ID HNMT_HUMAN Reviewed; 292 AA. AC P50135; B2R9J3; Q546Z6; Q7Z7I2; Q8IU56; Q8WW98; Q9BRW6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 147. DE RecName: Full=Histamine N-methyltransferase; DE Short=HMT; DE EC=2.1.1.8; GN Name=HNMT; 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). RC TISSUE=Kidney; RX PubMed=7943261; RA Yamauchi K., Sekizawa K., Suzuki H., Nakazawa H., Ohkawara Y., RA Katayose D., Ohtsu H., Tamura G., Shibahara S., Takemura M.; RT "Structure and function of human histamine N-methyltransferase: RT critical enzyme in histamine metabolism in airway."; RL Am. J. Physiol. 267:L342-L349(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=8145732; RA Girard B., Otterness D.M., Wood T.C., Honchel R., Wieben E.D., RA Weinshilboum R.M.; RT "Human histamine N-methyltransferase pharmacogenetics: cloning and RT expression of kidney cDNA."; RL Mol. Pharmacol. 45:461-468(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8605025; DOI=10.1006/bbrc.1996.0271; RA Aksoy S., Raftogianis R., Weinshilboum R.M.; RT "Human histamine N-methyltransferase gene: structural characterization RT and chromosomal location."; RL Biochem. Biophys. Res. Commun. 219:548-554(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Barnes W.G., Grinde E., Crawford D.R., Herrick-Davis K., Hough L.B.; RT "Further characterization of the histamine N-methyltransferase gene: a RT new mRNA species and several 3'-UTR Variants from human brain."; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=14667820; DOI=10.1016/S0888-7543(03)00236-2; RA Barnes W.G., Grinde E., Crawford D.R., Herrick-Davis K., Hough L.B.; RT "Characterization of a new mRNA species from the human histamine N- RT methyltransferase gene."; RL Genomics 83:168-171(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Liver, and Prostate; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-221. RA Thomae B., Wieben E., Eckloff B., Weinshilboum R.M.; RT "Homo sapiens histamine N-methyltransferase (HNMT) gene, consensus of RT Coriell PDR 90."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [11] 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND RP INHIBITOR. RX PubMed=11566133; DOI=10.1016/S0969-2126(01)00643-8; RA Horton J.R., Sawada K., Nishibori M., Zhang X., Cheng X.; RT "Two polymorphic forms of human histamine methyltransferase: RT structural, thermal, and kinetic comparisons."; RL Structure 9:837-849(2001). RN [14] RP VARIANT ILE-105. RX PubMed=9547362; RA Preuss C.V., Wood T.C., Szumlanski C.L., Raftogianis R.B., RA Otterness D.M., Girard B., Scott M.C., Weinshilboum R.M.; RT "Human histamine N-methyltransferase pharmacogenetics: common genetic RT polymorphisms that alter activity."; RL Mol. Pharmacol. 53:708-717(1998). RN [15] RP VARIANT ILE-105. RX PubMed=10803682; DOI=10.1097/00008571-200004000-00007; RA Yan L., Galinsky R.E., Bernstein J.A., Liggett S.B., RA Weinshilboum R.M.; RT "Histamine N-methyltransferase pharmacogenetics: association of a RT common functional polymorphism with asthma."; RL Pharmacogenetics 10:261-266(2000). CC -!- FUNCTION: Inactivates histamine by N-methylation. Plays an CC important role in degrading histamine and in regulating the airway CC response to histamine. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histamine = S- CC adenosyl-L-homocysteine + N(tau)-methylhistamine. CC {ECO:0000255|PROSITE-ProRule:PRU00929}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11566133}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P50135-1; Sequence=Displayed; CC Name=2; Synonyms=HNMT-S; CC IsoId=P50135-2; Sequence=VSP_042027; CC Note=Has no histamine-methylating activity.; CC Name=3; CC IsoId=P50135-3; Sequence=VSP_043482, VSP_043483; CC Note=No experimental confirmation available.; CC -!- POLYMORPHISM: Variant Ile-105 has a reduced activity and seems to CC be linked with a predisposition to asthma. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. HNMT family. {ECO:0000255|PROSITE- CC ProRule:PRU00929}. 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; D16224; BAA03752.1; -; mRNA. DR EMBL; U08092; AAA17423.1; -; mRNA. DR EMBL; U44111; AAB18137.1; -; Genomic_DNA. DR EMBL; U44106; AAB18137.1; JOINED; Genomic_DNA. DR EMBL; U44107; AAB18137.1; JOINED; Genomic_DNA. DR EMBL; U44108; AAB18137.1; JOINED; Genomic_DNA. DR EMBL; U44109; AAB18137.1; JOINED; Genomic_DNA. DR EMBL; U44110; AAB18137.1; JOINED; Genomic_DNA. DR EMBL; AF523358; AAN33016.1; -; mRNA. DR EMBL; AF523359; AAN33017.1; -; mRNA. DR EMBL; AF523360; AAN33018.1; -; mRNA. DR EMBL; AF523356; AAN33014.1; -; mRNA. DR EMBL; AF523357; AAN33015.1; -; mRNA. DR EMBL; AK313804; BAG36540.1; -; mRNA. DR EMBL; AC093674; AAY24212.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11612.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11613.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11614.1; -; Genomic_DNA. DR EMBL; BC005907; AAH05907.1; -; mRNA. DR EMBL; BC020677; AAH20677.1; -; mRNA. DR EMBL; AH012839; AAP42155.1; -; Genomic_DNA. DR CCDS; CCDS2181.1; -. [P50135-1] DR CCDS; CCDS33296.1; -. [P50135-2] DR CCDS; CCDS33297.1; -. [P50135-3] DR PIR; G01409; G01409. DR RefSeq; NP_001019245.1; NM_001024074.2. [P50135-3] DR RefSeq; NP_001019246.1; NM_001024075.1. [P50135-2] DR RefSeq; NP_008826.1; NM_006895.2. [P50135-1] DR UniGene; Hs.42151; -. DR PDB; 1ICZ; Model; -; A=1-249. DR PDB; 1JQD; X-ray; 2.28 A; A/B=1-292. DR PDB; 1JQE; X-ray; 1.91 A; A/B=1-292. DR PDB; 2AOT; X-ray; 1.90 A; A/B=1-292. DR PDB; 2AOU; X-ray; 2.30 A; A/B=1-292. DR PDB; 2AOV; X-ray; 2.48 A; A/B=1-292. DR PDB; 2AOW; X-ray; 2.97 A; A/B=1-292. DR PDB; 2AOX; X-ray; 3.12 A; A/B=1-292. DR PDBsum; 1ICZ; -. DR PDBsum; 1JQD; -. DR PDBsum; 1JQE; -. DR PDBsum; 2AOT; -. DR PDBsum; 2AOU; -. DR PDBsum; 2AOV; -. DR PDBsum; 2AOW; -. DR PDBsum; 2AOX; -. DR ProteinModelPortal; P50135; -. DR SMR; P50135; 5-292. DR BioGrid; 109418; 5. DR IntAct; P50135; 1. DR MINT; MINT-5001055; -. DR STRING; 9606.ENSP00000280097; -. DR BindingDB; P50135; -. DR ChEMBL; CHEMBL2190; -. DR DrugBank; DB00613; Amodiaquine. DR DrugBank; DB00878; Chlorhexidine. DR DrugBank; DB00667; Histamine Phosphate. DR DrugBank; DB01103; Quinacrine. DR PhosphoSite; P50135; -. DR BioMuta; HNMT; -. DR DMDM; 1708272; -. DR MaxQB; P50135; -. DR PaxDb; P50135; -. DR PeptideAtlas; P50135; -. DR PRIDE; P50135; -. DR DNASU; 3176; -. DR Ensembl; ENST00000280096; ENSP00000280096; ENSG00000150540. [P50135-3] DR Ensembl; ENST00000280097; ENSP00000280097; ENSG00000150540. [P50135-1] DR Ensembl; ENST00000329366; ENSP00000333259; ENSG00000150540. [P50135-2] DR Ensembl; ENST00000410115; ENSP00000386940; ENSG00000150540. [P50135-1] DR Ensembl; ENST00000475675; ENSP00000419415; ENSG00000150540. [P50135-3] DR GeneID; 3176; -. DR KEGG; hsa:3176; -. DR UCSC; uc002tvd.3; human. [P50135-3] DR UCSC; uc002tve.3; human. [P50135-2] DR UCSC; uc002tvf.3; human. [P50135-1] DR CTD; 3176; -. DR GeneCards; HNMT; -. DR HGNC; HGNC:5028; HNMT. DR HPA; HPA035480; -. DR HPA; HPA035481; -. DR MIM; 605238; gene. DR neXtProt; NX_P50135; -. DR PharmGKB; PA190; -. DR eggNOG; ENOG410IGS0; Eukaryota. DR eggNOG; ENOG410ZU1D; LUCA. DR GeneTree; ENSGT00390000002862; -. DR HOGENOM; HOG000231790; -. DR HOVERGEN; HBG051914; -. DR InParanoid; P50135; -. DR KO; K00546; -. DR OMA; MDISDCF; -. DR OrthoDB; EOG7Z69CQ; -. DR PhylomeDB; P50135; -. DR TreeFam; TF331080; -. DR BioCyc; MetaCyc:HS07674-MONOMER; -. DR BRENDA; 2.1.1.8; 2681. DR EvolutionaryTrace; P50135; -. DR GenomeRNAi; 3176; -. DR NextBio; 12602; -. DR PRO; PR:P50135; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; P50135; -. DR CleanEx; HS_HNMT; -. DR Genevisible; P50135; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0046539; F:histamine N-methyltransferase activity; IBA:GO_Central. DR GO; GO:0007420; P:brain development; IBA:GO_Central. DR GO; GO:0006972; P:hyperosmotic response; IEA:Ensembl. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL. DR GO; GO:0007585; P:respiratory gaseous exchange; TAS:ProtInc. DR GO; GO:0014075; P:response to amine; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl. DR GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl. DR GO; GO:0002347; P:response to tumor cell; IEA:Ensembl. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR016673; HHMT-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR PIRSF; PIRSF016616; HHMT; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51597; SAM_HNMT; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Methyltransferase; Polymorphism; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 292 Histamine N-methyltransferase. FT /FTId=PRO_0000084021. FT BINDING 28 28 Substrate. FT BINDING 60 60 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT BINDING 89 89 S-adenosyl-L-methionine. FT BINDING 94 94 S-adenosyl-L-methionine. FT BINDING 120 120 S-adenosyl-L-methionine; via amide FT nitrogen. FT BINDING 142 142 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT BINDING 283 283 Substrate. FT VAR_SEQ 47 51 IGDTK -> YQNCC (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_043482. FT VAR_SEQ 52 292 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_043483. FT VAR_SEQ 64 292 GEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAK FT TSNLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQML FT YYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKY FT GSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDIS FT DCFIDGNENGDLLWDFLTETCNFNATAPPDLRAELGKDLQE FT PEFSAKKEGKVLFNNTLSFIVIEA -> DCLIRGSSRVLKR FT NSCFILCSTRQKDKPGMRIHDERSSELPFGAARLESKSAFP FT SFLVSFILF (in isoform 2). FT {ECO:0000303|PubMed:14667820}. FT /FTId=VSP_042027. FT VARIANT 105 105 T -> I (in dbSNP:rs1801105). FT {ECO:0000269|PubMed:10803682, FT ECO:0000269|PubMed:9547362}. FT /FTId=VAR_010252. FT CONFLICT 199 199 I -> V (in Ref. 1; BAA03752). FT {ECO:0000305}. FT CONFLICT 234 234 N -> D (in Ref. 9; AAH20677). FT {ECO:0000305}. FT HELIX 8 10 {ECO:0000244|PDB:2AOT}. FT HELIX 12 23 {ECO:0000244|PDB:2AOT}. FT HELIX 28 38 {ECO:0000244|PDB:2AOT}. FT HELIX 40 43 {ECO:0000244|PDB:2AOT}. FT STRAND 44 46 {ECO:0000244|PDB:2AOT}. FT TURN 47 50 {ECO:0000244|PDB:2AOT}. FT STRAND 52 60 {ECO:0000244|PDB:2AOT}. FT HELIX 65 77 {ECO:0000244|PDB:2AOT}. FT STRAND 82 88 {ECO:0000244|PDB:2AOT}. FT HELIX 92 103 {ECO:0000244|PDB:2AOT}. FT STRAND 111 116 {ECO:0000244|PDB:2AOT}. FT HELIX 120 128 {ECO:0000244|PDB:2AOT}. FT TURN 129 131 {ECO:0000244|PDB:2AOT}. FT STRAND 136 143 {ECO:0000244|PDB:2AOT}. FT HELIX 145 147 {ECO:0000244|PDB:2AOT}. FT HELIX 151 160 {ECO:0000244|PDB:2AOT}. FT STRAND 162 173 {ECO:0000244|PDB:2AOT}. FT STRAND 175 177 {ECO:0000244|PDB:2AOW}. FT HELIX 178 186 {ECO:0000244|PDB:2AOT}. FT HELIX 187 189 {ECO:0000244|PDB:2AOT}. FT HELIX 201 211 {ECO:0000244|PDB:2AOT}. FT STRAND 215 220 {ECO:0000244|PDB:2AOT}. FT STRAND 223 225 {ECO:0000244|PDB:2AOT}. FT HELIX 227 230 {ECO:0000244|PDB:2AOT}. FT HELIX 235 245 {ECO:0000244|PDB:2AOT}. FT STRAND 247 249 {ECO:0000244|PDB:2AOT}. FT HELIX 250 253 {ECO:0000244|PDB:2AOT}. FT HELIX 256 265 {ECO:0000244|PDB:2AOT}. FT TURN 269 271 {ECO:0000244|PDB:2AOT}. FT STRAND 272 275 {ECO:0000244|PDB:2AOT}. FT STRAND 278 282 {ECO:0000244|PDB:2AOT}. FT STRAND 285 291 {ECO:0000244|PDB:2AOT}. SQ SEQUENCE 292 AA; 33295 MW; 9CCADD1EE0CCB653 CRC64; MASSMRSLFS DHGKYVESFR RFLNHSTEHQ CMQEFMDKKL PGIIGRIGDT KSEIKILSIG GGAGEIDLQI LSKVQAQYPG VCINNEVVEP SAEQIAKYKE LVAKTSNLEN VKFAWHKETS SEYQSRMLEK KELQKWDFIH MIQMLYYVKD IPATLKFFHS LLGTNAKMLI IVVSGSSGWD KLWKKYGSRF PQDDLCQYIT SDDLTQMLDN LGLKYECYDL LSTMDISDCF IDGNENGDLL WDFLTETCNF NATAPPDLRA ELGKDLQEPE FSAKKEGKVL FNNTLSFIVI EA //