IMA6_HUMAN
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 03-AUG-2022, entry version 195.
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=4; IntAct=EBI-540602, EBI-762428;
CC O15131; P46527: CDKN1B; NbExp=6; IntAct=EBI-540602, EBI-519280;
CC O15131; Q9UKX7: NUP50; NbExp=4; IntAct=EBI-540602, EBI-2371082;
CC O15131; Q6IQ16: SPOPL; NbExp=4; IntAct=EBI-540602, EBI-2822161;
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};
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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 BioGRID; 110039; 91.
DR ComplexPortal; CPX-1063; Importin complex, KPNA5 variant.
DR DIP; DIP-33405N; -.
DR ELM; O15131; -.
DR IntAct; O15131; 29.
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; O15131; -.
DR PeptideAtlas; O15131; -.
DR PRIDE; O15131; -.
DR ProteomicsDB; 48467; -.
DR Antibodypedia; 32522; 254 antibodies from 31 providers.
DR DNASU; 3841; -.
DR Ensembl; ENST00000356348.6; ENSP00000348704.1; ENSG00000196911.11.
DR Ensembl; ENST00000368564.7; ENSP00000357552.1; ENSG00000196911.11.
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 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 OrthoDB; 1111872at2759; -.
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 1083 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 191 other tissues.
DR ExpressionAtlas; O15131; baseline and differential.
DR Genevisible; O15131; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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 Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 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 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; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51214; IBB; 1.
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
