ID NMNA3_HUMAN Reviewed; 252 AA. AC Q96T66; B3KVR6; D3DNF2; D3DNF3; Q8N4G1; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 11-NOV-2015, entry version 120. DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 {ECO:0000305}; DE Short=NMN/NaMN adenylyltransferase 3; DE AltName: Full=Nicotinamide-nucleotide adenylyltransferase 3; DE Short=NMN adenylyltransferase 3; DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 3; DE Short=NaMN adenylyltransferase 3; DE EC=2.7.7.18; DE AltName: Full=Pyridine nucleotide adenylyltransferase 3; DE Short=PNAT-3; DE EC=2.7.7.1; GN Name=NMNAT3; ORFNames=FKSG76; 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). RA Wang Y.-G., Gong L.; RT "Identification of FKSG76, a novel gene encoding a NMN RT adenylyltransferase."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain cortex; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon, and Kidney; 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 [6] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16118205; DOI=10.1074/jbc.M508660200; RA Berger F., Lau C., Dahlmann M., Ziegler M.; RT "Subcellular compartmentation and differential catalytic properties of RT the three human nicotinamide mononucleotide adenylyltransferase RT isoforms."; RL J. Biol. Chem. 280:36334-36341(2005). RN [7] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND RP COFACTOR. RX PubMed=17402747; DOI=10.1021/bi6023379; RA Sorci L., Cimadamore F., Scotti S., Petrelli R., Cappellacci L., RA Franchetti P., Orsomando G., Magni G.; RT "Initial-rate kinetics of human NMN-adenylyltransferases: substrate RT and metal ion specificity, inhibition by products and multisubstrate RT analogues, and isozyme contributions to NAD+ biosynthesis."; RL Biochemistry 46:4912-4922(2007). RN [8] 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 [9] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NMN; NAD AND ATP RP ANALOG, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=12574164; DOI=10.1074/jbc.M300073200; RA Zhang X., Kurnasov O.V., Karthikeyan S., Grishin N.V., Osterman A.L., RA Zhang H.; RT "Structural characterization of a human cytosolic NMN/NaMN RT adenylyltransferase and implication in human NAD biosynthesis."; RL J. Biol. Chem. 278:13503-13511(2003). CC -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide CC mononucleotide (NMN) and ATP. Can also use the deamidated form; CC nicotinic acid mononucleotide (NaMN) as substrate with the same CC efficiency. Can use triazofurin monophosphate (TrMP) as substrate. CC Can also use GTP and ITP as nucleotide donors. Also catalyzes the CC reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). CC For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, CC nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide CC guanine dinucleotide (NGD) as substrates. Fails to cleave CC phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects CC against axonal degeneration following injury. CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}. CC -!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide = CC diphosphate + NAD(+). CC -!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide = CC diphosphate + deamido-NAD(+). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:17402747}; CC Note=Divalent metal cations. Mg(2+) confers the highest activity. CC {ECO:0000269|PubMed:17402747}; CC -!- ENZYME REGULATION: Activity is strongly inhibited by galotannin. CC Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')- CC tetraphosphate (Nap4AD). {ECO:0000269|PubMed:17402747}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=209 uM for NMN {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=130 uM for NAD(+) {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=29 uM for ATP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=390 uM for PPi {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=276 uM for GTP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=350 uM for ITP {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=111 uM for NaMN {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=130 uM for NMNH {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC KM=2.01 uM for triazofurin monophosphate CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC Vmax=3.6 umol/min/mg enzyme for NAD synthesis CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC Vmax=12.8 umol/min/mg enzyme for pyrophosphorolytic NAD(+) CC cleavage {ECO:0000269|PubMed:16118205, CC ECO:0000269|PubMed:17402747}; CC Vmax=2.9 umol/min/mg enzyme for pyrophosphorolytic NADH cleavage CC {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC nicotinamide D-ribonucleotide: step 1/1. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido- CC NAD(+) from nicotinate D-ribonucleotide: step 1/1. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12574164}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12574164, CC ECO:0000269|PubMed:16118205}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96T66-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96T66-2; Sequence=VSP_010267; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q96T66-3; Sequence=VSP_043203; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in lung and spleen with lower levels CC in placenta and kidney. {ECO:0000269|PubMed:12574164, CC ECO:0000269|PubMed:16118205}. CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase CC family. {ECO:0000305}. 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; AF345564; AAK52726.1; -; mRNA. DR EMBL; AK123208; BAG53878.1; -; mRNA. DR EMBL; AC046134; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79023.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79024.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79025.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79030.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79031.1; -; Genomic_DNA. DR EMBL; BC034374; AAH34374.1; -; mRNA. DR CCDS; CCDS3111.1; -. [Q96T66-2] DR CCDS; CCDS56282.1; -. [Q96T66-3] DR RefSeq; NP_001186976.1; NM_001200047.1. [Q96T66-3] DR RefSeq; NP_835471.1; NM_178177.3. [Q96T66-2] DR RefSeq; XP_006713691.1; XM_006713628.1. [Q96T66-1] DR RefSeq; XP_006713692.1; XM_006713629.1. [Q96T66-1] DR RefSeq; XP_011511092.1; XM_011512790.1. [Q96T66-2] DR RefSeq; XP_011511093.1; XM_011512791.1. [Q96T66-2] DR UniGene; Hs.208673; -. DR UniGene; Hs.745268; -. DR PDB; 1NUP; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUQ; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUR; X-ray; 2.15 A; A/B=1-252. DR PDB; 1NUS; X-ray; 2.20 A; A/B=1-252. DR PDB; 1NUT; X-ray; 1.90 A; A/B=1-252. DR PDB; 1NUU; X-ray; 1.90 A; A/B=1-252. DR PDBsum; 1NUP; -. DR PDBsum; 1NUQ; -. DR PDBsum; 1NUR; -. DR PDBsum; 1NUS; -. DR PDBsum; 1NUT; -. DR PDBsum; 1NUU; -. DR ProteinModelPortal; Q96T66; -. DR SMR; Q96T66; 3-235. DR BioGrid; 131564; 4. DR STRING; 9606.ENSP00000340523; -. DR PhosphoSite; Q96T66; -. DR DMDM; 116242680; -. DR MaxQB; Q96T66; -. DR PaxDb; Q96T66; -. DR PRIDE; Q96T66; -. DR DNASU; 349565; -. DR Ensembl; ENST00000296202; ENSP00000296202; ENSG00000163864. [Q96T66-1] DR Ensembl; ENST00000339837; ENSP00000340523; ENSG00000163864. [Q96T66-2] DR Ensembl; ENST00000406164; ENSP00000384319; ENSG00000163864. [Q96T66-1] DR Ensembl; ENST00000413939; ENSP00000412953; ENSG00000163864. [Q96T66-3] DR GeneID; 349565; -. DR KEGG; hsa:349565; -. DR UCSC; uc003etj.3; human. [Q96T66-1] DR UCSC; uc010hul.3; human. [Q96T66-3] DR CTD; 349565; -. DR GeneCards; NMNAT3; -. DR HGNC; HGNC:20989; NMNAT3. DR HPA; HPA057402; -. DR MIM; 608702; gene. DR neXtProt; NX_Q96T66; -. DR PharmGKB; PA134952303; -. DR eggNOG; KOG3199; Eukaryota. DR eggNOG; COG1057; LUCA. DR GeneTree; ENSGT00530000063189; -. DR HOGENOM; HOG000216047; -. DR HOVERGEN; HBG052640; -. DR InParanoid; Q96T66; -. DR KO; K06210; -. DR OMA; GMYQVIQ; -. DR PhylomeDB; Q96T66; -. DR TreeFam; TF315035; -. DR BioCyc; MetaCyc:HS08953-MONOMER; -. DR BRENDA; 2.7.7.1; 2681. DR BRENDA; 2.7.7.18; 2681. DR Reactome; R-HSA-196807; Nicotinate metabolism. DR SABIO-RK; Q96T66; -. DR UniPathway; UPA00253; UER00332. DR UniPathway; UPA00253; UER00600. DR ChiTaRS; NMNAT3; human. DR EvolutionaryTrace; Q96T66; -. DR GenomeRNAi; 349565; -. DR NextBio; 99518; -. DR PRO; PR:Q96T66; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; Q96T66; -. DR CleanEx; HS_NMNAT3; -. DR ExpressionAtlas; Q96T66; baseline and differential. DR Genevisible; Q96T66; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; TAS:Reactome. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB. DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central. DR GO; GO:0009435; P:NAD biosynthetic process; IC:UniProtKB. DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome. DR GO; GO:0009611; P:response to wounding; IEA:Ensembl. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome. DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR005248; NAMN_adtrnsfrase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR12039; PTHR12039; 1. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00482; TIGR00482; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome; KW Magnesium; Mitochondrion; NAD; Nucleotide-binding; KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 252 Nicotinamide/nicotinic acid FT mononucleotide adenylyltransferase 3. FT /FTId=PRO_0000135016. FT NP_BIND 13 15 ATP. {ECO:0000269|PubMed:12574164}. FT NP_BIND 135 137 ATP. {ECO:0000269|PubMed:12574164}. FT NP_BIND 203 206 ATP. {ECO:0000269|PubMed:12574164}. FT REGION 53 55 Substrate binding. FT {ECO:0000269|PubMed:12574164}. FT REGION 90 93 Substrate binding. FT {ECO:0000269|PubMed:12574164}. FT REGION 147 148 Substrate binding. FT {ECO:0000269|PubMed:12574164}. FT BINDING 22 22 ATP. {ECO:0000269|PubMed:12574164}. FT BINDING 56 56 ATP. {ECO:0000269|PubMed:12574164}. FT BINDING 140 140 ATP; shared with dimeric partner. FT {ECO:0000269|PubMed:12574164}. FT VAR_SEQ 1 37 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_010267. FT VAR_SEQ 37 125 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043203. FT CONFLICT 169 169 G -> S (in Ref. 1; AAK52726). FT {ECO:0000305}. FT STRAND 5 13 {ECO:0000244|PDB:1NUP}. FT HELIX 20 35 {ECO:0000244|PDB:1NUP}. FT STRAND 37 48 {ECO:0000244|PDB:1NUP}. FT STRAND 54 56 {ECO:0000244|PDB:1NUP}. FT HELIX 61 71 {ECO:0000244|PDB:1NUP}. FT HELIX 72 74 {ECO:0000244|PDB:1NUP}. FT STRAND 76 80 {ECO:0000244|PDB:1NUP}. FT HELIX 83 86 {ECO:0000244|PDB:1NUP}. FT STRAND 87 89 {ECO:0000244|PDB:1NUP}. FT HELIX 93 104 {ECO:0000244|PDB:1NUP}. FT STRAND 129 135 {ECO:0000244|PDB:1NUP}. FT HELIX 136 141 {ECO:0000244|PDB:1NUP}. FT TURN 145 147 {ECO:0000244|PDB:1NUP}. FT HELIX 150 159 {ECO:0000244|PDB:1NUP}. FT STRAND 162 165 {ECO:0000244|PDB:1NUP}. FT HELIX 172 178 {ECO:0000244|PDB:1NUP}. FT HELIX 180 184 {ECO:0000244|PDB:1NUP}. FT HELIX 186 188 {ECO:0000244|PDB:1NUP}. FT STRAND 189 192 {ECO:0000244|PDB:1NUP}. FT HELIX 202 210 {ECO:0000244|PDB:1NUP}. FT HELIX 221 229 {ECO:0000244|PDB:1NUP}. FT TURN 230 233 {ECO:0000244|PDB:1NUQ}. SQ SEQUENCE 252 AA; 28322 MW; 6402CFB2FE789CF4 CRC64; MKSRIPVVLL ACGSFNPITN MHLRMFEVAR DHLHQTGMYQ VIQGIISPVN DTYGKKDLAA SHHRVAMARL ALQTSDWIRV DPWESEQAQW METVKVLRHH HSKLLRSPPQ MEGPDHGKAL FSTPAAVPEL KLLCGADVLK TFQTPNLWKD AHIQEIVEKF GLVCVGRVGH DPKGYIAESP ILRMHQHNIH LAKEPVQNEI SATYIRRALG QGQSVKYLIP DAVITYIKDH GLYTKGSTWK GKSTQSTEGK TS //