INAR1_MOUSE
ID INAR1_MOUSE Reviewed; 590 AA.
AC P33896; Q80UJ3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Interferon alpha/beta receptor 1;
DE Short=IFN-R-1;
DE Short=IFN-alpha/beta receptor 1;
DE AltName: Full=Type I interferon receptor 1;
DE Flags: Precursor;
GN Name=Ifnar1; Synonyms=Ifar, Ifnar;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1533935; DOI=10.1073/pnas.89.10.4774;
RA Uze G., Lutfalla G., Bandu M.T., Proudhon D., Mogensen K.E.;
RT "Behavior of a cloned murine interferon alpha/beta receptor expressed in
RT homospecific or heterospecific background.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4774-4778(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7958966; DOI=10.1016/0378-1119(94)90710-2;
RA Lutfalla G., Uze G.;
RT "Structure of the murine interferon alpha/beta receptor-encoding gene:
RT high-frequency rearrangements in the interferon-resistant L1210 cell
RT line.";
RL Gene 148:343-346(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 FUNCTION, INTERACTION WITH FBXW11, UBIQUITINATION, PHOSPHORYLATION AT
RP SER-526, MUTAGENESIS OF SER-526, AND SUBCELLULAR LOCATION.
RX PubMed=14532120; DOI=10.1093/emboj/cdg524;
RA Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y.;
RT "SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of
RT the interferon-alpha receptor.";
RL EMBO J. 22:5480-5490(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=18724932; DOI=10.1016/j.cell.2008.06.032;
RA Stetson D.B., Ko J.S., Heidmann T., Medzhitov R.;
RT "Trex1 prevents cell-intrinsic initiation of autoimmunity.";
RL Cell 134:587-598(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
RA Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S., Katlinski K.,
RA Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y., Greenberg R.A.;
RT "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
RT responses.";
RL Cell Rep. 5:180-193(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-429 IN COMPLEX WITH IFNB1,
RP DISULFIDE BONDS, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23872679; DOI=10.1038/ni.2667;
RA de Weerd N.A., Vivian J.P., Nguyen T.K., Mangan N.E., Gould J.A.,
RA Braniff S.J., Zaker-Tabrizi L., Fung K.Y., Forster S.C., Beddoe T.,
RA Reid H.H., Rossjohn J., Hertzog P.J.;
RT "Structural basis of a unique interferon-beta signaling axis mediated via
RT the receptor IFNAR1.";
RL Nat. Immunol. 14:901-907(2013).
CC -!- FUNCTION: Component of the receptor for type I interferons, including
CC interferons alpha, IFNB1 and IFNW1 (PubMed:1533935, PubMed:14532120,
CC PubMed:23872679). Functions in general as heterodimer with IFNAR2 (By
CC similarity). Type I interferon binding activates the JAK-STAT signaling
CC cascade, and triggers tyrosine phosphorylation of a number of proteins
CC including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-
CC subunits themselves (PubMed:14532120). Can form an active IFNB1
CC receptor by itself and activate a signaling cascade that does not
CC involve activation of the JAK-STAT pathway (PubMed:23872679).
CC Contributes to modulate the innate immune response to bacterial
CC lipopolysaccharide (PubMed:23872679). {ECO:0000250|UniProtKB:P17181,
CC ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935,
CC ECO:0000269|PubMed:23872679, ECO:0000269|PubMed:24075985}.
CC -!- SUBUNIT: Heterodimer with IFNAR2. Interacts (serine-phosphorylated
CC form) with FBXW11, the substrate recognition component of a SCF (SKP1-
CC CUL1-F-box protein) E3 ubiquitin-protein ligase complex
CC (PubMed:14532120). Interacts with SHMT2; this promotes interaction with
CC ABRAXAS2 and the BRISC complex (By similarity). Interacts with TYK2 (By
CC similarity). Interacts with TRIM10; this interaction prevents
CC association between IFNAR1 and TYK2 (By similarity).
CC {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14532120,
CC ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:24075985}; Single-pass
CC type I membrane protein {ECO:0000305}. Late endosome
CC {ECO:0000305|PubMed:14532120}. Lysosome {ECO:0000305|PubMed:14532120}.
CC Note=Interferon binding triggers internalization of the receptor from
CC the cell membrane into endosomes and then into lysosomes.
CC {ECO:0000305|PubMed:14532120, ECO:0000305|PubMed:24075985}.
CC -!- PTM: Ubiquitinated (PubMed:14532120). This leads to its internalization
CC and lysosomal degradation. The 'Lys-63'-linked ubiquitin chains are
CC cleaved off by the BRISC complex; this prevents receptor
CC internalization and degradation. Probable ubiquitination sites have
CC been identified in human, but are poorly conserved across species.
CC {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120}.
CC -!- PTM: Phosphorylated on serine residues in response to interferon
CC binding; this promotes interaction with FBXW11 and ubiquitination
CC (PubMed:14532120). Phosphorylated on tyrosine residues by TYK2 tyrosine
CC kinase. Phosphorylated on tyrosine residues in response to interferon
CC (By similarity). {ECO:0000250|UniProtKB:P17181,
CC ECO:0000269|PubMed:14532120}.
CC -!- DISRUPTION PHENOTYPE: Mice are protected from the lethal septic effects
CC of intraperitoneal LPS administration observed in wild-type mice
CC (PubMed:23872679). Double knockout with TREX1 does not show a visible
CC phenotype (PubMed:18724932). {ECO:0000269|PubMed:18724932,
CC ECO:0000269|PubMed:23872679}.
CC -!- MISCELLANEOUS: The interferon signaling pathway is not identical
CC between species. Thus, the interaction with STAT1 and STAT2 may not be
CC conserved in mouse; in human it requires phosphorylation at 'Tyr-466',
CC but the mouse protein has a Phe at the equivalent position. Likewise,
CC cysteine palmitoylation is required for the activation of STAT1 and
CC STAT2 in human, but the Cys is not conserved in mouse. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; M89641; AAA37890.1; -; mRNA.
DR EMBL; AK132431; BAE21165.1; -; mRNA.
DR EMBL; AK141630; BAE24775.1; -; mRNA.
DR EMBL; CH466602; EDL03825.1; -; Genomic_DNA.
DR EMBL; BC043935; AAH43935.1; -; mRNA.
DR EMBL; BC052429; AAH52429.1; -; mRNA.
DR CCDS; CCDS28326.1; -.
DR PIR; A45283; A45283.
DR RefSeq; NP_034638.2; NM_010508.2.
DR PDB; 3WCY; X-ray; 2.90 A; A=27-429.
DR PDBsum; 3WCY; -.
DR AlphaFoldDB; P33896; -.
DR SMR; P33896; -.
DR IntAct; P33896; 4.
DR STRING; 10090.ENSMUSP00000023689; -.
DR GlyGen; P33896; 8 sites.
DR iPTMnet; P33896; -.
DR PhosphoSitePlus; P33896; -.
DR MaxQB; P33896; -.
DR PaxDb; P33896; -.
DR PRIDE; P33896; -.
DR ProteomicsDB; 269404; -.
DR Antibodypedia; 3016; 812 antibodies from 45 providers.
DR DNASU; 15975; -.
DR Ensembl; ENSMUST00000023689; ENSMUSP00000023689; ENSMUSG00000022967.
DR Ensembl; ENSMUST00000117748; ENSMUSP00000112670; ENSMUSG00000022967.
DR GeneID; 15975; -.
DR KEGG; mmu:15975; -.
DR UCSC; uc007zxn.2; mouse.
DR CTD; 3454; -.
DR MGI; MGI:107658; Ifnar1.
DR VEuPathDB; HostDB:ENSMUSG00000022967; -.
DR eggNOG; ENOG502RISU; Eukaryota.
DR GeneTree; ENSGT00940000158406; -.
DR HOGENOM; CLU_035134_0_0_1; -.
DR InParanoid; P33896; -.
DR OMA; YCINTTV; -.
DR OrthoDB; 941128at2759; -.
DR PhylomeDB; P33896; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR BioGRID-ORCS; 15975; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Ifnar1; mouse.
DR PRO; PR:P33896; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P33896; protein.
DR Bgee; ENSMUSG00000022967; Expressed in undifferentiated genital tubercle and 270 other tissues.
DR ExpressionAtlas; P33896; baseline and differential.
DR Genevisible; P33896; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004904; F:interferon receptor activity; IMP:UniProtKB.
DR GO; GO:0019962; F:type I interferon binding; IPI:UniProtKB.
DR GO; GO:0004905; F:type I interferon receptor activity; IDA:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IMP:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:CACAO.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IGI:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IGI:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR InterPro; IPR016669; Interferon_alpha/beta_rcpt-1.
DR Pfam; PF09294; Interfer-bind; 2.
DR Pfam; PF01108; Tissue_fac; 1.
DR PIRSF; PIRSF016567; IFN_alpha/beta_recept-1; 1.
DR SMART; SM00060; FN3; 3.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW Isopeptide bond; Lysosome; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..590
FT /note="Interferon alpha/beta receptor 1"
FT /id="PRO_0000011002"
FT TOPO_DOM 27..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..125
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 127..226
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 230..327
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 332..425
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 483..492
FT /note="Important for interaction with TYK2"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT REGION 514..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14532120"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..86
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT DISULFID 199..220
FT /evidence="ECO:0000269|PubMed:23872679"
FT DISULFID 284..292
FT /evidence="ECO:0000269|PubMed:23872679"
FT DISULFID 397..419
FT /evidence="ECO:0000269|PubMed:23872679"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P17181"
FT MUTAGEN 526
FT /note="S->A: Abolishes interaction with FBXW11. Prevents
FT interalization from the cell membrane and lysosomal
FT degradation."
FT /evidence="ECO:0000269|PubMed:14532120"
FT CONFLICT 274
FT /note="R -> H (in Ref. 1; AAA37890)"
FT /evidence="ECO:0000305"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3WCY"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3WCY"
FT TURN 157..162
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3WCY"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3WCY"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 362..369
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 376..387
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:3WCY"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:3WCY"
SQ SEQUENCE 590 AA; 65796 MW; E887ADFA6DFEAF3C CRC64;
MLAVVGAAAL VLVAGAPWVL PSAAGGENLK PPENIDVYII DDNYTLKWSS HGESMGSVTF
SAEYRTKDEA KWLKVPECQH TTTTKCEFSL LDTNVYIKTQ FRVRAEEGNS TSSWNEVDPF
IPFYTAHMSP PEVRLEAEDK AILVHISPPG QDGNMWALEK PSFSYTIRIW QKSSSDKKTI
NSTYYVEKIP ELLPETTYCL EVKAIHPSLK KHSNYSTVQC ISTTVANKMP VPGNLQVDAQ
GKSYVLKWDY IASADVLFRA QWLPGYSKSS SGSRSDKWKP IPTCANVQTT HCVFSQDTVY
TGTFFLHVQA SEGNHTSFWS EEKFIDSQKH ILPPPPVITV TAMSDTLLVY VNCQDSTCDG
LNYEIIFWEN TSNTKISMEK DGPEFTLKNL QPLTVYCVQA RVLFRALLNK TSNFSEKLCE
KTRPGSFSTI WIITGLGVVF FSVMVLYALR SVWKYLCHVC FPPLKPPRSI DEFFSEPPSK
NLVLLTAEEH TERCFIIENT DTVAVEVKHA PEEDLRKYSS QTSQDSGNYS NEEEESVGTE
SGQAVLSKAP CGGPCSVPSP PGTLEDGTCF LGNEKYLQSP ALRTEPALLC
