ID ARL2_HUMAN Reviewed; 184 AA. AC P36404; G3V184; Q9BUK8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 30-AUG-2017, entry version 168. DE RecName: Full=ADP-ribosylation factor-like protein 2; GN Name=ARL2; 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), AND VARIANT ALA-141. RX PubMed=8415637; DOI=10.1073/pnas.90.19.8952; RA Clark J., Moore L., Krasinskas A., Way J., Battey J.F., Tamkun J.W., RA Kahn R.A.; RT "Selective amplification of additional members of the ADP-ribosylation RT factor (ARF) family: cloning of additional human and Drosophila ARF- RT like genes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8952-8956(1993). RN [2] RP SEQUENCE REVISION TO 11. RA Kahn R.A.; RL Submitted (NOV-1997) to UniProtKB. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-141. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-141. RX PubMed=15146197; DOI=10.1038/nbt971; RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., RA Li Y., Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., RA Lebkowski J., Stanton L.W.; RT "Transcriptome characterization elucidates signaling networks that RT control human ES cell growth and differentiation."; RL Nat. Biotechnol. 22:707-716(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [8] RP INTERACTION WITH ARL2BP. RX PubMed=10488091; DOI=10.1074/jbc.274.39.27553; RA Sharer J.D., Kahn R.A.; RT "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, RT and initial characterization."; RL J. Biol. Chem. 274:27553-27561(1999). RN [9] RP FUNCTION, INTERACTION WITH TBCD, AND MUTAGENESIS OF THR-30; THR-47; RP PHE-50 AND GLN-70. RX PubMed=10831612; DOI=10.1083/jcb.149.5.1087; RA Bhamidipati A., Lewis S.A., Cowan N.J.; RT "ADP ribosylation factor-like protein 2 (Arl2) regulates the RT interaction of tubulin-folding cofactor D with native tubulin."; RL J. Cell Biol. 149:1087-1096(2000). RN [10] RP INTERACTION WITH ARL2BP AND PDE6D, AND MUTAGENESIS OF GLN-70. RX PubMed=11303027; DOI=10.1074/jbc.M102359200; RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.; RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both RT specific and shared effectors: characterizing ARL1-binding proteins."; RL J. Biol. Chem. 276:22826-22837(2001). RN [11] RP INTERACTION WITH ARL2BP. RX PubMed=11847227; DOI=10.1074/jbc.M200128200; RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., RA Cowan N.J.; RT "Functional overlap between retinitis pigmentosa 2 protein and the RT tubulin-specific chaperone cofactor C."; RL J. Biol. Chem. 277:14629-14634(2002). RN [12] RP SUBCELLULAR LOCATION, AND LACK OF N-MYRISTOYLATION. RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245; RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.; RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide RT transporter."; RL Mol. Biol. Cell 13:71-83(2002). RN [13] RP FUNCTION, MUTAGENESIS OF GLN-70, AND SUBCELLULAR LOCATION. RX PubMed=16525022; DOI=10.1091/mbc.E05-10-0929; RA Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.; RT "Arl2 and Arl3 regulate different microtubule-dependent processes."; RL Mol. Biol. Cell 17:2476-2487(2006). RN [14] RP INTERACTION WITH ELMOD2. RX PubMed=17452337; DOI=10.1074/jbc.M701347200; RA Bowzard J.B., Cheng D., Peng J., Kahn R.A.; RT "ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs."; RL J. Biol. Chem. 282:17568-17580(2007). RN [15] RP FUNCTION, AND GTP/GDP BINDING. RX PubMed=18588884; DOI=10.1016/j.febslet.2008.05.053; RA Veltel S., Kravchenko A., Ismail S., Wittinghofer A.; RT "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3- RT effector-GAP complex."; RL FEBS Lett. 582:2501-2507(2008). RN [16] RP FUNCTION, INTERACTION WITH ARL2BP, MUTAGENESIS OF THR-30 AND GLN-70, RP AND SUBCELLULAR LOCATION. RX PubMed=18234692; DOI=10.1093/intimm/dxm154; RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N., RA Matsuda T.; RT "BART is essential for nuclear retention of STAT3."; RL Int. Immunol. 20:395-403(2008). RN [17] RP INTERACTION WITH ARL2BP. RX PubMed=18981177; DOI=10.1074/jbc.M806167200; RA Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E., RA Nietlispach D., Owen D., Mott H.R.; RT "The structure of binder of Arl2 (BART) reveals a novel G protein RT binding domain: implications for function."; RL J. Biol. Chem. 284:992-999(2009). RN [18] RP FUNCTION. RX PubMed=20740604; DOI=10.1002/cm.20480; RA Tian G., Thomas S., Cowan N.J.; RT "Effect of TBCD and its regulatory interactor Arl2 on tubulin and RT microtubule integrity."; RL Cytoskeleton 67:706-714(2010). RN [19] 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 [20] RP INTERACTION WITH TBCD. RX PubMed=27666374; DOI=10.1016/j.ajhg.2016.08.005; RA Miyake N., Fukai R., Ohba C., Chihara T., Miura M., Shimizu H., RA Kakita A., Imagawa E., Shiina M., Ogata K., Okuno-Yuguchi J., RA Fueki N., Ogiso Y., Suzumura H., Watabe Y., Imataka G., Leong H.Y., RA Fattal-Valevski A., Kramer U., Miyatake S., Kato M., Okamoto N., RA Sato Y., Mitsuhashi S., Nishino I., Kaneko N., Nishiyama A., RA Tamura T., Mizuguchi T., Nakashima M., Tanaka F., Saitsu H., RA Matsumoto N.; RT "Biallelic TBCD mutations cause early-onset neurodegenerative RT encephalopathy."; RL Am. J. Hum. Genet. 99:950-961(2016). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-184 IN A COMPLEX WITH RP ARL2BP; GTP AND MAGNESIUM IONS, INTERACTION WITH ARL2BP, AND RP MUTAGENESIS OF LEU-3; LEU-4; ILE-6; LEU-7; PHE-50; TYR-76 AND TYR-80. RX PubMed=19368893; DOI=10.1016/j.str.2009.01.014; RA Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J.; RT "Crystal structure of the ARL2-GTP-BART complex reveals a novel RT recognition and binding mode of small GTPase with effector."; RL Structure 17:602-610(2009). CC -!- FUNCTION: Small GTP-binding protein which cycles between an CC inactive GDP-bound and an active GTP-bound form, and the rate of CC cycling is regulated by guanine nucleotide exchange factors (GEF) CC and GTPase-activating proteins (GAP). GTP-binding protein that CC does not act as an allosteric activator of the cholera toxin CC catalytic subunit. Regulates formation of new microtubules and CC centrosome integrity. Prevents the TBCD-induced microtubule CC destruction. Participates in association with TBCD, in the CC disassembly of the apical junction complexes. Antagonizes the CC effect of TBCD on epithelial cell detachment and tight and CC adherens junctions disassembly. Together with ARL2, plays a role CC in the nuclear translocation, retention and transcriptional CC activity of STAT3. Component of a regulated secretory pathway CC involved in Ca(2+)-dependent release of acetylcholine. Required CC for normal progress through the cell cycle. CC {ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:16525022, CC ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18588884, CC ECO:0000269|PubMed:20740604}. CC -!- SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6. Found CC in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E CC and TBCD. Found in a complex with ARL2, ARL2BP and SLC25A4. The CC GTP-bound form interacts with PDE6D. Interacts with ELMOD2. The CC GTP-bound form interacts with ARL2BP. Interacts, preferentially in CC its GDP-bound state, with TBCD. Interacts with UNC119. CC {ECO:0000269|PubMed:10488091, ECO:0000269|PubMed:10831612, CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:11847227, CC ECO:0000269|PubMed:17452337, ECO:0000269|PubMed:18234692, CC ECO:0000269|PubMed:18981177, ECO:0000269|PubMed:19368893, CC ECO:0000269|PubMed:27666374}. CC -!- INTERACTION: CC Q9Y2Y0:ARL2BP; NbExp=13; IntAct=EBI-752365, EBI-3449344; CC O43924:PDE6D; NbExp=16; IntAct=EBI-752365, EBI-712685; CC Q9BZK7:TBL1XR1; NbExp=3; IntAct=EBI-752365, EBI-765729; CC Q13432:UNC119; NbExp=8; IntAct=EBI-752365, EBI-711260; CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. CC Cytoplasm, cytoskeleton, microtubule organizing center, CC centrosome. Nucleus. Cytoplasm. Note=The complex formed with CC ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. The complex CC formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria CC (By similarity). Not detected in the Golgi, nucleus and on the CC mitotic spindle. Centrosome-associated throughout the cell cycle. CC Not detected to interphase microtubules. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P36404-1; Sequence=Displayed; CC Name=2; CC IsoId=P36404-2; Sequence=VSP_047278; CC -!- PTM: Not N-myristoylated. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {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; L13687; AAC37606.1; -; mRNA. DR EMBL; AF493888; AAM12602.1; -; mRNA. DR EMBL; CN338497; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AP000436; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74333.1; -; Genomic_DNA. DR EMBL; BC002530; AAH02530.1; -; mRNA. DR CCDS; CCDS55770.1; -. [P36404-2] DR CCDS; CCDS8088.1; -. [P36404-1] DR PIR; A48259; A48259. DR RefSeq; NP_001186674.1; NM_001199745.1. [P36404-2] DR RefSeq; NP_001658.2; NM_001667.3. [P36404-1] DR UniGene; Hs.502836; -. DR PDB; 3DOE; X-ray; 2.25 A; A=1-184. DR PDB; 3DOF; X-ray; 3.30 A; A=1-184. DR PDBsum; 3DOE; -. DR PDBsum; 3DOF; -. DR ProteinModelPortal; P36404; -. DR SMR; P36404; -. DR BioGrid; 106895; 32. DR DIP; DIP-47535N; -. DR IntAct; P36404; 11. DR MINT; MINT-6602180; -. DR STRING; 9606.ENSP00000246747; -. DR iPTMnet; P36404; -. DR PhosphoSitePlus; P36404; -. DR BioMuta; ARL2; -. DR DMDM; 116241255; -. DR EPD; P36404; -. DR PaxDb; P36404; -. DR PeptideAtlas; P36404; -. DR PRIDE; P36404; -. DR DNASU; 402; -. DR Ensembl; ENST00000246747; ENSP00000246747; ENSG00000213465. [P36404-1] DR Ensembl; ENST00000529384; ENSP00000436021; ENSG00000213465. [P36404-1] DR Ensembl; ENST00000533729; ENSP00000432971; ENSG00000213465. [P36404-2] DR GeneID; 402; -. DR KEGG; hsa:402; -. DR UCSC; uc021qlc.2; human. [P36404-1] DR CTD; 402; -. DR DisGeNET; 402; -. DR GeneCards; ARL2; -. DR H-InvDB; HIX0079396; -. DR HGNC; HGNC:693; ARL2. DR HPA; HPA044610; -. DR MIM; 601175; gene. DR neXtProt; NX_P36404; -. DR OpenTargets; ENSG00000213465; -. DR PharmGKB; PA24986; -. DR eggNOG; KOG0073; Eukaryota. DR eggNOG; ENOG410XRG9; LUCA. DR GeneTree; ENSGT00780000121855; -. DR HOGENOM; HOG000163691; -. DR HOVERGEN; HBG002073; -. DR InParanoid; P36404; -. DR KO; K07943; -. DR OMA; RTLRPYW; -. DR OrthoDB; EOG091G0O6V; -. DR PhylomeDB; P36404; -. DR TreeFam; TF105462; -. DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway. DR Reactome; R-HSA-422356; Regulation of insulin secretion. DR EvolutionaryTrace; P36404; -. DR GeneWiki; ARL2; -. DR GenomeRNAi; 402; -. DR PRO; PR:P36404; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000213465; -. DR CleanEx; HS_ARL2; -. DR ExpressionAtlas; P36404; baseline and differential. DR Genevisible; P36404; HS. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IEA:Ensembl. DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB. DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc. DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB. DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:UniProtKB. DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome. DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR GO; GO:0007021; P:tubulin complex assembly; TAS:ProtInc. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR024156; Small_GTPase_ARF. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51417; ARF; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Complete proteome; KW Cytoplasm; Cytoskeleton; GTP-binding; Isopeptide bond; Lipoprotein; KW Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Ubl conjugation. FT INIT_MET 1 1 Removed. {ECO:0000255}. FT CHAIN 2 184 ADP-ribosylation factor-like protein 2. FT /FTId=PRO_0000207453. FT NP_BIND 23 30 GTP. {ECO:0000250}. FT NP_BIND 66 70 GTP. {ECO:0000250}. FT NP_BIND 125 128 GTP. {ECO:0000250}. FT BINDING 68 68 GTP; via amide nitrogen. {ECO:0000250}. FT MOD_RES 45 45 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9D0J4}. FT LIPID 2 2 N-myristoyl glycine. {ECO:0000255}. FT CROSSLNK 71 71 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 113 139 Missing (in isoform 2). FT {ECO:0000303|PubMed:15146197}. FT /FTId=VSP_047278. FT VARIANT 141 141 V -> A (in dbSNP:rs664226). FT {ECO:0000269|PubMed:15146197, FT ECO:0000269|PubMed:8415637, FT ECO:0000269|Ref.3}. FT /FTId=VAR_028056. FT MUTAGEN 3 3 L->A: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT MUTAGEN 3 3 L->D: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT MUTAGEN 4 4 L->A: Does not reduce interaction with FT ARL2BP. {ECO:0000269|PubMed:19368893}. FT MUTAGEN 4 4 L->D: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT MUTAGEN 6 6 I->R: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT MUTAGEN 7 7 L->A: Does not reduce interaction with FT ARL2BP. {ECO:0000269|PubMed:19368893}. FT MUTAGEN 7 7 L->D: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT MUTAGEN 30 30 T->N: Does not inhibit the interaction FT with TBCD and rescues the TBCD-induced FT microtubule destruction. Reduces FT interaction with ARL2BP. Inhibits FT accumulation of STAT3 in the nucleus. FT {ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:18234692}. FT MUTAGEN 47 47 T->A: Does not inhibit the interaction FT with TBCD and rescues the TBCD-induced FT microtubule destruction. FT {ECO:0000269|PubMed:10831612}. FT MUTAGEN 50 50 F->A: Reduces interaction with ARL2BP. FT Inhibits the interaction with TBCD and FT rescues the TBCD-induced microtubule FT destruction. FT {ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:19368893}. FT MUTAGEN 70 70 Q->L: Induces cell cycle arrest, reduces FT ability to form microtubules and FT centrosome fragmentation. Inhibits the FT interaction with TBCD and does not rescue FT the TBCD-induced microtubule destruction. FT Interacts with ARL2BP and PDE6D. FT {ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:11303027, FT ECO:0000269|PubMed:16525022, FT ECO:0000269|PubMed:18234692}. FT MUTAGEN 76 76 Y->A: Does not reduce interaction with FT ARL2BP. {ECO:0000269|PubMed:19368893}. FT MUTAGEN 80 80 Y->A: Reduces interaction with ARL2BP. FT {ECO:0000269|PubMed:19368893}. FT HELIX 3 9 {ECO:0000244|PDB:3DOE}. FT STRAND 16 22 {ECO:0000244|PDB:3DOE}. FT HELIX 29 37 {ECO:0000244|PDB:3DOE}. FT STRAND 48 54 {ECO:0000244|PDB:3DOE}. FT STRAND 60 67 {ECO:0000244|PDB:3DOE}. FT HELIX 71 80 {ECO:0000244|PDB:3DOE}. FT STRAND 85 92 {ECO:0000244|PDB:3DOE}. FT HELIX 96 98 {ECO:0000244|PDB:3DOE}. FT HELIX 99 110 {ECO:0000244|PDB:3DOE}. FT HELIX 113 115 {ECO:0000244|PDB:3DOE}. FT STRAND 119 125 {ECO:0000244|PDB:3DOE}. FT HELIX 135 140 {ECO:0000244|PDB:3DOE}. FT HELIX 141 146 {ECO:0000244|PDB:3DOE}. FT STRAND 152 156 {ECO:0000244|PDB:3DOE}. FT TURN 159 162 {ECO:0000244|PDB:3DOE}. FT HELIX 165 184 {ECO:0000244|PDB:3DOE}. SQ SEQUENCE 184 AA; 20878 MW; 0823F005719C17F9 CRC64; MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE VLELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD //