ID IMA6_HUMAN Reviewed; 539 AA. AC O15131; B2RAI5; Q86X23; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 27-MAR-2024, entry version 204. DE RecName: Full=Importin subunit alpha-6 {ECO:0000305}; DE AltName: Full=Karyopherin subunit alpha-5; GN Name=KPNA5 {ECO:0000312|HGNC:HGNC:6398}; 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 [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [2] 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-539. RX PubMed=9395085; DOI=10.1016/s0014-5793(97)01265-9; RA Koehler M., Ansieau S., Prehn S., Leutz A., Haller H., Hartmann E.; RT "Cloning of two novel human importin-alpha subunits and analysis of the RT expression pattern of the importin-alpha protein family."; RL FEBS Lett. 417:104-108(1997). RN [6] RP INTERACTION WITH STAT1; STAT2 AND INFLUENZA VIRUS NP. RX PubMed=12740372; DOI=10.1074/jbc.m303571200; RA Melen K., Fagerlund R., Franke J., Koehler M., Kinnunen L., Julkunen I.; RT "Importin alpha nuclear localization signal binding sites for STAT1, STAT2, RT and influenza A virus nucleoprotein."; RL J. Biol. Chem. 278:28193-28200(2003). RN [7] RP INTERACTION WITH HCMV UL84. RX PubMed=12610148; DOI=10.1128/jvi.77.6.3734-3748.2003; RA Lischka P., Sorg G., Kann M., Winkler M., Stamminger T.; RT "A nonconventional nuclear localization signal within the UL84 protein of RT human cytomegalovirus mediates nuclear import via the importin alpha/beta RT pathway."; RL J. Virol. 77:3734-3748(2003). RN [8] RP INTERACTION WITH EBOLAVIRUS VP24 (MICROBIAL INFECTION). RX PubMed=17928350; DOI=10.1128/jvi.01097-07; RA Reid S.P., Valmas C., Martinez O., Sanchez F.M., Basler C.F.; RT "Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily RT karyopherin alpha proteins with activated STAT1."; RL J. Virol. 81:13469-13477(2007). RN [9] 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 [10] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-48 AND SER-319. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Functions in nuclear protein import as an adapter protein for CC nuclear receptor KPNB1. Binds specifically and directly to substrates CC containing either a simple or bipartite NLS motif. Docking of the CC importin/substrate complex to the nuclear pore complex (NPC) is CC mediated by KPNB1 through binding to nucleoporin FxFG repeats and the CC complex is subsequently translocated through the pore by an energy CC requiring, Ran-dependent mechanism. At the nucleoplasmic side of the CC NPC, Ran binds to importin-beta and the three components separate and CC importin-alpha and -beta are re-exported from the nucleus to the CC cytoplasm where GTP hydrolysis releases Ran from importin. 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. Mediates nuclear import of STAT1 homodimers CC and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1 CC and STAT2 through ARM repeats 8-9. Recognizes influenza A virus CC nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear CC import of human cytomegalovirus UL84 by recognizing a non-classical CC NLS. CC -!- SUBUNIT: Forms a complex with importin subunit beta-1. CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus protein VP24. CC {ECO:0000269|PubMed:17928350}. CC -!- INTERACTION: CC O15131; Q9GZX7: AICDA; NbExp=2; IntAct=EBI-540602, EBI-3834328; CC O15131; Q92688: ANP32B; NbExp=7; IntAct=EBI-540602, EBI-762428; CC O15131; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-540602, EBI-745689; CC O15131; P46527: CDKN1B; NbExp=6; IntAct=EBI-540602, EBI-519280; CC O15131; P13569: CFTR; NbExp=4; IntAct=EBI-540602, EBI-349854; CC O15131; Q96C86: DCPS; NbExp=3; IntAct=EBI-540602, EBI-3917181; CC O15131; P07910: HNRNPC; NbExp=3; IntAct=EBI-540602, EBI-357966; CC O15131; Q92993: KAT5; NbExp=3; IntAct=EBI-540602, EBI-399080; CC O15131; P20700: LMNB1; NbExp=3; IntAct=EBI-540602, EBI-968218; CC O15131; P40692: MLH1; NbExp=3; IntAct=EBI-540602, EBI-744248; CC O15131; Q9HAN9: NMNAT1; NbExp=3; IntAct=EBI-540602, EBI-3917542; CC O15131; Q16656-4: NRF1; NbExp=3; IntAct=EBI-540602, EBI-11742836; CC O15131; Q9UKX7: NUP50; NbExp=9; IntAct=EBI-540602, EBI-2371082; CC O15131; Q9BUI4: POLR3C; NbExp=5; IntAct=EBI-540602, EBI-5452779; CC O15131; P78424: POU6F2; NbExp=3; IntAct=EBI-540602, EBI-12029004; CC O15131; P43351: RAD52; NbExp=3; IntAct=EBI-540602, EBI-706448; CC O15131; Q6IQ16: SPOPL; NbExp=4; IntAct=EBI-540602, EBI-2822161; CC O15131; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-540602, EBI-2559824; CC O15131; Q5BKZ1: ZNF326; NbExp=3; IntAct=EBI-540602, EBI-2560158; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Testis. CC -!- DOMAIN: Consists of an N-terminal hydrophilic region, a hydrophobic CC central region composed of 10 repeats, and a short hydrophilic C- CC terminus. The N-terminal hydrophilic region contains the importin beta CC binding domain (IBB domain), which is sufficient for binding importin CC beta and essential for nuclear protein import. CC -!- DOMAIN: The IBB domain is thought to act as an intrasteric CC autoregulatory sequence by interacting with the internal autoinhibitory CC NLS. Binding of KPNB1 probably overlaps the internal NLS and CC contributes to a high affinity for cytoplasmic NLS-containing cargo CC substrates. After dissociation of the importin/substrate complex in the CC nucleus the internal autohibitory NLS contributes to a low affinity for CC nuclear NLS-containing proteins (By similarity). {ECO:0000250}. CC -!- DOMAIN: The major and minor NLS binding sites are mainly involved in CC recognition of simple or bipartite NLS motifs. Structurally located CC within in a helical surface groove they contain several conserved Trp CC and Asn residues of the corresponding third helices (H3) of ARM repeats CC which mainly contribute to binding (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC51868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG36882.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW48216.1; Type=Erroneous gene model prediction; 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; AK314206; BAG36882.1; ALT_INIT; mRNA. DR EMBL; AL132795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF458260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48216.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC047409; AAH47409.1; -; mRNA. DR EMBL; AF005361; AAC51868.1; ALT_INIT; mRNA. DR CCDS; CCDS5111.1; -. DR RefSeq; NP_002260.2; NM_002269.2. DR RefSeq; XP_016866328.1; XM_017010839.1. DR RefSeq; XP_016866329.1; XM_017010840.1. DR PDB; 4U2X; X-ray; 3.15 A; D/E/F=332-506. DR PDBsum; 4U2X; -. DR AlphaFoldDB; O15131; -. DR SMR; O15131; -. DR BioGRID; 110039; 104. DR ComplexPortal; CPX-1063; Importin complex, KPNA5 variant. DR DIP; DIP-33405N; -. DR ELM; O15131; -. DR IntAct; O15131; 43. DR MINT; O15131; -. DR STRING; 9606.ENSP00000357552; -. DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family. DR iPTMnet; O15131; -. DR PhosphoSitePlus; O15131; -. DR SwissPalm; O15131; -. DR BioMuta; KPNA5; -. DR EPD; O15131; -. DR jPOST; O15131; -. DR MassIVE; O15131; -. DR MaxQB; O15131; -. DR PaxDb; 9606-ENSP00000357552; -. DR PeptideAtlas; O15131; -. DR ProteomicsDB; 48467; -. DR Pumba; O15131; -. DR Antibodypedia; 32522; 266 antibodies from 31 providers. DR DNASU; 3841; -. DR Ensembl; ENST00000356348.6; ENSP00000348704.1; ENSG00000196911.12. DR Ensembl; ENST00000368564.7; ENSP00000357552.1; ENSG00000196911.12. DR GeneID; 3841; -. DR KEGG; hsa:3841; -. DR MANE-Select; ENST00000368564.7; ENSP00000357552.1; NM_001366306.2; NP_001353235.1. DR UCSC; uc003pxh.4; human. DR AGR; HGNC:6398; -. DR CTD; 3841; -. DR DisGeNET; 3841; -. DR GeneCards; KPNA5; -. DR HGNC; HGNC:6398; KPNA5. DR HPA; ENSG00000196911; Tissue enhanced (testis). DR MIM; 604545; gene. DR neXtProt; NX_O15131; -. DR OpenTargets; ENSG00000196911; -. DR PharmGKB; PA30189; -. DR VEuPathDB; HostDB:ENSG00000196911; -. DR eggNOG; KOG0166; Eukaryota. DR GeneTree; ENSGT01050000244950; -. DR HOGENOM; CLU_018084_6_0_1; -. DR InParanoid; O15131; -. DR OMA; NWSTISV; -. DR OrthoDB; 916229at2759; -. DR PhylomeDB; O15131; -. DR TreeFam; TF354205; -. DR PathwayCommons; O15131; -. DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism. DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways. DR SignaLink; O15131; -. DR BioGRID-ORCS; 3841; 14 hits in 1162 CRISPR screens. DR ChiTaRS; KPNA5; human. DR GeneWiki; KPNA5; -. DR GenomeRNAi; 3841; -. DR Pharos; O15131; Tbio. DR PRO; PR:O15131; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O15131; Protein. DR Bgee; ENSG00000196911; Expressed in calcaneal tendon and 193 other cell types or tissues. DR ExpressionAtlas; O15131; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central. DR GO; GO:0006606; P:protein import into nucleus; ISS:ComplexPortal. DR Gene3D; 1.20.5.690; Importin-alpha, importin-beta-binding domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR032413; Arm_3. DR InterPro; IPR000225; Armadillo. DR InterPro; IPR002652; Importin-a_IBB. DR InterPro; IPR036975; Importin-a_IBB_sf. DR InterPro; IPR024931; Importin_alpha. DR PANTHER; PTHR23316; IMPORTIN ALPHA; 1. DR PANTHER; PTHR23316:SF10; IMPORTIN SUBUNIT ALPHA-6; 1. DR Pfam; PF00514; Arm; 8. DR Pfam; PF16186; Arm_3; 1. DR Pfam; PF01749; IBB; 1. DR PIRSF; PIRSF005673; Importin_alpha; 1. DR SMART; SM00185; ARM; 8. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50176; ARM_REPEAT; 2. DR PROSITE; PS51214; IBB; 1. DR Genevisible; O15131; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Host-virus interaction; Protein transport; KW Reference proteome; Repeat; Transport. FT CHAIN 1..539 FT /note="Importin subunit alpha-6" FT /id="PRO_0000120728" FT DOMAIN 1..60 FT /note="IBB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561" FT REPEAT 76..116 FT /note="ARM 1; truncated" FT REPEAT 117..157 FT /note="ARM 2" FT /evidence="ECO:0000255" FT REPEAT 160..199 FT /note="ARM 3" FT /evidence="ECO:0000255" FT REPEAT 202..242 FT /note="ARM 4" FT /evidence="ECO:0000255" FT REPEAT 245..284 FT /note="ARM 5" FT /evidence="ECO:0000255" FT REPEAT 287..326 FT /note="ARM 6" FT /evidence="ECO:0000255" FT REPEAT 329..368 FT /note="ARM 7" FT /evidence="ECO:0000255" FT REPEAT 371..410 FT /note="ARM 8" FT /evidence="ECO:0000255" FT REPEAT 414..453 FT /note="ARM 9" FT /evidence="ECO:0000255" FT REPEAT 460..505 FT /note="ARM 10; atypical" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 150..242 FT /note="NLS binding site (major)" FT /evidence="ECO:0000250" FT REGION 319..407 FT /note="NLS binding site (minor)" FT /evidence="ECO:0000250" FT MOTIF 45..54 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT COMPBIAS 22..40 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 48 FT /note="F -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036245" FT VARIANT 319 FT /note="R -> S (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036246" FT CONFLICT 70 FT /note="P -> S (in Ref. 5; AAC51868)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="E -> G (in Ref. 5; AAC51868)" FT /evidence="ECO:0000305" FT HELIX 342..347 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 353..367 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 371..379 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 383..392 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 395..411 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 414..423 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 426..431 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 438..460 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 468..475 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 478..485 FT /evidence="ECO:0007829|PDB:4U2X" FT HELIX 491..504 FT /evidence="ECO:0007829|PDB:4U2X" SQ SEQUENCE 539 AA; 60666 MW; 6A2B71FEEA7E1B1F CRC64; MDAMASPGKD NYRMKSYKNK ALNPQEMRRR REEEGIQLRK QKREEQLFKR RNVYLPRNDE SMLESPIQDP DISSTVPIPE EEVVTTDMVQ MIFSNNADQQ LTATQKFRKL LSKEPNPPID QVIQKPGVVQ RFVKFLERNE NCTLQFEAAW ALTNIASGTF LHTKVVIETG AVPIFIKLLN SEHEDVQEQA VWALGNIAGD NAECRDFVLN CEILPPLLEL LTNSNRLTTT RNAVWALSNL CRGKNPPPNF SKVSPCLNVL SRLLFSSDPD VLADVCWALS YLSDGPNDKI QAVIDSGVCR RLVELLMHND YKVVSPALRA VGNIVTGDDI QTQVILNCSA LPCLLHLLSS PKESIRKEAC WTVSNITAGN RAQIQAVIDA NIFPVLIEIL QKAEFRTRKE AAWAITNATS GGTPEQIRYL VALGCIKPLC DLLTVMDSKI VQVALNGLEN ILRLGEQESK QNGIGINPYC ALIEEAYGLD KIEFLQSHEN QEIYQKAFDL IEHYFGVEED DPSIVPQVDE NQQQFIFQQQ EAPMDGFQL //