IPO13_HUMAN
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 03-AUG-2022, entry version 174.
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};
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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; 112.
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; O94829; -.
DR PeptideAtlas; O94829; -.
DR PRIDE; O94829; -.
DR ProteomicsDB; 50474; -.
DR Antibodypedia; 32405; 119 antibodies from 20 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 CTD; 9670; -.
DR DisGeNET; 9670; -.
DR GeneCards; IPO13; -.
DR HGNC; HGNC:16853; IPO13.
DR HPA; ENSG00000117408; Tissue enhanced (brain, skeletal muscle).
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; DTFMYCY; -.
DR OrthoDB; 1032285at2759; -.
DR PhylomeDB; O94829; -.
DR TreeFam; TF314539; -.
DR PathwayCommons; O94829; -.
DR SignaLink; O94829; -.
DR BioGRID-ORCS; 9670; 717 hits in 1092 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 199 other tissues.
DR ExpressionAtlas; O94829; baseline and differential.
DR Genevisible; O94829; HS.
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; -; 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 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; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
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
