XPO1_MOUSE
ID XPO1_MOUSE Reviewed; 1071 AA.
AC Q6P5F9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Exportin-1;
DE Short=Exp1;
DE AltName: Full=Chromosome region maintenance 1 protein homolog;
GN Name=Xpo1; Synonyms=Crm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH NCBP1; NCBP2; RAN; PHAX AND
RP M7G-CAPPED RNA.
RX PubMed=10786834; DOI=10.1016/s0092-8674(00)80829-6;
RA Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.;
RT "PHAX, a mediator of U snRNA nuclear export whose activity is regulated by
RT phosphorylation.";
RL Cell 101:187-198(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH DTNBP1, AND FUNCTION.
RX PubMed=20921223; DOI=10.1074/jbc.m110.107912;
RA Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.;
RT "Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related
RT protein, regulates synapsin I expression.";
RL J. Biol. Chem. 285:38630-38640(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Mediates the nuclear export of cellular proteins (cargos)
CC bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the
CC nucleus, in association with RANBP3, binds cooperatively to the NES on
CC its target protein and to the GTPase Ran in its active GTP-bound form.
CC Docking of this complex to the nuclear pore complex (NPC) is mediated
CC through binding to nucleoporins. Upon transit of a nuclear export
CC complex into the cytoplasm, disassembling of the complex and hydrolysis
CC of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively)
CC cause release of the cargo from the export receptor. The directionality
CC of nuclear export is thought to be conferred by an asymmetric
CC distribution of the GTP- and GDP-bound forms of Ran between the
CC cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal
CC bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:20921223}.
CC -!- SUBUNIT: Found in a U snRNA export complex with PHAX/RNUXA,
CC NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA
CC (PubMed:10786834). Component of a nuclear export receptor complex
CC composed of KPNB1, RAN, SNUPN and XPO1. Found in a trimeric export
CC complex with SNUPN, RAN and XPO1. Found in a nuclear export complex
CC with RANBP3 and RAN. Found in a 60S ribosomal subunit export complex
CC with NMD3, RAN, XPO1. Interacts with DDX3X, NMD3, NUP42, NUP88, NUP214,
CC RANBP3 and TERT. Interacts with NEMF (via its N-terminus). Interacts
CC with the monomeric form of BIRC5/survivin deacetylated at 'Lys-129'.
CC Interacts with SERTAD2; the interaction translocates SERTAD2 out of the
CC nucleus. Interacts with ATF2. Interacts with SLC35G1 and STIM1.
CC Interacts with DCAF8 (By similarity). Interacts with DTNBP1 and the
CC interaction translocates DTNBP1 out of the nucleus (PubMed:20921223).
CC Interacts with CPEB3 (By similarity). Interacts with HAX1 (By
CC similarity). Interacts with BOK; translocates to the cytoplasm (By
CC similarity). Interacts with HSP90AB1 (By similarity).
CC {ECO:0000250|UniProtKB:O14980, ECO:0000269|PubMed:10786834,
CC ECO:0000269|PubMed:20921223}.
CC -!- INTERACTION:
CC Q6P5F9; Q6GNU1: arpc1b-b; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-11607516;
CC Q6P5F9; Q3B8L5: LOC495502; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-11608794;
CC Q6P5F9; Q00987: MDM2; Xeno; NbExp=4; IntAct=EBI-2550236, EBI-389668;
CC Q6P5F9; P0DJZ2: NS2; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-9673535;
CC Q6P5F9; P61925: PKIA; Xeno; NbExp=4; IntAct=EBI-2550236, EBI-2682139;
CC Q6P5F9; P62826: RAN; Xeno; NbExp=3; IntAct=EBI-2550236, EBI-286642;
CC Q6P5F9; B7ZR20: septin2.L; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-11608460;
CC Q6P5F9; O95149: SNUPN; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-714033;
CC Q6P5F9; Q91855: SUP35; Xeno; NbExp=2; IntAct=EBI-2550236, EBI-11606693;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=Located in the nucleoplasm, Cajal bodies and
CC nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; BC062912; AAH62912.1; -; mRNA.
DR CCDS; CCDS24475.1; -.
DR RefSeq; NP_001030303.1; NM_001035226.1.
DR RefSeq; NP_598775.2; NM_134014.3.
DR RefSeq; XP_006514493.1; XM_006514430.2.
DR PDB; 3GJX; X-ray; 2.50 A; A/D=1-1071.
DR PDB; 3NBY; X-ray; 3.42 A; A/D=1-1071.
DR PDB; 3NBZ; X-ray; 2.80 A; A/D=1-1071.
DR PDB; 3NC0; X-ray; 2.90 A; A/D=1-1071.
DR PDB; 3NC1; X-ray; 3.35 A; A=1-1071.
DR PDBsum; 3GJX; -.
DR PDBsum; 3NBY; -.
DR PDBsum; 3NBZ; -.
DR PDBsum; 3NC0; -.
DR PDBsum; 3NC1; -.
DR AlphaFoldDB; Q6P5F9; -.
DR SASBDB; Q6P5F9; -.
DR SMR; Q6P5F9; -.
DR BioGRID; 222117; 29.
DR DIP; DIP-48612N; -.
DR IntAct; Q6P5F9; 1784.
DR STRING; 10090.ENSMUSP00000099933; -.
DR iPTMnet; Q6P5F9; -.
DR PhosphoSitePlus; Q6P5F9; -.
DR SwissPalm; Q6P5F9; -.
DR EPD; Q6P5F9; -.
DR jPOST; Q6P5F9; -.
DR MaxQB; Q6P5F9; -.
DR PaxDb; Q6P5F9; -.
DR PeptideAtlas; Q6P5F9; -.
DR PRIDE; Q6P5F9; -.
DR ProteomicsDB; 300006; -.
DR Antibodypedia; 4124; 376 antibodies from 35 providers.
DR DNASU; 103573; -.
DR Ensembl; ENSMUST00000020538; ENSMUSP00000020538; ENSMUSG00000020290.
DR Ensembl; ENSMUST00000102869; ENSMUSP00000099933; ENSMUSG00000020290.
DR Ensembl; ENSMUST00000102870; ENSMUSP00000099934; ENSMUSG00000020290.
DR Ensembl; ENSMUST00000109551; ENSMUSP00000105178; ENSMUSG00000020290.
DR GeneID; 103573; -.
DR KEGG; mmu:103573; -.
DR UCSC; uc007iet.1; mouse.
DR CTD; 7514; -.
DR MGI; MGI:2144013; Xpo1.
DR VEuPathDB; HostDB:ENSMUSG00000020290; -.
DR eggNOG; KOG2020; Eukaryota.
DR GeneTree; ENSGT00940000153408; -.
DR HOGENOM; CLU_011906_0_0_1; -.
DR InParanoid; Q6P5F9; -.
DR OMA; HNINTLC; -.
DR OrthoDB; 132850at2759; -.
DR PhylomeDB; Q6P5F9; -.
DR TreeFam; TF105695; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-9707616; Heme signaling.
DR BioGRID-ORCS; 103573; 29 hits in 68 CRISPR screens.
DR ChiTaRS; Xpo1; mouse.
DR EvolutionaryTrace; Q6P5F9; -.
DR PRO; PR:Q6P5F9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6P5F9; protein.
DR Bgee; ENSMUSG00000020290; Expressed in metanephric loop of Henle and 274 other tissues.
DR ExpressionAtlas; Q6P5F9; baseline and differential.
DR Genevisible; Q6P5F9; MM.
DR GO; GO:0005642; C:annulate lamellae; ISO:MGI.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IDA:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISO:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0042176; P:regulation of protein catabolic process; IMP:MGI.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IMP:MGI.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:MGI.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; ISO:MGI.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; ISO:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID50151; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR041123; CRM1_repeat.
DR InterPro; IPR041235; Exp1_repeat_2.
DR InterPro; IPR013598; Exportin-1/Importin-b-like.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR045065; XPO1/5.
DR InterPro; IPR014877; XPO1_C_dom.
DR InterPro; IPR040485; XPO1_repeat_3.
DR PANTHER; PTHR11223; PTHR11223; 1.
DR Pfam; PF08767; CRM1_C; 1.
DR Pfam; PF18777; CRM1_repeat; 1.
DR Pfam; PF18784; CRM1_repeat_2; 1.
DR Pfam; PF18787; CRM1_repeat_3; 1.
DR Pfam; PF03810; IBN_N; 1.
DR Pfam; PF08389; Xpo1; 1.
DR SMART; SM01102; CRM1_C; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; mRNA transport; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; RNA-binding;
KW Transport.
FT CHAIN 1..1071
FT /note="Exportin-1"
FT /id="PRO_0000204706"
FT DOMAIN 46..112
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 217..240
FT /note="HEAT 1"
FT REPEAT 241..277
FT /note="HEAT 2"
FT REPEAT 354..472
FT /note="HEAT 3"
FT REPEAT 515..553
FT /note="HEAT 4"
FT REPEAT 560..597
FT /note="HEAT 5"
FT REPEAT 602..639
FT /note="HEAT 6"
FT REPEAT 775..813
FT /note="HEAT 7"
FT REPEAT 885..916
FT /note="HEAT 8"
FT REPEAT 917..954
FT /note="HEAT 9"
FT REPEAT 1002..1039
FT /note="HEAT 10"
FT REGION 327..450
FT /note="Necessary for interaction with Ran and nuclear
FT export complex formation"
FT /evidence="ECO:0000250"
FT REGION 411..481
FT /note="Necessary for interaction with RANBP3"
FT /evidence="ECO:0000250"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 454
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80U96"
FT MOD_RES 693
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14980"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3NC1"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3NC1"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 219..232
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 258..273
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3NBY"
FT HELIX 304..309
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 315..339
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 344..357
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 363..383
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 449..467
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 469..484
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 510..530
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 534..550
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 552..557
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 559..572
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 580..594
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 610..615
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 618..622
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 627..641
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 647..657
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 659..674
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 676..680
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 682..702
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 707..735
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 737..740
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 743..763
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 769..775
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 778..783
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 785..790
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 799..811
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 819..834
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 838..840
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 842..858
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 860..862
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 863..865
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 868..882
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 887..904
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 908..930
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 936..938
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 939..953
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:3NC0"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 965..968
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 970..985
FT /evidence="ECO:0007829|PDB:3GJX"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:3NBY"
FT HELIX 991..1003
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 1004..1006
FT /evidence="ECO:0007829|PDB:3NC1"
FT HELIX 1008..1022
FT /evidence="ECO:0007829|PDB:3GJX"
FT TURN 1027..1029
FT /evidence="ECO:0007829|PDB:3GJX"
FT HELIX 1037..1052
FT /evidence="ECO:0007829|PDB:3GJX"
SQ SEQUENCE 1071 AA; 123093 MW; B451A19780024562 CRC64;
MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL THLKEHPDAW
TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE GIKKYVVGLI IKTSSDPTCV
EKEKVYIGKL NMILVQILKQ EWPKHWPTFI SDIVGASRTS ESLCQNNMVI LKLLSEEVFD
FSSGQITQVK AKHLKDSMCN EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY
IFETKLISTL IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFETLFTLT MMQLKQMLPL
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHGQLLEKR LNLREALMEA LHYMLLVSEV
EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF DIPPRRQLYL TVLSKVRLLM
VSRMAKPEEV LVVENDQGEV VREFMKDTDS INLYKNMRET LVYLTHLDYV DTEIIMTKKL
QNQVNGTEWS WKNLNTLCWA IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII
ASNIMYIVGQ YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ EHLIEKYMLL
PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK AVGHPFVIQL GRIYLDMLNV
YKCLSENISA AIQANGEMVT KQPLIRSMRT VKRETLKLIS GWVSRSNDPQ MVAENFVPPL
LDAVLIDYQR NVPAAREPEV LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE
YPEHRTNFFL LLQAVNSHCF PAFLAIPPAQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF NLVEEGKIST
PLNPGNPVNN QMFIQDYVAN LLKSAFPHLQ DAQVKLFVTG LFSLNQDIPA FKEHLRDFLV
QIKEFAGEDT SDLFLEERET ALRQAQEEKH KLQMSVPGIL NPHEIPEEMC D
