IL21R_HUMAN
ID IL21R_HUMAN Reviewed; 538 AA.
AC Q9HBE5; A8K9E8; D3DWF7; Q96HZ1; Q9HB91;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Interleukin-21 receptor;
DE Short=IL-21 receptor;
DE Short=IL-21R;
DE AltName: Full=Novel interleukin receptor;
DE AltName: CD_antigen=CD360;
DE Flags: Precursor;
GN Name=IL21R; Synonyms=NILR; ORFNames=UNQ3121/PRO10273;
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].
RX PubMed=11081504; DOI=10.1038/35040504;
RA Parrish-Novak J., Dillon S.R., Nelson A., Hammond A., Sprecher C.,
RA Gross J.A., Johnston J., Madden K., Xu W., West J., Schrader S.,
RA Burkhead S., Heipel M., Brandt C., Kuijper J.L., Kramer J., Conklin D.,
RA Presnell S.R., Berry J., Shiota F., Bort S., Hambly K., Mudri S., Clegg C.,
RA Moore M., Grant F.J., Lofton-Day C., Gilbert T., Raymond F., Ching A.,
RA Yao L., Smith D., Webster P., Whitmore T., Maurer M., Kaushansky K.,
RA Holly R.D., Foster D.;
RT "Interleukin 21 and its receptor are involved in NK cell expansion and
RT regulation of lymphocyte function.";
RL Nature 408:57-63(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11016959; DOI=10.1073/pnas.200360997;
RA Ozaki K., Kikly K., Michalovich D., Young P.R., Leonard W.J.;
RT "Cloning of a type I cytokine receptor most related to the IL-2 receptor
RT beta chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11439-11444(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-191; ARG-318 AND
RP SER-484.
RG SeattleSNPs variation discovery resource;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell, and Lymph;
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 [8]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [9]
RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION
RP WITH BCL6.
RX PubMed=11821949; DOI=10.1038/sj.onc.1205099;
RA Ueda C., Akasaka T., Kurata M., Maesako Y., Nishikori M., Ichinohasama R.,
RA Imada K., Uchiyama T., Ohno H.;
RT "The gene for interleukin-21 receptor is the partner of BCL6 in
RT t(3;16)(q27;p11), which is recurrently observed in diffuse large B-cell
RT lymphoma.";
RL Oncogene 21:368-376(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-232 IN COMPLEX WITH IL21,
RP DOMAIN WSXWS MOTIF, GLYCOSYLATION AT ASN-73 AND TRP-214, DOMAINS
RP FIBRONECTIN, AND DISULFIDE BONDS.
RX PubMed=22235133; DOI=10.1074/jbc.m111.311084;
RA Hamming O.J., Kang L., Svensson A., Karlsen J.L., Rahbek-Nielsen H.,
RA Paludan S.R., Hjorth S.A., Bondensgaard K., Hartmann R.;
RT "Crystal structure of interleukin-21 receptor (IL-21R) bound to IL-21
RT reveals that sugar chain interacting with WSXWS motif is integral part of
RT IL-21R.";
RL J. Biol. Chem. 287:9454-9460(2012).
RN [11]
RP VARIANTS IMD56 81-CYS-HIS-82 DEL AND LEU-201, AND CHARACTERIZATION VARIANT
RP IMD56 LEU-201.
RX PubMed=23440042; DOI=10.1084/jem.20111229;
RA Kotlarz D., Zietara N., Uzel G., Weidemann T., Braun C.J., Diestelhorst J.,
RA Krawitz P.M., Robinson P.N., Hecht J., Puchalka J., Gertz E.M.,
RA Schaeffer A.A., Lawrence M.G., Kardava L., Pfeifer D., Baumann U.,
RA Pfister E.D., Hanson E.P., Schambach A., Jacobs R., Kreipe H., Moir S.,
RA Milner J.D., Schwille P., Mundlos S., Klein C.;
RT "Loss-of-function mutations in the IL-21 receptor gene cause a primary
RT immunodeficiency syndrome.";
RL J. Exp. Med. 210:433-443(2013).
CC -!- FUNCTION: This is a receptor for interleukin-21.
CC -!- SUBUNIT: Heterodimer with the common gamma subunit. Associates with
CC JAK1. {ECO:0000269|PubMed:22235133}.
CC -!- INTERACTION:
CC Q9HBE5; P29972: AQP1; NbExp=3; IntAct=EBI-12558959, EBI-745213;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Selectively expressed in lymphoid tissues. Most
CC highly expressed in thymus and spleen.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding. {ECO:0000269|PubMed:22235133}.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation. {ECO:0000269|PubMed:22235133}.
CC -!- PTM: C-mannosylated at Trp-214 in the WSXWS motif, the sugar chain
CC makes extensive hydrogen bonds with Asn-73 sugar, and bridges the two
CC fibronectin domains transforming the V-shaped receptor into an A-frame.
CC -!- DISEASE: Immunodeficiency 56 (IMD56) [MIM:615207]: An autosomal
CC recessive primary immunodeficiency characterized by B- and T-cell
CC defects and variable dysfunction of NK cells. Patients tend to have
CC normal numbers of lymphocytes, but show defective class-switched B-
CC cells, low IgG, defective antibody response, and defective T-cell
CC responses to certain antigens. {ECO:0000269|PubMed:23440042}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Chromosomal aberrations involving IL21R is a cause of B-
CC cell non-Hodgkin lymphomas (B-cell NHL). Translocation
CC t(3;16)(q27;p11), with BCL6.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL21RID40955ch16p12.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il21r/";
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DR EMBL; AF254067; AAG29346.1; -; mRNA.
DR EMBL; AF269133; AAG23419.1; -; mRNA.
DR EMBL; AY358826; AAQ89185.1; -; mRNA.
DR EMBL; AY064474; AAL39168.1; -; Genomic_DNA.
DR EMBL; AK292663; BAF85352.1; -; mRNA.
DR EMBL; CH471145; EAW55746.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55747.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55748.1; -; Genomic_DNA.
DR EMBL; BC004348; AAH04348.1; -; mRNA.
DR EMBL; BC007946; AAH07946.2; -; mRNA.
DR CCDS; CCDS10630.1; -.
DR RefSeq; NP_068570.1; NM_021798.3.
DR RefSeq; NP_851564.1; NM_181078.2.
DR RefSeq; NP_851565.4; NM_181079.4.
DR RefSeq; XP_016878746.1; XM_017023257.1.
DR PDB; 3TGX; X-ray; 2.80 A; A/C/E/G/I/K/M/O=20-232.
DR PDB; 4NZD; X-ray; 2.75 A; A/B/C=20-232.
DR PDB; 6PLH; X-ray; 1.60 A; C=202-232.
DR PDB; 7KQ7; X-ray; 2.20 A; B=20-233.
DR PDBsum; 3TGX; -.
DR PDBsum; 4NZD; -.
DR PDBsum; 6PLH; -.
DR PDBsum; 7KQ7; -.
DR AlphaFoldDB; Q9HBE5; -.
DR SMR; Q9HBE5; -.
DR BioGRID; 119095; 6.
DR IntAct; Q9HBE5; 1.
DR STRING; 9606.ENSP00000338010; -.
DR GlyGen; Q9HBE5; 6 sites.
DR iPTMnet; Q9HBE5; -.
DR PhosphoSitePlus; Q9HBE5; -.
DR BioMuta; IL21R; -.
DR DMDM; 20454997; -.
DR MassIVE; Q9HBE5; -.
DR MaxQB; Q9HBE5; -.
DR PaxDb; Q9HBE5; -.
DR PeptideAtlas; Q9HBE5; -.
DR PRIDE; Q9HBE5; -.
DR ProteomicsDB; 81535; -.
DR ABCD; Q9HBE5; 59 sequenced antibodies.
DR Antibodypedia; 12828; 457 antibodies from 41 providers.
DR DNASU; 50615; -.
DR Ensembl; ENST00000337929.8; ENSP00000338010.3; ENSG00000103522.16.
DR Ensembl; ENST00000395754.4; ENSP00000379103.4; ENSG00000103522.16.
DR Ensembl; ENST00000564089.5; ENSP00000456707.1; ENSG00000103522.16.
DR GeneID; 50615; -.
DR KEGG; hsa:50615; -.
DR MANE-Select; ENST00000337929.8; ENSP00000338010.3; NM_181078.3; NP_851564.1.
DR UCSC; uc002doq.2; human.
DR CTD; 50615; -.
DR DisGeNET; 50615; -.
DR GeneCards; IL21R; -.
DR HGNC; HGNC:6006; IL21R.
DR HPA; ENSG00000103522; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; IL21R; -.
DR MIM; 605383; gene.
DR MIM; 615207; phenotype.
DR neXtProt; NX_Q9HBE5; -.
DR OpenTargets; ENSG00000103522; -.
DR Orphanet; 357329; Combined immunodeficiency due to IL21R deficiency.
DR PharmGKB; PA29821; -.
DR VEuPathDB; HostDB:ENSG00000103522; -.
DR eggNOG; ENOG502S0QM; Eukaryota.
DR GeneTree; ENSGT00510000048783; -.
DR HOGENOM; CLU_039739_0_0_1; -.
DR InParanoid; Q9HBE5; -.
DR OMA; RFFQPLY; -.
DR OrthoDB; 774083at2759; -.
DR PhylomeDB; Q9HBE5; -.
DR TreeFam; TF337874; -.
DR PathwayCommons; Q9HBE5; -.
DR Reactome; R-HSA-9020958; Interleukin-21 signaling.
DR SignaLink; Q9HBE5; -.
DR SIGNOR; Q9HBE5; -.
DR BioGRID-ORCS; 50615; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; IL21R; human.
DR GeneWiki; Interleukin-21_receptor; -.
DR GenomeRNAi; 50615; -.
DR Pharos; Q9HBE5; Tbio.
DR PRO; PR:Q9HBE5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9HBE5; protein.
DR Bgee; ENSG00000103522; Expressed in granulocyte and 139 other tissues.
DR Genevisible; Q9HBE5; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004896; F:cytokine receptor activity; IDA:MGI.
DR GO; GO:0001532; F:interleukin-21 receptor activity; NAS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0030101; P:natural killer cell activation; NAS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosomal rearrangement; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..538
FT /note="Interleukin-21 receptor"
FT /id="PRO_0000010881"
FT TOPO_DOM 20..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..118
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 119..228
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 342..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..218
FT /note="WSXWS motif"
FT MOTIF 266..274
FT /note="Box 1 motif"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22235133"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:22235133"
FT DISULFID 20..109
FT /evidence="ECO:0000269|PubMed:22235133"
FT DISULFID 25..35
FT /evidence="ECO:0000269|PubMed:22235133"
FT DISULFID 65..81
FT /evidence="ECO:0000269|PubMed:22235133"
FT VARIANT 81..82
FT /note="Missing (in IMD56; loss of function mutation)"
FT /evidence="ECO:0000269|PubMed:23440042"
FT /id="VAR_069898"
FT VARIANT 191
FT /note="R -> C (in dbSNP:rs3093370)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014360"
FT VARIANT 201
FT /note="R -> L (in IMD56; loss of function mutation; the
FT mutation results in defective trafficking of the protein,
FT with misfolding, impaired processing and abnormal
FT subcellular distribution rather than proper expression at
FT the plasma membrane; dbSNP:rs397514685)"
FT /evidence="ECO:0000269|PubMed:23440042"
FT /id="VAR_069899"
FT VARIANT 318
FT /note="S -> R (in dbSNP:rs3093385)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014361"
FT VARIANT 484
FT /note="G -> S (in dbSNP:rs3093386)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_014362"
FT CONFLICT 386
FT /note="G -> R (in Ref. 2; AAG23419)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:7KQ7"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3TGX"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:7KQ7"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:7KQ7"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3TGX"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7KQ7"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:7KQ7"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4NZD"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:7KQ7"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4NZD"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7KQ7"
SQ SEQUENCE 538 AA; 59130 MW; 414079CCB974850A CRC64;
MPRGWAAPLL LLLLQGGWGC PDLVCYTDYL QTVICILEMW NLHPSTLTLT WQDQYEELKD
EATSCSLHRS AHNATHATYT CHMDVFHFMA DDIFSVNITD QSGNYSQECG SFLLAESIKP
APPFNVTVTF SGQYNISWRS DYEDPAFYML KGKLQYELQY RNRGDPWAVS PRRKLISVDS
RSVSLLPLEF RKDSSYELQV RAGPMPGSSY QGTWSEWSDP VIFQTQSEEL KEGWNPHLLL
LLLLVIVFIP AFWSLKTHPL WRLWKKIWAV PSPERFFMPL YKGCSGDFKK WVGAPFTGSS
LELGPWSPEV PSTLEVYSCH PPRSPAKRLQ LTELQEPAEL VESDGVPKPS FWPTAQNSGG
SAYSEERDRP YGLVSIDTVT VLDAEGPCTW PCSCEDDGYP ALDLDAGLEP SPGLEDPLLD
AGTTVLSCGC VSAGSPGLGG PLGSLLDRLK PPLADGEDWA GGLPWGGRSP GGVSESEAGS
PLAGLDMDTF DSGFVGSDCS SPVECDFTSP GDEGPPRSYL RQWVVIPPPL SSPGPQAS
