ID RNT2_HUMAN Reviewed; 256 AA. AC O00584; B2RDA7; E1P5C3; Q5T8Q0; Q8TCU2; Q9BZ46; Q9BZ47; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 2. DT 13-FEB-2019, entry version 161. DE RecName: Full=Ribonuclease T2; DE EC=3.1.27.-; DE AltName: Full=Ribonuclease 6; DE Flags: Precursor; GN Name=RNASET2; Synonyms=RNASE6PL; 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] (ISOFORM 1). RX PubMed=9192857; DOI=10.1006/geno.1997.4679; RA Trubia M., Sessa L., Taramelli R.; RT "Mammalian Rh/T2/S-glycoprotein ribonuclease family genes: cloning of RT a human member located in a region of chromosome 6 (6q27) frequently RT deleted in human malignancies."; RL Genomics 42:342-344(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11821951; DOI=10.1038/sj.onc.1205067; RA Liu Y., Emilion G., Mungall A.J., Dunham I., Beck S., RA LeMeuth-Metzinger V., Shelling A.N., Charnock F.M., Ganesan T.S.; RT "Physical and transcript map of the region between D6S264 and D6S149 RT on chromosome 6q27, the minimal region of allele loss in sporadic RT epithelial ovarian cancer."; RL Oncogene 21:387-399(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, Pancreas, and Spleen; 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 SUBCELLULAR LOCATION. RX PubMed=15809705; RA Acquati F., Possati L., Ferrante L., Campomenosi P., Talevi S., RA Bardelli S., Margiotta C., Russo A., Bortoletto E., Rocchetti R., RA Calza R., Cinquetti R., Monti L., Salis S., Barbanti-Brodano G., RA Taramelli R.; RT "Tumor and metastasis suppression by the human RNASET2 gene."; RL Int. J. Oncol. 26:1159-1168(2005). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16620762; DOI=10.1016/j.abb.2006.02.022; RA Campomenosi P., Salis S., Lindqvist C., Mariani D., Nordstrom T., RA Acquati F., Taramelli R.; RT "Characterization of RNASET2, the first human member of the Rh/T2/S RT family of glycoproteins."; RL Arch. Biochem. Biophys. 449:17-26(2006). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT LCWM RP ARG-184, AND CHARACTERIZATION OF VARIANT LCWM ARG-184. RX PubMed=19525954; DOI=10.1038/ng.398; RA Henneke M., Diekmann S., Ohlenbusch A., Kaiser J., Engelbrecht V., RA Kohlschutter A., Kratzner R., Madruga-Garrido M., Mayer M., Opitz L., RA Rodriguez D., Ruschendorf F., Schumacher J., Thiele H., Thoms S., RA Steinfeld R., Nurnberg P., Gartner J.; RT "RNASET2-deficient cystic leukoencephalopathy resembles congenital RT cytomegalovirus brain infection."; RL Nat. Genet. 41:773-775(2009). RN [10] 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., RA Buerckstuemmer T., 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 [11] RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT LCWM ARG-184. RX PubMed=21199949; DOI=10.1073/pnas.1009811107; RA Haud N., Kara F., Diekmann S., Henneke M., Willer J.R., Hillwig M.S., RA Gregg R.G., Macintosh G.C., Gartner J., Alia A., Hurlstone A.F.; RT "rnaset2 mutant zebrafish model familial cystic leukoencephalopathy RT and reveal a role for RNase T2 in degrading ribosomal RNA."; RL Proc. Natl. Acad. Sci. U.S.A. 108:1099-1103(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 25-256, GLYCOSYLATION AT RP ASN-76; ASN-106 AND ASN-212, FUNCTION, ACTIVITY REGULATION, DISULFIDE RP BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22735700; DOI=10.1093/nar/gks614; RA Thorn A., Steinfeld R., Ziegenbein M., Grapp M., Hsiao H.H., RA Urlaub H., Sheldrick G.M., Gartner J., Kratzner R.; RT "Structure and activity of the only human RNase T2."; RL Nucleic Acids Res. 40:8733-8742(2012). CC -!- FUNCTION: Has ribonuclease activity, with higher activity at CC acidic pH. Probably is involved in lysosomal degradation of CC ribosomal RNA (By similarity). Probably plays a role in cellular CC RNA catabolism. {ECO:0000250, ECO:0000269|PubMed:16620762, CC ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:22735700}. CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+). CC {ECO:0000269|PubMed:22735700}. CC -!- SUBCELLULAR LOCATION: Secreted. Lysosome lumen. Endoplasmic CC reticulum lumen. Note=Subcellular fractionation of transfected CC ovarian cancer cells reveals full-length RNASET2 in the CC endoplasmic reticulum fraction and the 2 smaller RNASET2 CC proteolytic products in the lysosome fraction. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00584-1; Sequence=Displayed; CC Name=2; CC IsoId=O00584-2; Sequence=VSP_008405, VSP_008406; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression levels observed CC in the temporal lobe and fetal brain. CC {ECO:0000269|PubMed:19525954}. CC -!- DISEASE: Leukoencephalopathy, cystic, without megalencephaly CC (LCWM) [MIM:612951]: An infantile-onset syndrome of cerebral CC leukoencephalopathy. Affected newborns develop microcephaly and CC neurologic abnormalities including psychomotor impairment, CC seizures and sensorineural hearing impairment. The brain shows CC multifocal white matter lesions, anterior temporal lobe CC subcortical cysts, pericystic abnormal myelination, CC ventriculomegaly and intracranial calcifications. CC {ECO:0000269|PubMed:19525954, ECO:0000269|PubMed:21199949}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/RNASET2ID518ch6q27.html"; 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; U85625; AAC51363.2; -; mRNA. DR EMBL; AJ419865; CAD12030.1; -; mRNA. DR EMBL; AJ419866; CAD12031.1; -; mRNA. DR EMBL; AK315467; BAG37854.1; -; mRNA. DR EMBL; AL133458; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL159163; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47512.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47513.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47514.1; -; Genomic_DNA. DR EMBL; BC001660; AAH01660.1; -; mRNA. DR EMBL; BC001819; AAH01819.1; -; mRNA. DR EMBL; BC039713; AAH39713.1; -; mRNA. DR EMBL; BC051912; AAH51912.1; -; mRNA. DR CCDS; CCDS5295.1; -. [O00584-1] DR PIR; S78046; S78046. DR RefSeq; NP_003721.2; NM_003730.4. [O00584-1] DR UniGene; Hs.529989; -. DR PDB; 3T0O; X-ray; 1.59 A; A=25-256. DR PDBsum; 3T0O; -. DR ProteinModelPortal; O00584; -. DR SMR; O00584; -. DR BioGrid; 114188; 12. DR IntAct; O00584; 5. DR STRING; 9606.ENSP00000422846; -. DR GlyConnect; 1719; -. DR iPTMnet; O00584; -. DR PhosphoSitePlus; O00584; -. DR SwissPalm; O00584; -. DR BioMuta; RNASET2; -. DR EPD; O00584; -. DR jPOST; O00584; -. DR MaxQB; O00584; -. DR PaxDb; O00584; -. DR PeptideAtlas; O00584; -. DR PRIDE; O00584; -. DR ProteomicsDB; 47985; -. DR ProteomicsDB; 47986; -. [O00584-2] DR Ensembl; ENST00000421787; ENSP00000390833; ENSG00000026297. [O00584-2] DR Ensembl; ENST00000476238; ENSP00000422846; ENSG00000026297. [O00584-1] DR Ensembl; ENST00000508775; ENSP00000426455; ENSG00000026297. [O00584-1] DR GeneID; 8635; -. DR KEGG; hsa:8635; -. DR UCSC; uc003qve.4; human. [O00584-1] DR CTD; 8635; -. DR DisGeNET; 8635; -. DR EuPathDB; HostDB:ENSG00000026297.15; -. DR GeneCards; RNASET2; -. DR HGNC; HGNC:21686; RNASET2. DR HPA; HPA029013; -. DR HPA; HPA066509; -. DR MalaCards; RNASET2; -. DR MIM; 612944; gene. DR MIM; 612951; phenotype. DR neXtProt; NX_O00584; -. DR OpenTargets; ENSG00000026297; -. DR Orphanet; 85136; Cystic leukoencephalopathy without megalencephaly. DR PharmGKB; PA128394541; -. DR eggNOG; KOG1642; Eukaryota. DR eggNOG; ENOG4111M7G; LUCA. DR GeneTree; ENSGT00640000091563; -. DR HOVERGEN; HBG050037; -. DR InParanoid; O00584; -. DR KO; K01166; -. DR OrthoDB; 994722at2759; -. DR PhylomeDB; O00584; -. DR TreeFam; TF315063; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; RNASET2; human. DR GeneWiki; RNASET2; -. DR GenomeRNAi; 8635; -. DR PRO; PR:O00584; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000026297; Expressed in 232 organ(s), highest expression level in endometrium. DR ExpressionAtlas; O00584; baseline and differential. DR Genevisible; O00584; HS. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central. DR GO; GO:0004540; F:ribonuclease activity; IDA:UniProtKB. DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB. DR CDD; cd01061; RNase_T2_euk; 1. DR Gene3D; 3.90.730.10; -; 1. DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic. DR InterPro; IPR001568; RNase_T2-like. DR InterPro; IPR036430; RNase_T2-like_sf. DR InterPro; IPR018188; RNase_T2_His_AS_1. DR InterPro; IPR033130; RNase_T2_His_AS_2. DR PANTHER; PTHR11240; PTHR11240; 1. DR Pfam; PF00445; Ribonuclease_T2; 1. DR SUPFAM; SSF55895; SSF55895; 1. DR PROSITE; PS00530; RNASE_T2_1; 1. DR PROSITE; PS00531; RNASE_T2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Disease mutation; Disulfide bond; Endonuclease; Endoplasmic reticulum; KW Glycoprotein; Hydrolase; Lysosome; Nuclease; Polymorphism; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 256 Ribonuclease T2. FT /FTId=PRO_0000030987. FT ACT_SITE 65 65 {ECO:0000250}. FT ACT_SITE 114 114 {ECO:0000250}. FT ACT_SITE 118 118 {ECO:0000250}. FT CARBOHYD 76 76 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22735700}. FT CARBOHYD 106 106 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22735700}. FT CARBOHYD 212 212 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:22735700}. FT DISULFID 48 55 {ECO:0000269|PubMed:22735700}. FT DISULFID 75 121 {ECO:0000269|PubMed:22735700}. FT DISULFID 184 241 {ECO:0000269|PubMed:22735700}. FT DISULFID 202 213 {ECO:0000269|PubMed:22735700}. FT VAR_SEQ 88 121 DLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTC -> KNW FT MEITDSSLPSPSTLPIINIFYSVLHLLQLMN (in FT isoform 2). FT {ECO:0000303|PubMed:11821951}. FT /FTId=VSP_008405. FT VAR_SEQ 122 256 Missing (in isoform 2). FT {ECO:0000303|PubMed:11821951}. FT /FTId=VSP_008406. FT VARIANT 184 184 C -> R (in LCWM; the loss of a disulfide FT bond may affect protein folding and FT stability; the protein is retained in the FT endoplasmic reticulum; FT dbSNP:rs121918137). FT {ECO:0000269|PubMed:19525954, FT ECO:0000269|PubMed:21199949}. FT /FTId=VAR_063596. FT VARIANT 236 236 R -> W (in dbSNP:rs11159). FT /FTId=VAR_013004. FT STRAND 36 42 {ECO:0000244|PDB:3T0O}. FT HELIX 44 47 {ECO:0000244|PDB:3T0O}. FT STRAND 50 52 {ECO:0000244|PDB:3T0O}. FT HELIX 53 55 {ECO:0000244|PDB:3T0O}. FT STRAND 63 71 {ECO:0000244|PDB:3T0O}. FT HELIX 83 89 {ECO:0000244|PDB:3T0O}. FT HELIX 90 96 {ECO:0000244|PDB:3T0O}. FT HELIX 108 117 {ECO:0000244|PDB:3T0O}. FT HELIX 119 122 {ECO:0000244|PDB:3T0O}. FT HELIX 126 128 {ECO:0000244|PDB:3T0O}. FT HELIX 131 145 {ECO:0000244|PDB:3T0O}. FT HELIX 147 153 {ECO:0000244|PDB:3T0O}. FT HELIX 165 176 {ECO:0000244|PDB:3T0O}. FT STRAND 181 185 {ECO:0000244|PDB:3T0O}. FT STRAND 195 204 {ECO:0000244|PDB:3T0O}. FT TURN 205 207 {ECO:0000244|PDB:3T0O}. FT STRAND 243 247 {ECO:0000244|PDB:3T0O}. SQ SEQUENCE 256 AA; 29481 MW; 7C8BB08B8ED853EB CRC64; MRPAALRGAL LGCLCLALLC LGGADKRLRD NHEWKKLIMV QHWPETVCEK IQNDCRDPPD YWTIHGLWPD KSEGCNRSWP FNLEEIKDLL PEMRAYWPDV IHSFPNRSRF WKHEWEKHGT CAAQVDALNS QKKYFGRSLE LYRELDLNSV LLKLGIKPSI NYYQVADFKD ALARVYGVIP KIQCLPPSQD EEVQTIGQIE LCLTKQDQQL QNCTEPGEQP SPKQEVWLAN GAAESRGLRV CEDGPVFYPP PKKTKH //