -. DR eggNOG; ENOG502R7EA; Eukaryota. DR GeneTree; ENSGT00390000000113; -. DR HOGENOM; CLU_030161_1_0_1; -. DR InParanoid; P02771; -. DR OMA; HEECCRG; -. DR OrthoDB; 5196468at2759; -. DR PhylomeDB; P02771; -. DR TreeFam; TF335561; -. DR PathwayCommons; P02771; -. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR SignaLink; P02771; -. DR SIGNOR; P02771; -. DR BioGRID-ORCS; 174; 14 hits in 1151 CRISPR screens. DR ChiTaRS; AFP; human. DR GeneWiki; Alpha-fetoprotein; -. DR GenomeRNAi; 174; -. DR Pharos; P02771; Tbio. DR PRO; PR:P02771; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P02771; Protein. DR Bgee; ENSG00000081051; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 111 other cell types or tissues. DR ExpressionAtlas; P02771; baseline and differential. DR Genevisible; P02771; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl. DR GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl. DR CDD; cd00015; ALBUMIN; 3. DR Gene3D; 1.10.246.10; -; 6. DR InterPro; IPR000264; ALB/AFP/VDB. DR InterPro; IPR020858; Serum_albumin-like. DR InterPro; IPR021177; Serum_albumin/AFP/Afamin. DR InterPro; IPR020857; Serum_albumin_CS. DR InterPro; IPR014760; Serum_albumin_N. DR PANTHER; PTHR11385:SF7; ALPHA-FETOPROTEIN; 1. DR PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 1. DR Pfam; PF00273; Serum_albumin; 3. DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1. DR PRINTS; PR00803; AFETOPROTEIN. DR PRINTS; PR00802; SERUMALBUMIN. DR SMART; SM00103; ALBUMIN; 3. DR SUPFAM; SSF48552; Serum albumin-like; 3. DR PROSITE; PS00212; ALBUMIN_1; 2. DR PROSITE; PS51438; ALBUMIN_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Metal-binding; Nickel; Phosphoprotein; Reference proteome; KW Repeat; Secreted; Signal; Sulfation. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:1709810" FT CHAIN 19..609 FT /note="Alpha-fetoprotein" FT /id="PRO_0000001097" FT DOMAIN 19..210 FT /note="Albumin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 211..402 FT /note="Albumin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 403..601 FT /note="Albumin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT BINDING 22 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:80265" FT MOD_RES 111 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 115 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 117 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 344 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 444 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 445 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT CARBOHYD 251 FT /note="N-linked (GlcNAc...) asparagine" FT /id="CAR_000070" FT DISULFID 99..114 FT DISULFID 113..124 FT DISULFID 148..193 FT DISULFID 192..201 FT DISULFID 224..270 FT DISULFID 269..277 FT DISULFID 289..303 FT DISULFID 302..313 FT DISULFID 384..393 FT DISULFID 416..462 FT DISULFID 461..472 FT DISULFID 485..501 FT DISULFID 500..511 FT DISULFID 538..583 FT DISULFID 582..591 FT VARIANT 187 FT /note="K -> Q (in dbSNP:rs35765619)" FT /id="VAR_033928" FT VARIANT 570 FT /note="A -> G (in dbSNP:rs7790)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_012049" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 43..54 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 60..74 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 102..107 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 118..127 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 155..167 FT /evidence="ECO:0007829|PDB:7YIM" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 175..192 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 198..230 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 232..246 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 252..270 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 274..289 FT /evidence="ECO:0007829|PDB:7YIM" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:7YIM" FT TURN 299..301 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 307..316 FT /evidence="ECO:0007829|PDB:7YIM" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:7YIM" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 344..360 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 367..384 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:7YIM" FT TURN 399..402 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 403..438 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 444..461 FT /evidence="ECO:0007829|PDB:7YIM" FT STRAND 462..464 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 468..490 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 495..502 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:7YIM" FT TURN 535..539 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 543..559 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 566..581 FT /evidence="ECO:0007829|PDB:7YIM" FT STRAND 582..587 FT /evidence="ECO:0007829|PDB:7YIM" FT HELIX 588..607 FT /evidence="ECO:0007829|PDB:7YIM" SQ SEQUENCE 609 AA; 68678 MW; 4D4E45820E1C2D4F CRC64; MKWVESIFLI FLLNFTESRT LHRNEYGIAS ILDSYQCTAE ISLADLATIF FAQFVQEATY KEVSKMVKDA LTAIEKPTGD EQSSGCLENQ LPAFLEELCH EKEILEKYGH SDCCSQSEEG RHNCFLAHKK PTPASIPLFQ VPEPVTSCEA YEEDRETFMN KFIYEIARRH PFLYAPTILL WAARYDKIIP SCCKAENAVE CFQTKAATVT KELRESSLLN QHACAVMKNF GTRTFQAITV TKLSQKFTKV NFTEIQKLVL DVAHVHEHCC RGDVLDCLQD GEKIMSYICS QQDTLSNKIT ECCKLTTLER GQCIIHAEND EKPEGLSPNL NRFLGDRDFN QFSSGEKNIF LASFVHEYSR RHPQLAVSVI LRVAKGYQEL LEKCFQTENP LECQDKGEEE LQKYIQESQA LAKRSCGLFQ KLGEYYLQNA FLVAYTKKAP QLTSSELMAI TRKMAATAAT CCQLSEDKLL ACGEGAADII IGHLCIRHEM TPVNPGVGQC CTSSYANRRP CFSSLVVDET YVPPAFSDDK FIFHKDLCQA QGVALQTMKQ EFLINLVKQK PQITEEQLEA VIADFSGLLE KCCQGQEQEV CFAEEGQKLI SKTRAALGV //