ID VNN1_HUMAN Reviewed; 513 AA. AC O95497; A8K310; Q4JFW6; Q4VAS7; Q4VAS8; Q4VAS9; Q9UF16; Q9UJF4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 13-FEB-2019, entry version 163. DE RecName: Full=Pantetheinase; DE EC=3.5.1.92 {ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849}; DE AltName: Full=Pantetheine hydrolase; DE AltName: Full=Tiff66; DE AltName: Full=Vascular non-inflammatory molecule 1; DE Short=Vanin-1; DE Flags: Precursor; GN Name=VNN1; 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], AND VARIANT ILE-26. RC TISSUE=Liver; RX PubMed=9790769; DOI=10.1006/geno.1998.5481; RA Galland F., Malergue F., Bazin H., Mattei M.-G., Aurrand-Lions M., RA Theillet C., Naquet P.; RT "Two human genes related to murine vanin-1 are located on the long arm RT of human chromosome 6."; RL Genomics 53:203-213(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-26. RA Prehn S., Friedrichson T., Henske A., Boehm S., Hartmann E., RA Kurzchalia T.V.; RT "Human Tiff66."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-26. RC TISSUE=Umbilical cord blood; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [GENOMIC DNA], AND VARIANTS ILE-26; THR-63; RP SER-131; LEU-136; ASN-146; ASP-296; GLU-325; ALA-336 AND THR-373. RG NIEHS SNPs program; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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], AND VARIANT SER-131. 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 [7] RP IDENTIFICATION. RX PubMed=10567687; DOI=10.1016/S0014-5793(99)01439-8; RA Maras B., Barra D., Dupre S., Pitari G.; RT "Is pantetheinase the actual identity of mouse and human vanin-1 RT proteins?"; RL FEBS Lett. 461:149-152(1999). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=11491533; DOI=10.1007/s002510100327; RA Martin F., Malergue F., Pitari G., Philippe J.M., Philips S., RA Chabret C., Granjeaud S., Mattei M.G., Mungall A.J., Naquet P., RA Galland F.; RT "Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode RT isoforms of pantetheinase ectoenzymes."; RL Immunogenetics 53:296-306(2001). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38 AND ASN-353. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-283; ASN-315 AND RP ASN-353. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [11] RP TISSUE SPECIFICITY, AND INDUCTION BY CYTOKINES. RX PubMed=19322213; DOI=10.1038/jid.2009.67; RA Jansen P.A.M., Kamsteeg M., Rodijk-Olthuis D., RA van Vlijmen-Willems I.M.J.J., de Jongh G.J., Bergers M., RA Tjabringa G.S., Zeeuwen P.L.J.M., Schalkwijk J.; RT "Expression of the vanin gene family in normal and inflamed human RT skin: induction by proinflammatory cytokines."; RL J. Invest. Dermatol. 129:2167-2174(2009). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-353. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 22-513 IN COMPLEX WITH RP SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT RP ASN-38; ASN-130; ASN-200; ASN-315 AND ASN-353, ACTIVE SITE, SUBUNIT, RP AND MUTAGENESIS OF GLU-79 AND LYS-178. RX PubMed=25478849; DOI=10.1107/S1399004714022767; RA Boersma Y.L., Newman J., Adams T.E., Cowieson N., Krippner G., RA Bozaoglu K., Peat T.S.; RT "The structure of vanin 1: a key enzyme linking metabolic disease and RT inflammation."; RL Acta Crystallogr. D 70:3320-3329(2014). CC -!- FUNCTION: Amidohydrolase that hydrolyzes specifically one of the CC carboamide linkages in D-pantetheine thus recycling pantothenic CC acid (vitamin B5) and releasing cysteamine. CC {ECO:0000269|PubMed:10567687, ECO:0000269|PubMed:11491533, CC ECO:0000269|PubMed:25478849}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine; CC Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753, CC ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92; CC Evidence={ECO:0000269|PubMed:11491533, CC ECO:0000269|PubMed:25478849}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25478849}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11491533}; CC Lipid-anchor, GPI-anchor {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in CC spleen, kidney and blood. Overexpressed in lesional psoriatic CC skin. {ECO:0000269|PubMed:19322213}. CC -!- INDUCTION: By Th17/Th1 type cytokines, but not by Th2-type. CC {ECO:0000269|PubMed:19322213}. CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. CC BTD/VNN family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/vnn1/"; 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; AJ132099; CAA10568.1; -; mRNA. DR EMBL; U39664; AAF21453.1; -; mRNA. DR EMBL; AK290425; BAF83114.1; -; mRNA. DR EMBL; DQ100297; AAY88742.1; -; Genomic_DNA. DR EMBL; AL032821; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC096265; AAH96265.1; -; mRNA. DR EMBL; BC096266; AAH96266.1; -; mRNA. DR EMBL; BC096267; AAH96267.1; -; mRNA. DR EMBL; BC096268; AAH96268.1; -; mRNA. DR CCDS; CCDS5159.1; -. DR RefSeq; NP_004657.2; NM_004666.2. DR UniGene; Hs.12114; -. DR UniGene; Hs.720659; -. DR PDB; 4CYF; X-ray; 2.25 A; A/B=22-513. DR PDB; 4CYG; X-ray; 2.30 A; A/B=22-513. DR PDB; 4CYY; X-ray; 2.89 A; A=27-513. DR PDBsum; 4CYF; -. DR PDBsum; 4CYG; -. DR PDBsum; 4CYY; -. DR ProteinModelPortal; O95497; -. DR SMR; O95497; -. DR BioGrid; 114395; 9. DR STRING; 9606.ENSP00000356905; -. DR GlyConnect; 1966; -. DR iPTMnet; O95497; -. DR PhosphoSitePlus; O95497; -. DR BioMuta; VNN1; -. DR jPOST; O95497; -. DR PaxDb; O95497; -. DR PeptideAtlas; O95497; -. DR PRIDE; O95497; -. DR ProteomicsDB; 50924; -. DR Ensembl; ENST00000367928; ENSP00000356905; ENSG00000112299. DR GeneID; 8876; -. DR KEGG; hsa:8876; -. DR UCSC; uc003qdo.4; human. DR CTD; 8876; -. DR DisGeNET; 8876; -. DR EuPathDB; HostDB:ENSG00000112299.7; -. DR GeneCards; VNN1; -. DR H-InvDB; HIX0022602; -. DR HGNC; HGNC:12705; VNN1. DR HPA; HPA064145; -. DR MIM; 603570; gene. DR neXtProt; NX_O95497; -. DR OpenTargets; ENSG00000112299; -. DR PharmGKB; PA37321; -. DR eggNOG; KOG0806; Eukaryota. DR eggNOG; COG0388; LUCA. DR GeneTree; ENSGT00390000013823; -. DR HOVERGEN; HBG003996; -. DR InParanoid; O95497; -. DR KO; K08069; -. DR OMA; KDWASNA; -. DR OrthoDB; 1276751at2759; -. DR PhylomeDB; O95497; -. DR TreeFam; TF323645; -. DR BRENDA; 3.5.1.92; 2681. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR GeneWiki; VNN1; -. DR GenomeRNAi; 8876; -. DR PRO; PR:O95497; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000112299; Expressed in 124 organ(s), highest expression level in jejunal mucosa. DR Genevisible; O95497; HS. DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; TAS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0017159; F:pantetheine hydrolase activity; IDA:UniProtKB. DR GO; GO:0002526; P:acute inflammatory response; ISS:BHF-UCL. DR GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL. DR GO; GO:0002544; P:chronic inflammatory response; ISS:BHF-UCL. DR GO; GO:0006954; P:inflammatory response; ISS:BHF-UCL. DR GO; GO:0045087; P:innate immune response; ISS:BHF-UCL. DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:BHF-UCL. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0015939; P:pantothenate metabolic process; IDA:UniProtKB. DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:BHF-UCL. DR GO; GO:0006979; P:response to oxidative stress; TAS:BHF-UCL. DR CDD; cd07567; biotinidase_like; 1. DR Gene3D; 3.60.110.10; -; 1. DR InterPro; IPR012101; Biotinidase-like_euk. DR InterPro; IPR040154; Biotinidase/VNN. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR PANTHER; PTHR10609; PTHR10609; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR PIRSF; PIRSF011861; Biotinidase; 1. DR SUPFAM; SSF56317; SSF56317; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Glycoprotein; KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Polymorphism; KW Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 491 Pantetheinase. FT /FTId=PRO_0000019712. FT PROPEP 492 513 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000019713. FT DOMAIN 39 306 CN hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT ACT_SITE 79 79 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00054, FT ECO:0000305|PubMed:25478849}. FT ACT_SITE 178 178 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU00054, FT ECO:0000305|PubMed:25478849}. FT ACT_SITE 211 211 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU00054, FT ECO:0000269|PubMed:25478849}. FT LIPID 491 491 GPI-anchor amidated glycine. FT {ECO:0000255}. FT CARBOHYD 38 38 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:4CYF, FT ECO:0000244|PDB:4CYG, FT ECO:0000244|PDB:4CYY, FT ECO:0000269|PubMed:15084671}. FT CARBOHYD 130 130 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:4CYF, FT ECO:0000244|PDB:4CYG, FT ECO:0000244|PDB:4CYY, FT ECO:0000269|PubMed:16335952}. FT CARBOHYD 200 200 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:4CYY, ECO:0000255}. FT CARBOHYD 283 283 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 315 315 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:4CYF, FT ECO:0000244|PDB:4CYG, FT ECO:0000244|PDB:4CYY, FT ECO:0000269|PubMed:16335952}. FT CARBOHYD 353 353 N-linked (GlcNAc...) asparagine. FT {ECO:0000244|PDB:4CYF, FT ECO:0000244|PDB:4CYG, FT ECO:0000244|PDB:4CYY, FT ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT VARIANT 26 26 T -> I (in dbSNP:rs2294757). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9790769, FT ECO:0000269|Ref.2, ECO:0000269|Ref.4}. FT /FTId=VAR_023529. FT VARIANT 63 63 A -> T. {ECO:0000269|Ref.4}. FT /FTId=VAR_023967. FT VARIANT 131 131 N -> S (in dbSNP:rs2272996). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|Ref.4}. FT /FTId=VAR_023968. FT VARIANT 136 136 V -> L (in dbSNP:rs45610032). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023969. FT VARIANT 146 146 D -> N (in dbSNP:rs45624336). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023970. FT VARIANT 296 296 E -> D (in dbSNP:rs45523444). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023971. FT VARIANT 325 325 A -> E (in dbSNP:rs34535050). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023972. FT VARIANT 336 336 T -> A (in dbSNP:rs45562238). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023973. FT VARIANT 373 373 I -> T (in dbSNP:rs35938565). FT {ECO:0000269|Ref.4}. FT /FTId=VAR_023974. FT MUTAGEN 79 79 E->A: Abolishes enzyme activity. FT {ECO:0000269|PubMed:25478849}. FT MUTAGEN 178 178 K->A: Abolishes enzyme activity. FT {ECO:0000269|PubMed:25478849}. FT CONFLICT 101 101 D -> N (in Ref. 6; AAH96268). FT {ECO:0000305}. FT CONFLICT 113 113 N -> I (in Ref. 4; AAY88742). FT {ECO:0000305}. FT CONFLICT 423 423 E -> D (in Ref. 2; AAF21453). FT {ECO:0000305}. FT STRAND 24 32 {ECO:0000244|PDB:4CYF}. FT HELIX 46 68 {ECO:0000244|PDB:4CYF}. FT TURN 69 71 {ECO:0000244|PDB:4CYF}. FT STRAND 73 76 {ECO:0000244|PDB:4CYF}. FT TURN 79 83 {ECO:0000244|PDB:4CYF}. FT HELIX 89 92 {ECO:0000244|PDB:4CYF}. FT HELIX 93 95 {ECO:0000244|PDB:4CYF}. FT HELIX 102 104 {ECO:0000244|PDB:4CYF}. FT TURN 108 110 {ECO:0000244|PDB:4CYF}. FT TURN 112 115 {ECO:0000244|PDB:4CYF}. FT HELIX 119 130 {ECO:0000244|PDB:4CYF}. FT STRAND 134 144 {ECO:0000244|PDB:4CYF}. FT STRAND 156 166 {ECO:0000244|PDB:4CYF}. FT STRAND 172 177 {ECO:0000244|PDB:4CYF}. FT STRAND 198 201 {ECO:0000244|PDB:4CYF}. FT STRAND 204 208 {ECO:0000244|PDB:4CYF}. FT HELIX 211 215 {ECO:0000244|PDB:4CYF}. FT TURN 217 219 {ECO:0000244|PDB:4CYY}. FT HELIX 220 225 {ECO:0000244|PDB:4CYF}. FT STRAND 230 236 {ECO:0000244|PDB:4CYF}. FT TURN 242 244 {ECO:0000244|PDB:4CYF}. FT HELIX 247 258 {ECO:0000244|PDB:4CYF}. FT STRAND 261 267 {ECO:0000244|PDB:4CYF}. FT HELIX 270 272 {ECO:0000244|PDB:4CYF}. FT STRAND 277 280 {ECO:0000244|PDB:4CYF}. FT STRAND 282 289 {ECO:0000244|PDB:4CYF}. FT STRAND 298 307 {ECO:0000244|PDB:4CYF}. FT HELIX 318 321 {ECO:0000244|PDB:4CYF}. FT STRAND 332 337 {ECO:0000244|PDB:4CYF}. FT STRAND 340 346 {ECO:0000244|PDB:4CYF}. FT STRAND 349 358 {ECO:0000244|PDB:4CYF}. FT STRAND 361 371 {ECO:0000244|PDB:4CYF}. FT STRAND 378 387 {ECO:0000244|PDB:4CYF}. FT STRAND 393 402 {ECO:0000244|PDB:4CYF}. FT STRAND 404 407 {ECO:0000244|PDB:4CYF}. FT HELIX 408 410 {ECO:0000244|PDB:4CYF}. FT STRAND 422 429 {ECO:0000244|PDB:4CYF}. FT STRAND 436 442 {ECO:0000244|PDB:4CYF}. FT HELIX 443 445 {ECO:0000244|PDB:4CYF}. FT STRAND 451 454 {ECO:0000244|PDB:4CYF}. FT STRAND 460 465 {ECO:0000244|PDB:4CYF}. FT STRAND 470 478 {ECO:0000244|PDB:4CYF}. FT HELIX 480 482 {ECO:0000244|PDB:4CYF}. SQ SEQUENCE 513 AA; 57012 MW; 018D2417C12E403F CRC64; MTTQLPAYVA ILLFYVSRAS CQDTFTAAVY EHAAILPNAT LTPVSREEAL ALMNRNLDIL EGAITSAADQ GAHIIVTPED AIYGWNFNRD SLYPYLEDIP DPEVNWIPCN NRNRFGQTPV QERLSCLAKN NSIYVVANIG DKKPCDTSDP QCPPDGRYQY NTDVVFDSQG KLVARYHKQN LFMGENQFNV PKEPEIVTFN TTFGSFGIFT CFDILFHDPA VTLVKDFHVD TIVFPTAWMN VLPHLSAVEF HSAWAMGMRV NFLASNIHYP SKKMTGSGIY APNSSRAFHY DMKTEEGKLL LSQLDSHPSH SAVVNWTSYA SSIEALSSGN KEFKGTVFFD EFTFVKLTGV AGNYTVCQKD LCCHLSYKMS ENIPNEVYAL GAFDGLHTVE GRYYLQICTL LKCKTTNLNT CGDSAETAST RFEMFSLSGT FGTQYVFPEV LLSENQLAPG EFQVSTDGRL FSLKPTSGPV LTVTLFGRLY EKDWASNASS GLTAQARIIM LIVIAPIVCS LSW //