UN93B_MOUSE
ID UN93B_MOUSE Reviewed; 598 AA.
AC Q8VCW4; O89077; Q3TNR9; Q710D2; Q8CIK1; Q8R3D0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein unc-93 homolog B1 {ECO:0000305};
DE Short=Unc-93B1;
GN Name=Unc93b1 {ECO:0000312|MGI:MGI:1859307}; Synonyms=Unc93b;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 264-315 (ISOFORM 1).
RC STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
RA Kollewe A.;
RT "Cloning and characterization of mammalian homologs of unc-93 from
RT Caenorhabditis elegans, a protein relevant for muscle contraction.";
RL Thesis (2001), University of Hannover, Germany.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 317-434 (ISOFORM 1), AND INDUCTION.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [5]
RP FUNCTION, MUTAGENESIS OF HIS-412, AND SUBCELLULAR LOCATION.
RX PubMed=16415873; DOI=10.1038/ni1297;
RA Tabeta K., Hoebe K., Janssen E.M., Du X., Georgel P., Crozat K., Mudd S.,
RA Mann N., Sovath S., Goode J., Shamel L., Herskovits A.A., Portnoy D.A.,
RA Cooke M., Tarantino L.M., Wiltshire T., Steinberg B.E., Grinstein S.,
RA Beutler B.;
RT "The Unc93b1 mutation 3d disrupts exogenous antigen presentation and
RT signaling via Toll-like receptors 3, 7 and 9.";
RL Nat. Immunol. 7:156-164(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND INTERACTION WITH TLR3;
RP TLR7; TLR9 AND TLR13.
RX PubMed=17452530; DOI=10.1083/jcb.200612056;
RA Brinkmann M.M., Spooner E., Hoebe K., Beutler B., Ploegh H.L., Kim Y.M.;
RT "The interaction between the ER membrane protein UNC93B and TLR3, 7, and 9
RT is crucial for TLR signaling.";
RL J. Cell Biol. 177:265-275(2007).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18305481; DOI=10.1038/nature06726;
RA Kim Y.M., Brinkmann M.M., Paquet M.E., Ploegh H.L.;
RT "UNC93B1 delivers nucleotide-sensing toll-like receptors to
RT endolysosomes.";
RL Nature 452:234-238(2008).
RN [8]
RP MUTAGENESIS OF ASP-34, AND INTERACTION WITH TLR7; TLR8 AND TLR13.
RX PubMed=19451267; DOI=10.1084/jem.20082316;
RA Fukui R., Saitoh S., Matsumoto F., Kozuka-Hata H., Oyama M., Tabeta K.,
RA Beutler B., Miyake K.;
RT "Unc93B1 biases Toll-like receptor responses to nucleic acid in dendritic
RT cells toward DNA- but against RNA-sensing.";
RL J. Exp. Med. 206:1339-1350(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
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 [10] {ECO:0007744|PDB:7C77}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH TLR3,
RP INTERACTION WITH TLR3, AND MUTAGENESIS OF PHE-133; TRP-137; PHE-140;
RP ALA-147; LEU-148; SER-151; TYR-154; TRP-155; THR-160; ARG-281; SER-282;
RP ILE-286; PHE-297 AND MET-300.
RX PubMed=33432245; DOI=10.1038/s41594-020-00542-w;
RA Ishida H., Asami J., Zhang Z., Nishizawa T., Shigematsu H., Ohto U.,
RA Shimizu T.;
RT "Cryo-EM structures of Toll-like receptors in complex with UNC93B1.";
RL Nat. Struct. Mol. Biol. 28:173-180(2021).
CC -!- FUNCTION: Plays an important role in innate and adaptive immunity by
CC regulating nucleotide-sensing Toll-like receptor (TLR) signaling.
CC Required for the transport of a subset of TLRs (including TLR3, TLR7
CC and TLR9) from the endoplasmic reticulum to endolysosomes where they
CC can engage pathogen nucleotides and activate signaling cascades. May
CC play a role in autoreactive B-cells removal.
CC {ECO:0000269|PubMed:16415873, ECO:0000269|PubMed:17452530,
CC ECO:0000269|PubMed:18305481}.
CC -!- SUBUNIT: Interacts with TLR3, TLR5, TLR7, TLR8, TLR9 and TLR13
CC (probably via transmembrane domain). {ECO:0000269|PubMed:17452530,
CC ECO:0000269|PubMed:19451267, ECO:0000269|PubMed:33432245}.
CC -!- INTERACTION:
CC Q8VCW4; O96005: CLPTM1; Xeno; NbExp=2; IntAct=EBI-6116986, EBI-2873194;
CC Q8VCW4; P51617: IRAK1; Xeno; NbExp=2; IntAct=EBI-6116986, EBI-358664;
CC Q8VCW4; Q96N66: MBOAT7; Xeno; NbExp=2; IntAct=EBI-6116986, EBI-6116499;
CC Q8VCW4; O15260: SURF4; Xeno; NbExp=2; IntAct=EBI-6116986, EBI-1044848;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Endosome. Lysosome. Cytoplasmic vesicle, phagosome.
CC Note=Colocalizes with LAMP5 in large endosomal intracellular vesicles
CC (By similarity). Relocalizes from endoplasmic reticulum to endosome and
CC lysosome upon cell-stimulation with CpG dinucleotides. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VCW4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCW4-2; Sequence=VSP_014036;
CC -!- INDUCTION: Upon interleukin-4 treatment in B-cells.
CC {ECO:0000269|PubMed:9798653}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17452530}.
CC -!- SIMILARITY: Belongs to the unc-93 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25587.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK165060; BAE38019.1; -; mRNA.
DR EMBL; BC018388; AAH18388.1; -; mRNA.
DR EMBL; BC023731; AAH23731.1; -; mRNA.
DR EMBL; BC025587; AAH25587.1; ALT_INIT; mRNA.
DR EMBL; AJ422144; CAD19524.1; -; mRNA.
DR EMBL; U89424; AAC36530.1; -; mRNA.
DR CCDS; CCDS29404.2; -. [Q8VCW4-1]
DR RefSeq; NP_001154900.1; NM_001161428.1.
DR RefSeq; NP_062322.2; NM_019449.2.
DR PDB; 7C77; EM; 3.30 A; B=1-598.
DR PDBsum; 7C77; -.
DR AlphaFoldDB; Q8VCW4; -.
DR SMR; Q8VCW4; -.
DR BioGRID; 207660; 2.
DR IntAct; Q8VCW4; 27.
DR STRING; 10090.ENSMUSP00000124272; -.
DR GlyGen; Q8VCW4; 3 sites.
DR iPTMnet; Q8VCW4; -.
DR PhosphoSitePlus; Q8VCW4; -.
DR SwissPalm; Q8VCW4; -.
DR EPD; Q8VCW4; -.
DR MaxQB; Q8VCW4; -.
DR PaxDb; Q8VCW4; -.
DR PeptideAtlas; Q8VCW4; -.
DR PRIDE; Q8VCW4; -.
DR ProteomicsDB; 300092; -. [Q8VCW4-1]
DR ProteomicsDB; 300093; -. [Q8VCW4-2]
DR DNASU; 54445; -.
DR GeneID; 54445; -.
DR KEGG; mmu:54445; -.
DR UCSC; uc008fxt.1; mouse. [Q8VCW4-1]
DR CTD; 81622; -.
DR MGI; MGI:1859307; Unc93b1.
DR eggNOG; KOG3097; Eukaryota.
DR InParanoid; Q8VCW4; -.
DR OrthoDB; 394901at2759; -.
DR Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
DR BioGRID-ORCS; 54445; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Unc93b1; mouse.
DR PRO; PR:Q8VCW4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VCW4; protein.
DR GO; GO:0032009; C:early phagosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0002457; P:T cell antigen processing and presentation; IMP:MGI.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:MGI.
DR InterPro; IPR010291; Ion_channel_UNC-93.
DR InterPro; IPR043268; UNC93B1.
DR PANTHER; PTHR46744; PTHR46744; 1.
DR Pfam; PF05978; UNC-93; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Antiviral defense;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Immunity; Innate immunity; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..598
FT /note="Protein unc-93 homolog B1"
FT /id="PRO_0000190041"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1C4"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1C4"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014036"
FT MUTAGEN 34
FT /note="D->A: Increases the TLR7 response and decreases the
FT TLR9 response. Enhances interaction with TLR7, TLR8 and
FT TLR13 and TLR7 transport to endolysosomes in presence of
FT single-stranded RNA. Decreases affinity for TLR9 and its
FT transport to endolysosomes in presence of DNA."
FT /evidence="ECO:0000269|PubMed:19451267"
FT MUTAGEN 36
FT /note="L->A: Increases the TLR7 response and decreases the
FT TLR9 response."
FT MUTAGEN 133
FT /note="F->A,W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 137
FT /note="W->A: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 140
FT /note="F->A: Decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 140
FT /note="F->W: Increases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 147
FT /note="A->W: Decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 148
FT /note="L->A: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 148
FT /note="L->W: Increases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 151
FT /note="S->A,W: Strongly decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 154
FT /note="Y->A,W: Strongly decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 155
FT /note="W->A: Decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 160
FT /note="T->A,W: Decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 281
FT /note="R->A: Strongly decreases interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 281
FT /note="R->W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 282
FT /note="S->W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 286
FT /note="I->A,W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 297
FT /note="F->W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 300
FT /note="M->A,W: No effect on interaction with TLR3."
FT /evidence="ECO:0000269|PubMed:33432245"
FT MUTAGEN 412
FT /note="H->R: Loss of function in TLR signaling. Impaired in
FT its own transport from endoplasmic reticulum to endosome,
FT lysosome and phagosome. Loss of the interaction with TLR3,
FT TLR7, TLR9 and TLR13 and of the ability to transport them
FT to endolysosome."
FT /evidence="ECO:0000269|PubMed:16415873"
FT CONFLICT 325..326
FT /note="GN -> RS (in Ref. 4; AAC36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="F -> S (in Ref. 4; AAC36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="F -> L (in Ref. 4; AAC36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="I -> T (in Ref. 4; AAC36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..403
FT /note="RSV -> HSA (in Ref. 4; AAC36530)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="A -> T (in Ref. 2; AAH18388/AAH23731/AAH25587)"
FT /evidence="ECO:0000305"
FT HELIX 47..88
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 158..198
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 214..234
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 242..245
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 282..306
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 340..358
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 359..367
FT /evidence="ECO:0007829|PDB:7C77"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 375..394
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 404..418
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 433..460
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 464..487
FT /evidence="ECO:0007829|PDB:7C77"
FT HELIX 495..516
FT /evidence="ECO:0007829|PDB:7C77"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:7C77"
SQ SEQUENCE 598 AA; 66981 MW; E0E8AC1C3BBD9E10 CRC64;
MEVEPPLYPV AGAAGPQGDE DRHGVPDGPE APLDELVGAY PNYNEEEEER RYYRRKRLGV
VKNVLAASTG VTLTYGVYLG LLQMQLILHY DETYREVKYG NMGLPDIDSK MLMGINVTPI
AALLYTPVLI RFFGTKWMMF LAVGIYALFV STNYWERYYT LVPSAVALGM AIVPLWASMG
NYITRMSQKY YEYSHYKEQD EQGPQQRPPR GSHAPYLLVF QAIFYSFFHL SFACAQLPMI
YFLNNYLYDL NHTLINVQSC GTKSQGILNG FNKTVLRTLP RSKNLIVVES VLMAVAFLAM
LMVLGLCGAA YRPTEEIDLR SVGWGNIFQL PFKHVRDFRL RHLVPFFIYS GFEVLFACTG
FALGYGVCSM GLERLAYLLI AYSLGASASS VLGLLGLWLP RSVPLVAGAG LHLLLTLSLF
FWAPAPRVLQ HSWIFYFVAA LWGVGSALNK TGLSTLLGIL YEDKERQDFI FTIYHWWQAV
AIFVVYLGSS LPMKAKLAVL LVTLVAAAAS YLWMEQKLQQ GLVPRQPRIP KPQHKVRGYR
YLEEDNSDES DMEGEQGQGD CAEDEAPQAG PLGAEPAGPC RKPCPYEQAL GGDGPEEQ
