I13R2_HUMAN
ID I13R2_HUMAN Reviewed; 380 AA.
AC Q14627; A8K7E2; O00667;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Interleukin-13 receptor subunit alpha-2;
DE Short=IL-13 receptor subunit alpha-2;
DE Short=IL-13R subunit alpha-2;
DE Short=IL-13R-alpha-2;
DE Short=IL-13RA2;
DE AltName: Full=Interleukin-13-binding protein;
DE AltName: CD_antigen=CD213a2;
DE Flags: Precursor;
GN Name=IL13RA2; Synonyms=IL13R;
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].
RC TISSUE=Renal cell carcinoma;
RX PubMed=8663118; DOI=10.1074/jbc.271.28.16921;
RA Caput D., Laurent P., Kaghad M., Lelias J.M., Lefort S., Vita N.,
RA Ferrara P.;
RT "Cloning and characterization of a specific interleukin (IL)-13 binding
RT protein structurally related to the IL-5 receptor alpha chain.";
RL J. Biol. Chem. 271:16921-16926(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Donaldson D.D., Whitters M.J., Fitz L., Neben T., Finnerty H.,
RA Henderson S.L., O'Hara R.M. Jr., Turner K.J., Wood C.R., Collins M.;
RT "Identification of a third chain for the murine Il-13 receptor.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9177784; DOI=10.1006/geno.1997.4628;
RA Guo J., Apiou F., Mellerin M.P., Lebeau B., Jacques Y., Minvielle S.;
RT "Chromosome mapping and expression of the human interleukin-13 receptor.";
RL Genomics 42:141-145(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-111.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Prostate;
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 X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH IL13, FUNCTION,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-215.
RX PubMed=20223216; DOI=10.1016/j.str.2010.01.003;
RA Lupardus P.J., Birnbaum M.E., Garcia K.C.;
RT "Molecular basis for shared cytokine recognition revealed in the structure
RT of an unusually high affinity complex between IL-13 and IL-13Ralpha2.";
RL Structure 18:332-342(2010).
CC -!- FUNCTION: Binds as a monomer with high affinity to interleukin-13
CC (IL13), but not to interleukin-4 (IL4). {ECO:0000269|PubMed:20223216}.
CC -!- INTERACTION:
CC Q14627; P36222: CHI3L1; NbExp=9; IntAct=EBI-4320063, EBI-6917454;
CC Q14627; P35225: IL13; NbExp=9; IntAct=EBI-4320063, EBI-1647828;
CC Q14627; P17931: LGALS3; NbExp=2; IntAct=EBI-4320063, EBI-1170392;
CC Q14627; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-4320063, EBI-11721828;
CC Q14627; Q86XT9: TMEM219; NbExp=9; IntAct=EBI-4320063, EBI-20264080;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il13ra2/";
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DR EMBL; X95302; CAA64617.1; -; mRNA.
DR EMBL; U70981; AAB17170.1; -; mRNA.
DR EMBL; Y08768; CAA70021.1; -; mRNA.
DR EMBL; AK291957; BAF84646.1; -; mRNA.
DR EMBL; AY656702; AAT49099.1; -; Genomic_DNA.
DR EMBL; AL121878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020739; AAH20739.1; -; mRNA.
DR EMBL; BC033705; AAH33705.1; -; mRNA.
DR CCDS; CCDS14565.1; -.
DR RefSeq; NP_000631.1; NM_000640.2.
DR PDB; 3LB6; X-ray; 3.05 A; C/D=1-380.
DR PDBsum; 3LB6; -.
DR AlphaFoldDB; Q14627; -.
DR SMR; Q14627; -.
DR BioGRID; 109812; 131.
DR DIP; DIP-3340N; -.
DR IntAct; Q14627; 112.
DR MINT; Q14627; -.
DR STRING; 9606.ENSP00000361004; -.
DR ChEMBL; CHEMBL3713941; -.
DR DrugBank; DB05078; AER001.
DR GlyGen; Q14627; 4 sites.
DR iPTMnet; Q14627; -.
DR BioMuta; IL13RA2; -.
DR DMDM; 2494720; -.
DR jPOST; Q14627; -.
DR MassIVE; Q14627; -.
DR MaxQB; Q14627; -.
DR PaxDb; Q14627; -.
DR PeptideAtlas; Q14627; -.
DR PRIDE; Q14627; -.
DR ProteomicsDB; 60078; -.
DR ABCD; Q14627; 2 sequenced antibodies.
DR Antibodypedia; 29593; 568 antibodies from 39 providers.
DR DNASU; 3598; -.
DR Ensembl; ENST00000243213.2; ENSP00000243213.1; ENSG00000123496.8.
DR Ensembl; ENST00000371936.5; ENSP00000361004.1; ENSG00000123496.8.
DR GeneID; 3598; -.
DR KEGG; hsa:3598; -.
DR MANE-Select; ENST00000243213.2; ENSP00000243213.1; NM_000640.3; NP_000631.1.
DR UCSC; uc004epx.4; human.
DR CTD; 3598; -.
DR DisGeNET; 3598; -.
DR GeneCards; IL13RA2; -.
DR HGNC; HGNC:5975; IL13RA2.
DR HPA; ENSG00000123496; Tissue enhanced (brain, pituitary gland, testis).
DR MIM; 300130; gene.
DR neXtProt; NX_Q14627; -.
DR OpenTargets; ENSG00000123496; -.
DR PharmGKB; PA29788; -.
DR VEuPathDB; HostDB:ENSG00000123496; -.
DR eggNOG; ENOG502RV4W; Eukaryota.
DR GeneTree; ENSGT00940000159971; -.
DR HOGENOM; CLU_054773_1_0_1; -.
DR InParanoid; Q14627; -.
DR OMA; DCIYYNW; -.
DR OrthoDB; 1151666at2759; -.
DR PhylomeDB; Q14627; -.
DR TreeFam; TF331549; -.
DR PathwayCommons; Q14627; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; Q14627; -.
DR BioGRID-ORCS; 3598; 10 hits in 696 CRISPR screens.
DR ChiTaRS; IL13RA2; human.
DR EvolutionaryTrace; Q14627; -.
DR GeneWiki; IL13RA2; -.
DR GenomeRNAi; 3598; -.
DR Pharos; Q14627; Tbio.
DR PRO; PR:Q14627; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14627; protein.
DR Bgee; ENSG00000123496; Expressed in sperm and 114 other tissues.
DR Genevisible; Q14627; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..380
FT /note="Interleukin-13 receptor subunit alpha-2"
FT /id="PRO_0000010942"
FT TOPO_DOM 27..343
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..134
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 139..235
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 240..333
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 322..326
FT /note="WSXWS motif"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20223216"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..113
FT /evidence="ECO:0000269|PubMed:20223216"
FT DISULFID 145..155
FT /evidence="ECO:0000269|PubMed:20223216"
FT DISULFID 184..197
FT /evidence="ECO:0000269|PubMed:20223216"
FT DISULFID 269..316
FT /evidence="ECO:0000269|PubMed:20223216"
FT VARIANT 111
FT /note="W -> R (in dbSNP:rs17095919)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021256"
FT CONFLICT 8
FT /note="I -> V (in Ref. 4; BAF84646)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Q -> R (in Ref. 4; BAF84646)"
FT /evidence="ECO:0000305"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 44..54
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 82..94
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3LB6"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3LB6"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3LB6"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3LB6"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:3LB6"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:3LB6"
SQ SEQUENCE 380 AA; 44176 MW; 3C6ACB1B5562C887 CRC64;
MAFVCLAIGC LYTFLISTTF GCTSSSDTEI KVNPPQDFEI VDPGYLGYLY LQWQPPLSLD
HFKECTVEYE LKYRNIGSET WKTIITKNLH YKDGFDLNKG IEAKIHTLLP WQCTNGSEVQ
SSWAETTYWI SPQGIPETKV QDMDCVYYNW QYLLCSWKPG IGVLLDTNYN LFYWYEGLDH
ALQCVDYIKA DGQNIGCRFP YLEASDYKDF YICVNGSSEN KPIRSSYFTF QLQNIVKPLP
PVYLTFTRES SCEIKLKWSI PLGPIPARCF DYEIEIREDD TTLVTATVEN ETYTLKTTNE
TRQLCFVVRS KVNIYCSDDG IWSEWSDKQC WEGEDLSKKT LLRFWLPFGF ILILVIFVTG
LLLRKPNTYP KMIPEFFCDT
