XPO1_YEAST
ID XPO1_YEAST Reviewed; 1084 AA.
AC P30822; D6VV01;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Exportin-1;
DE AltName: Full=Chromosome region maintenance protein 1;
DE AltName: Full=Karyopherin-124;
GN Name=CRM1; Synonyms=KAP124, XPO1; OrderedLocusNames=YGR218W;
GN ORFNames=G8514;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1448080; DOI=10.1128/mcb.12.12.5474-5484.1992;
RA Toda T., Shimanuki M., Saka Y., Yamano H., Adachi Y., Shirakawa M.,
RA Kyogoku Y., Yanagida M.;
RT "Fission yeast pap1-dependent transcription is negatively regulated by an
RT essential nuclear protein, crm1.";
RL Mol. Cell. Biol. 12:5474-5484(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9323132; DOI=10.1016/s0092-8674(00)80370-0;
RA Stade K., Ford C.S., Guthrie C., Weis K.;
RT "Exportin 1 (Crm1p) is an essential nuclear export factor.";
RL Cell 90:1041-1050(1997).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP INTERACTION WITH PAB1.
RX PubMed=15769879; DOI=10.1261/rna.7291205;
RA Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K.;
RT "Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the
RT cytoplasm and functions in mRNA export.";
RL RNA 11:517-531(2005).
RN [9]
RP INTERACTION WITH PRP40.
RX PubMed=15020406; DOI=10.1534/genetics.166.1.53;
RA Murphy M.W., Olson B.L., Siliciano P.G.;
RT "The yeast splicing factor Prp40p contains functional leucine-rich nuclear
RT export signals that are essential for splicing.";
RL Genetics 166:53-65(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1080, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Receptor for the leucine-rich nuclear export signal (NES).
CC -!- SUBUNIT: Interacts with GSP1/GSP2, polyadenylate-binding protein PAB1
CC and PRP40. {ECO:0000269|PubMed:15020406, ECO:0000269|PubMed:15769879}.
CC -!- INTERACTION:
CC P30822; P21192: ACE2; NbExp=3; IntAct=EBI-20589, EBI-2073;
CC P30822; P61925: PKIA; Xeno; NbExp=17; IntAct=EBI-20589, EBI-2682139;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:14562095}. Note=Localized in the
CC nucleus and at its periphery.
CC -!- MISCELLANEOUS: Present with 7080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
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DR EMBL; D13039; BAA02371.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61166.1; -; Genomic_DNA.
DR EMBL; Z73003; CAA97246.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08312.1; -; Genomic_DNA.
DR PIR; S57681; S57681.
DR RefSeq; NP_011734.3; NM_001181347.3.
DR PDB; 3M1I; X-ray; 2.00 A; C=1-1084.
DR PDB; 3VYC; X-ray; 2.10 A; A=1-1084.
DR PDB; 3WYF; X-ray; 2.22 A; C/F=1-1084.
DR PDB; 3WYG; X-ray; 2.15 A; C=1-1084.
DR PDB; 4GMX; X-ray; 2.10 A; C=1-1058.
DR PDB; 4GPT; X-ray; 2.22 A; C=1-1058.
DR PDB; 4HAT; X-ray; 1.78 A; C=1-1058.
DR PDB; 4HAU; X-ray; 2.00 A; C=1-1058.
DR PDB; 4HAV; X-ray; 2.00 A; C=1-1058.
DR PDB; 4HAW; X-ray; 1.90 A; C=1-1058.
DR PDB; 4HAX; X-ray; 2.28 A; C=1-1058.
DR PDB; 4HAY; X-ray; 2.30 A; C=1-1058.
DR PDB; 4HAZ; X-ray; 1.90 A; C=1-1058.
DR PDB; 4HB0; X-ray; 2.20 A; C=1-1058.
DR PDB; 4HB2; X-ray; 1.80 A; C=1-1058.
DR PDB; 4HB3; X-ray; 2.80 A; C=1-1058.
DR PDB; 4HB4; X-ray; 2.05 A; C=1-1058.
DR PDB; 5DH9; X-ray; 2.55 A; C=1-1058.
DR PDB; 5DHA; X-ray; 2.95 A; C=1-1058.
DR PDB; 5DHF; X-ray; 2.29 A; C=1-1058.
DR PDB; 5DI9; X-ray; 2.28 A; C=1-1058.
DR PDB; 5DIF; X-ray; 2.09 A; C=1-1058.
DR PDB; 5JLJ; X-ray; 2.50 A; C=1-1058.
DR PDB; 5UWH; X-ray; 2.26 A; C=1-1058.
DR PDB; 5UWI; X-ray; 2.14 A; C=1-1058.
DR PDB; 5UWJ; X-ray; 2.22 A; C=1-1058.
DR PDB; 5UWO; X-ray; 2.35 A; C=1-1058.
DR PDB; 5UWP; X-ray; 2.05 A; C=1-1058.
DR PDB; 5UWQ; X-ray; 2.28 A; C=1-1058.
DR PDB; 5UWR; X-ray; 2.24 A; C=1-1058.
DR PDB; 5UWS; X-ray; 2.40 A; C=1-1058.
DR PDB; 5UWT; X-ray; 2.34 A; C=1-1058.
DR PDB; 5UWU; X-ray; 2.24 A; C=1-1058.
DR PDB; 5UWW; X-ray; 2.15 A; C=1-1058.
DR PDB; 5XOJ; X-ray; 2.20 A; C=1-1084.
DR PDB; 5YRO; X-ray; 2.40 A; C=1-1058.
DR PDB; 5YST; X-ray; 2.04 A; C=1-1052.
DR PDB; 5YSU; X-ray; 2.30 A; C=1-1055.
DR PDB; 5YTB; X-ray; 2.30 A; C=1-1052.
DR PDB; 5ZPU; X-ray; 2.60 A; C=1-1058.
DR PDB; 6A38; X-ray; 2.69 A; C=1-1058.
DR PDB; 6A3A; X-ray; 2.30 A; C=1-1058.
DR PDB; 6A3B; X-ray; 2.51 A; C=1-1058.
DR PDB; 6A3C; X-ray; 2.35 A; C=1-1058.
DR PDB; 6A3E; X-ray; 2.70 A; C=1-1058.
DR PDB; 6CIT; X-ray; 2.03 A; C=1-1058.
DR PDB; 6KFT; X-ray; 2.51 A; C=1-1058.
DR PDB; 6LQ9; X-ray; 2.50 A; C=1-1058.
DR PDB; 6M60; X-ray; 2.17 A; C=1-1058.
DR PDB; 6M6X; X-ray; 2.88 A; C=1-1058.
DR PDB; 6X2M; X-ray; 2.35 A; C=1-1058.
DR PDB; 6X2O; X-ray; 2.55 A; C=1-1058.
DR PDB; 6X2P; X-ray; 2.40 A; C=1-1058.
DR PDB; 6X2R; X-ray; 2.30 A; C=1-1058.
DR PDB; 6X2S; X-ray; 2.50 A; C=1-1058.
DR PDB; 6X2U; X-ray; 2.20 A; C=1-1058.
DR PDB; 6X2V; X-ray; 2.82 A; C=1-1058.
DR PDB; 6X2W; X-ray; 3.00 A; C=1-1058.
DR PDB; 6X2X; X-ray; 2.46 A; C=1-1058.
DR PDB; 6X2Y; X-ray; 2.30 A; C=1-1058.
DR PDB; 6XJP; X-ray; 2.80 A; C=1-1058.
DR PDB; 6XJR; X-ray; 1.94 A; C=1-1058.
DR PDB; 6XJS; X-ray; 1.94 A; C=1-1058.
DR PDB; 6XJT; X-ray; 2.41 A; C=1-1058.
DR PDB; 6XJU; X-ray; 2.19 A; C=1-1058.
DR PDB; 7CND; X-ray; 1.80 A; C=1-1058.
DR PDB; 7DBG; X-ray; 2.06 A; C=1-1058.
DR PDB; 7L5E; X-ray; 1.94 A; C=1-1058.
DR PDBsum; 3M1I; -.
DR PDBsum; 3VYC; -.
DR PDBsum; 3WYF; -.
DR PDBsum; 3WYG; -.
DR PDBsum; 4GMX; -.
DR PDBsum; 4GPT; -.
DR PDBsum; 4HAT; -.
DR PDBsum; 4HAU; -.
DR PDBsum; 4HAV; -.
DR PDBsum; 4HAW; -.
DR PDBsum; 4HAX; -.
DR PDBsum; 4HAY; -.
DR PDBsum; 4HAZ; -.
DR PDBsum; 4HB0; -.
DR PDBsum; 4HB2; -.
DR PDBsum; 4HB3; -.
DR PDBsum; 4HB4; -.
DR PDBsum; 5DH9; -.
DR PDBsum; 5DHA; -.
DR PDBsum; 5DHF; -.
DR PDBsum; 5DI9; -.
DR PDBsum; 5DIF; -.
DR PDBsum; 5JLJ; -.
DR PDBsum; 5UWH; -.
DR PDBsum; 5UWI; -.
DR PDBsum; 5UWJ; -.
DR PDBsum; 5UWO; -.
DR PDBsum; 5UWP; -.
DR PDBsum; 5UWQ; -.
DR PDBsum; 5UWR; -.
DR PDBsum; 5UWS; -.
DR PDBsum; 5UWT; -.
DR PDBsum; 5UWU; -.
DR PDBsum; 5UWW; -.
DR PDBsum; 5XOJ; -.
DR PDBsum; 5YRO; -.
DR PDBsum; 5YST; -.
DR PDBsum; 5YSU; -.
DR PDBsum; 5YTB; -.
DR PDBsum; 5ZPU; -.
DR PDBsum; 6A38; -.
DR PDBsum; 6A3A; -.
DR PDBsum; 6A3B; -.
DR PDBsum; 6A3C; -.
DR PDBsum; 6A3E; -.
DR PDBsum; 6CIT; -.
DR PDBsum; 6KFT; -.
DR PDBsum; 6LQ9; -.
DR PDBsum; 6M60; -.
DR PDBsum; 6M6X; -.
DR PDBsum; 6X2M; -.
DR PDBsum; 6X2O; -.
DR PDBsum; 6X2P; -.
DR PDBsum; 6X2R; -.
DR PDBsum; 6X2S; -.
DR PDBsum; 6X2U; -.
DR PDBsum; 6X2V; -.
DR PDBsum; 6X2W; -.
DR PDBsum; 6X2X; -.
DR PDBsum; 6X2Y; -.
DR PDBsum; 6XJP; -.
DR PDBsum; 6XJR; -.
DR PDBsum; 6XJS; -.
DR PDBsum; 6XJT; -.
DR PDBsum; 6XJU; -.
DR PDBsum; 7CND; -.
DR PDBsum; 7DBG; -.
DR PDBsum; 7L5E; -.
DR AlphaFoldDB; P30822; -.
DR SMR; P30822; -.
DR BioGRID; 33472; 994.
DR DIP; DIP-2244N; -.
DR IntAct; P30822; 747.
DR MINT; P30822; -.
DR STRING; 4932.YGR218W; -.
DR ChEMBL; CHEMBL4630873; -.
DR MoonDB; P30822; Predicted.
DR iPTMnet; P30822; -.
DR MaxQB; P30822; -.
DR PaxDb; P30822; -.
DR PRIDE; P30822; -.
DR EnsemblFungi; YGR218W_mRNA; YGR218W; YGR218W.
DR GeneID; 853133; -.
DR KEGG; sce:YGR218W; -.
DR SGD; S000003450; CRM1.
DR VEuPathDB; FungiDB:YGR218W; -.
DR eggNOG; KOG2020; Eukaryota.
DR GeneTree; ENSGT00940000153408; -.
DR HOGENOM; CLU_011906_0_0_1; -.
DR InParanoid; P30822; -.
DR OMA; HNINTLC; -.
DR BioCyc; YEAST:G3O-30900-MON; -.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR EvolutionaryTrace; P30822; -.
DR PRO; PR:P30822; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P30822; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0005049; F:nuclear export signal receptor activity; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:SGD.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:SGD.
DR GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0051168; P:nuclear export; IMP:SGD.
DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR GO; GO:0034501; P:protein localization to kinetochore; IGI:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR IDEAL; IID50169; -.
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; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1084
FT /note="Exportin-1"
FT /id="PRO_0000204710"
FT DOMAIN 34..100
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6XJR"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 176..203
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4HB2"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 269..289
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 308..326
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 356..373
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 417..420
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:5YTB"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 462..478
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 480..495
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:7CND"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 521..541
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 545..560
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 570..583
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 589..606
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:5YRO"
FT HELIX 621..627
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 629..633
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:6X2O"
FT HELIX 638..652
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 658..668
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 670..685
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 693..713
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 718..746
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 748..752
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 754..776
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 780..786
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 788..801
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 809..822
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 827..845
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 849..852
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 853..869
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 872..875
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 879..893
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 898..918
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 922..944
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 945..947
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 949..951
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 952..967
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 978..980
FT /evidence="ECO:0007829|PDB:4HB2"
FT HELIX 987..1002
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 1008..1020
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 1021..1023
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 1025..1038
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 1041..1043
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 1046..1050
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 1051..1054
FT /evidence="ECO:0007829|PDB:3WYG"
FT TURN 1055..1057
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 1079..1081
FT /evidence="ECO:0007829|PDB:3VYC"
SQ SEQUENCE 1084 AA; 124104 MW; A81833C7F60F5202 CRC64;
MEGILDFSND LDIALLDQVV STFYQGSGVQ QKQAQEILTK FQDNPDAWQK ADQILQFSTN
PQSKFIALSI LDKLITRKWK LLPNDHRIGI RNFVVGMIIS MCQDDEVFKT QKNLINKSDL
TLVQILKQEW PQNWPEFIPE LIGSSSSSVN VCENNMIVLK LLSEEVFDFS AEQMTQAKAL
HLKNSMSKEF EQIFKLCFQV LEQGSSSSLI VATLESLLRY LHWIPYRYIY ETNILELLST
KFMTSPDTRA ITLKCLTEVS NLKIPQDNDL IKRQTVLFFQ NTLQQIATSV MPVTADLKAT
YANANGNDQS FLQDLAMFLT TYLARNRALL ESDESLRELL LNAHQYLIQL SKIEERELFK
TTLDYWHNLV ADLFYEVQRL PATEMSPLIQ LSVGSQAIST GSGALNPEYM KRFPLKKHIY
EEICSQLRLV IIENMVRPEE VLVVENDEGE IVREFVKESD TIQLYKSERE VLVYLTHLNV
IDTEEIMISK LARQIDGSEW SWHNINTLSW AIGSISGTMS EDTEKRFVVT VIKDLLDLTV
KKRGKDNKAV VASDIMYVVG QYPRFLKAHW NFLRTVILKL FEFMHETHEG VQDMACDTFI
KIVQKCKYHF VIQQPRESEP FIQTIIRDIQ KTTADLQPQQ VHTFYKACGI IISEERSVAE
RNRLLSDLMQ LPNMAWDTIV EQSTANPTLL LDSETVKIIA NIIKTNVAVC TSMGADFYPQ
LGHIYYNMLQ LYRAVSSMIS AQVAAEGLIA TKTPKVRGLR TIKKEILKLV ETYISKARNL
DDVVKVLVEP LLNAVLEDYM NNVPDARDAE VLNCMTTVVE KVGHMIPQGV ILILQSVFEC
TLDMINKDFT EYPEHRVEFY KLLKVINEKS FAAFLELPPA AFKLFVDAIC WAFKHNNRDV
EVNGLQIALD LVKNIERMGN VPFANEFHKN YFFIFVSETF FVLTDSDHKS GFSKQALLLM
KLISLVYDNK ISVPLYQEAE VPQGTSNQVY LSQYLANMLS NAFPHLTSEQ IASFLSALTK
QYKDLVVFKG TLRDFLVQIK EVGGDPTDYL FAEDKENALM EQNRLEREKA AKIGGLLKPS
ELDD
