ID IPO13_HUMAN Reviewed; 963 AA. AC O94829; D3DPY4; Q5T4X3; Q7LC04; Q96HS3; Q9H8N3; Q9UFR1; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 3. DT 27-MAR-2024, entry version 183. DE RecName: Full=Importin-13; DE Short=Imp13; DE AltName: Full=Karyopherin-13; DE Short=Kap13; DE AltName: Full=Ran-binding protein 13; DE Short=RanBP13; GN Name=IPO13; Synonyms=KIAA0724, RANBP13; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RBM8A; UBC9 AND RP EIF1A. RX PubMed=11447110; DOI=10.1093/emboj/20.14.3685; RA Mingot J.-M., Kostka S., Kraft R., Hartmann E., Goerlich D.; RT "Importin 13: a novel mediator of nuclear import and export."; RL EMBO J. 20:3685-3694(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-963. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-963. RC TISSUE=Placenta; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [8] RP FUNCTION, AND INTERACTION WITH PAX6. RX PubMed=15143176; DOI=10.1128/mcb.24.11.4824-4834.2004; RA Ploski J.E., Shamsher M.K., Radu A.; RT "Paired-type homeodomain transcription factors are imported into the RT nucleus by karyopherin 13."; RL Mol. Cell. Biol. 24:4824-4834(2004). RN [9] RP TISSUE SPECIFICITY. RX PubMed=10745026; DOI=10.1165/ajrcmb.22.4.3929; RA Zhang C., Sweezey N.B., Gagnon S., Muskat B., Koehler D., Post M., RA Kaplan F.; RT "A novel karyopherin-beta homolog is developmentally and hormonally RT regulated in fetal lung."; RL Am. J. Respir. Cell Mol. Biol. 22:451-459(2000). 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., Buerckstuemmer T., RA 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 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH YEAST GSP1/RAN, AND RP REPEAT STRUCTURE. RX PubMed=20122403; DOI=10.1016/j.molcel.2010.01.007; RA Bono F., Cook A.G., Grunwald M., Ebert J., Conti E.; RT "Nuclear import mechanism of the EJC component Mago-Y14 revealed by RT structural studies of importin 13."; RL Mol. Cell 37:211-222(2010). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH UBE2I/UBC. RX PubMed=21139563; DOI=10.1038/emboj.2010.320; RA Grunwald M., Bono F.; RT "Structure of Importin13-Ubc9 complex: nuclear import and release of a key RT regulator of sumoylation."; RL EMBO J. 30:427-438(2011). CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport CC receptor. Serves as receptor for nuclear localization signals (NLS) in CC cargo substrates. Is thought to mediate docking of the CC importin/substrate complex to the nuclear pore complex (NPC) through CC binding to nucleoporin and the complex is subsequently translocated CC through the pore by an energy requiring, Ran-dependent mechanism. At CC the nucleoplasmic side of the NPC, Ran binds to the importin, the CC importin/substrate complex dissociates and importin is re-exported from CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The CC directionality of nuclear import is thought to be conferred by an CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between CC the cytoplasm and nucleus (By similarity). Mediates the nuclear import CC of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of CC the paired homeobox family. Also mediates nuclear export of eIF-1A, and CC the cytoplasmic release of eIF-1A is triggered by the loading of import CC substrates onto IPO13. {ECO:0000250, ECO:0000269|PubMed:11447110, CC ECO:0000269|PubMed:15143176}. CC -!- SUBUNIT: Interacts with UBC9, RAN, RBM8A, eIF-1A and PAX6. CC {ECO:0000269|PubMed:11447110, ECO:0000269|PubMed:15143176, CC ECO:0000269|PubMed:20122403, ECO:0000269|PubMed:21139563}. CC -!- INTERACTION: CC O94829; Q15699: ALX1; NbExp=2; IntAct=EBI-747310, EBI-750671; CC O94829; Q6RFH8: DUX4L9; NbExp=2; IntAct=EBI-747310, EBI-11599882; CC O94829; P47813: EIF1AX; NbExp=14; IntAct=EBI-747310, EBI-1045377; CC O94829; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-747310, EBI-2549423; CC O94829; P61326: MAGOH; NbExp=4; IntAct=EBI-747310, EBI-299134; CC O94829; P23760-8: PAX3; NbExp=3; IntAct=EBI-747310, EBI-12105196; CC O94829; Q9BYU1: PBX4; NbExp=8; IntAct=EBI-747310, EBI-10302990; CC O94829; P78337: PITX1; NbExp=4; IntAct=EBI-747310, EBI-748265; CC O94829; P25786: PSMA1; NbExp=3; IntAct=EBI-747310, EBI-359352; CC O94829; P62826: RAN; NbExp=13; IntAct=EBI-747310, EBI-286642; CC O94829; P63279: UBE2I; NbExp=6; IntAct=EBI-747310, EBI-80168; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, heart, intestine and CC kidney. {ECO:0000269|PubMed:10745026}. CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34444.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14575.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AF267987; AAF73471.1; -; mRNA. DR EMBL; AB018267; BAA34444.2; ALT_INIT; mRNA. DR EMBL; AL357079; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07072.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07073.1; -; Genomic_DNA. DR EMBL; BC008194; AAH08194.1; -; mRNA. DR EMBL; AL117501; CAB55966.1; -; mRNA. DR EMBL; AK023441; BAB14575.1; ALT_INIT; mRNA. DR CCDS; CCDS503.1; -. DR PIR; T17276; T17276. DR RefSeq; NP_055467.3; NM_014652.3. DR PDB; 2X19; X-ray; 2.80 A; B=1-963. DR PDB; 2XWU; X-ray; 2.80 A; B=1-963. DR PDB; 3ZJY; X-ray; 3.60 A; B/E/G=1-963. DR PDBsum; 2X19; -. DR PDBsum; 2XWU; -. DR PDBsum; 3ZJY; -. DR AlphaFoldDB; O94829; -. DR SMR; O94829; -. DR BioGRID; 115025; 122. DR CORUM; O94829; -. DR IntAct; O94829; 38. DR MINT; O94829; -. DR STRING; 9606.ENSP00000361418; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR iPTMnet; O94829; -. DR PhosphoSitePlus; O94829; -. DR BioMuta; IPO13; -. DR EPD; O94829; -. DR jPOST; O94829; -. DR MassIVE; O94829; -. DR MaxQB; O94829; -. DR PaxDb; 9606-ENSP00000361418; -. DR PeptideAtlas; O94829; -. DR ProteomicsDB; 50474; -. DR Pumba; O94829; -. DR Antibodypedia; 32405; 140 antibodies from 21 providers. DR DNASU; 9670; -. DR Ensembl; ENST00000372343.8; ENSP00000361418.3; ENSG00000117408.11. DR GeneID; 9670; -. DR KEGG; hsa:9670; -. DR MANE-Select; ENST00000372343.8; ENSP00000361418.3; NM_014652.4; NP_055467.3. DR UCSC; uc001ckx.4; human. DR AGR; HGNC:16853; -. DR CTD; 9670; -. DR DisGeNET; 9670; -. DR GeneCards; IPO13; -. DR HGNC; HGNC:16853; IPO13. DR HPA; ENSG00000117408; Tissue enhanced (skeletal). DR MIM; 610411; gene. DR neXtProt; NX_O94829; -. DR OpenTargets; ENSG00000117408; -. DR PharmGKB; PA134981096; -. DR VEuPathDB; HostDB:ENSG00000117408; -. DR eggNOG; KOG2022; Eukaryota. DR GeneTree; ENSGT00530000063347; -. DR HOGENOM; CLU_005996_3_0_1; -. DR InParanoid; O94829; -. DR OMA; KYPAEMA; -. DR OrthoDB; 4504744at2759; -. DR PhylomeDB; O94829; -. DR TreeFam; TF314539; -. DR PathwayCommons; O94829; -. DR SignaLink; O94829; -. DR BioGRID-ORCS; 9670; 751 hits in 1170 CRISPR screens. DR ChiTaRS; IPO13; human. DR EvolutionaryTrace; O94829; -. DR GeneWiki; IPO13; -. DR GenomeRNAi; 9670; -. DR Pharos; O94829; Tbio. DR PRO; PR:O94829; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; O94829; Protein. DR Bgee; ENSG00000117408; Expressed in C1 segment of cervical spinal cord and 201 other cell types or tissues. DR ExpressionAtlas; O94829; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR013598; Exportin-1/Importin-b-like. DR InterPro; IPR001494; Importin-beta_N. DR InterPro; IPR040709; Importin_rep_1. DR InterPro; IPR040944; Importin_rep_2. DR InterPro; IPR040520; Importin_rep_3. DR PANTHER; PTHR12363:SF56; IMPORTIN-13; 1. DR PANTHER; PTHR12363; TRANSPORTIN 3 AND IMPORTIN 13; 1. DR Pfam; PF03810; IBN_N; 1. DR Pfam; PF18773; Importin_rep; 1. DR Pfam; PF18786; Importin_rep_2; 2. DR Pfam; PF18806; Importin_rep_3; 1. DR Pfam; PF08389; Xpo1; 1. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; O94829; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Nucleus; Protein transport; Reference proteome; KW Repeat; Transport. FT CHAIN 1..963 FT /note="Importin-13" FT /id="PRO_0000120758" FT REPEAT 24..54 FT /note="HEAT 1" FT /evidence="ECO:0000269|PubMed:20122403" FT DOMAIN 45..111 FT /note="Importin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115" FT REPEAT 56..88 FT /note="HEAT 2" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 95..135 FT /note="HEAT 3" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 142..179 FT /note="HEAT 4" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 194..231 FT /note="HEAT 5" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 236..268 FT /note="HEAT 6" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 276..325 FT /note="HEAT 7" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 330..372 FT /note="HEAT 8" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 375..438 FT /note="HEAT 9" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 440..476 FT /note="HEAT 10" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 487..522 FT /note="HEAT 11" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 524..558 FT /note="HEAT 12" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 562..600 FT /note="HEAT 13" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 603..648 FT /note="HEAT 14" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 676..716 FT /note="HEAT 15" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 720..754 FT /note="HEAT 16" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 761..803 FT /note="HEAT 17" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 815..845 FT /note="HEAT 18" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 860..893 FT /note="HEAT 19" FT /evidence="ECO:0000269|PubMed:20122403" FT REPEAT 897..931 FT /note="HEAT 20" FT /evidence="ECO:0000269|PubMed:20122403" FT CONFLICT 202 FT /note="F -> V (in Ref. 6; CAB55966)" FT /evidence="ECO:0000305" FT CONFLICT 715 FT /note="T -> A (in Ref. 7; BAB14575)" FT /evidence="ECO:0000305" FT CONFLICT 817 FT /note="A -> S (in Ref. 5; AAH08194)" FT /evidence="ECO:0000305" FT HELIX 23..35 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 39..54 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 72..88 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 98..111 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 117..134 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 135..138 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 142..150 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 160..177 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 216..230 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:2XWU" FT HELIX 236..238 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 240..249 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 256..267 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 276..287 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 290..298 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 302..325 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 330..344 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 350..353 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 361..371 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 376..401 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 406..410 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 414..438 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 440..455 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 463..476 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 483..486 FT /evidence="ECO:0007829|PDB:2XWU" FT HELIX 487..494 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 495..497 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 503..515 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 517..522 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 524..527 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 528..530 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 531..537 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 541..543 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 544..557 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 563..565 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 566..578 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 584..598 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 603..625 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 631..650 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 676..695 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 699..715 FT /evidence="ECO:0007829|PDB:2X19" FT STRAND 716..718 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 721..723 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 724..737 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 741..754 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 758..760 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 762..781 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 783..785 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 787..803 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 805..809 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 815..825 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 831..844 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 845..847 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 853..857 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 858..860 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 862..873 FT /evidence="ECO:0007829|PDB:2X19" FT TURN 874..876 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 879..881 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 882..895 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 897..907 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 920..930 FT /evidence="ECO:0007829|PDB:2X19" FT HELIX 937..952 FT /evidence="ECO:0007829|PDB:2X19" SQ SEQUENCE 963 AA; 108195 MW; 8C696EE2B92365F0 CRC64; MERREEQPGA AGAGAAPALD FTVENVEKAL HQLYYDPNIE NKNLAQKWLM QAQVSPQAWH FSWQLLQPDK VPEIQYFGAS ALHIKISRYW SDIPTDQYES LKAQLFTQIT RFASGSKIVL TRLCVALASL ALSMMPDAWP CAVADMVRLF QAEDSPVDGQ GRCLALLELL TVLPEEFQTS RLPQYRKGLV RTSLAVECGA VFPLLEQLLQ QPSSPSCVRQ KVLKCFSSWV QLEVPLQDCE ALIQAAFAAL QDSELFDSSV EAIVNAISQP DAQRYVNTLL KLIPLVLGLQ EQLRQAVQNG DMETSHGICR IAVALGENHS RALLDQVEHW QSFLALVNMI MFCTGIPGHY PVNETTSSLT LTFWYTLQDD ILSFEAEKQA VYQQVYRPVY FQLVDVLLHK AQFPSDEEYG FWSSDEKEQF RIYRVDISDT LMYVYEMLGA ELLSNLYDKL GRLLTSSEEP YSWQHTEALL YGFQSIAETI DVNYSDVVPG LIGLIPRISI SNVQLADTVM FTIGALSEWL ADHPVMINSV LPLVLHALGN PELSVSSVST LKKICRECKY DLPPYAANIV AVSQDVLMKQ IHKTSQCMWL MQALGFLLSA LQVEEILKNL HSLISPYIQQ LEKLAEEIPN PSNKLAIVHI LGLLSNLFTT LDISHHEDDH EGPELRKLPV PQGPNPVVVV LQQVFQLIQK VLSKWLNDAQ VVEAVCAIFE KSVKTLLDDF APMVPQLCEM LGRMYSTIPQ ASALDLTRQL VHIFAHEPAH FPPIEALFLL VTSVTLTLFQ QGPRDHPDIV DSFMQLLAQA LKRKPDLFLC ERLDVKAVFQ CAVLALKFPE APTVKASCGF FTELLPRCGE VESVGKVVQE DGRMLLIAVL EAIGGQASRS LMDCFADILF ALNKHCFSLL SMWIKEALQP PGFPSARLSP EQKDTFSQQI LRERVNKRRV KEMVKEFTLL CRGLHGTDYT ADY //