IRPL2_HUMAN
ID IRPL2_HUMAN Reviewed; 686 AA.
AC Q9NP60; Q2M3U3; Q9NZN0;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=X-linked interleukin-1 receptor accessory protein-like 2;
DE Short=IL-1 receptor accessory protein-like 2;
DE Short=IL-1-RAPL-2;
DE Short=IL-1RAPL-2;
DE Short=IL1RAPL-2;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=IL1RAPL-2-related protein;
DE AltName: Full=Interleukin-1 receptor 9;
DE Short=IL-1R-9;
DE Short=IL-1R9;
DE AltName: Full=Three immunoglobulin domain-containing IL-1 receptor-related 1;
DE Short=TIGIRR-1;
DE Flags: Precursor;
GN Name=IL1RAPL2; Synonyms=IL1R9;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=11031108; DOI=10.1006/geno.2000.6328;
RA Sana T.R., Debets R., Timans J.C., Bazan J.F., Kastelein R.A.;
RT "Computational identification, cloning, and characterization of IL-1R9, a
RT novel interleukin-1 receptor-like gene encoded over an unusually large
RT interval of human chromosome Xq22.2-q22.3.";
RL Genomics 69:252-262(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10882729; DOI=10.1074/jbc.m004077200;
RA Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S., Sims J.E.;
RT "Identification and characterization of two members of a novel class of the
RT interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-
RT related proteins based on signaling.";
RL J. Biol. Chem. 275:29946-29954(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Grabowski M., Lorenz B., Hubel R., Strom T.M.;
RT "A gene (IL1RAPL-2) with 61% identity to IL1RAPL maps to Xq22.2.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11587848; DOI=10.1016/s0378-1119(01)00659-x;
RA Ferrante M.I., Ghiani M., Bulfone A., Franco B.;
RT "IL1RAPL2 maps to Xq22 and is specifically expressed in the central nervous
RT system.";
RL Gene 275:217-221(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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].
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=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 29-686.
RX PubMed=10757639; DOI=10.1038/sj.ejhg.5200415;
RA Jin H., Gardner R.J., Viswesvaraiah R., Muntoni F., Roberts R.G.;
RT "Two novel members of the interleukin-1 receptor gene family, one deleted
RT in Xp22.3-Xp21.3 mental retardation.";
RL Eur. J. Hum. Genet. 8:87-94(2000).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-606.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Detected at low levels in fetal and adult brain, in
CC particular in the frontal lobe, temporal lobe and cerebellum. Detected
CC at very low levels in skin, liver, fetal ovary and in placenta.
CC {ECO:0000269|PubMed:10882729, ECO:0000269|PubMed:11031108,
CC ECO:0000269|PubMed:11587848}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF212016; AAF61307.1; -; mRNA.
DR EMBL; AF284436; AAG21370.1; -; mRNA.
DR EMBL; AJ272208; CAB86868.1; -; mRNA.
DR EMBL; AJ290436; CAB89867.1; -; mRNA.
DR EMBL; AK290196; BAF82885.1; -; mRNA.
DR EMBL; AL050401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z68328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z68330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z68908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z69721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z74477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z74619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z81144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF181285; AAF59412.1; -; mRNA.
DR EMBL; BC104784; AAI04785.1; -; mRNA.
DR EMBL; BC104786; AAI04787.1; -; mRNA.
DR CCDS; CCDS14517.1; -.
DR RefSeq; NP_059112.1; NM_017416.1.
DR RefSeq; XP_016884892.1; XM_017029403.1.
DR PDB; 7SZL; X-ray; 2.30 A; A=400-559.
DR PDBsum; 7SZL; -.
DR AlphaFoldDB; Q9NP60; -.
DR SMR; Q9NP60; -.
DR BioGRID; 117663; 2.
DR IntAct; Q9NP60; 1.
DR STRING; 9606.ENSP00000361663; -.
DR GlyGen; Q9NP60; 5 sites.
DR iPTMnet; Q9NP60; -.
DR PhosphoSitePlus; Q9NP60; -.
DR BioMuta; IL1RAPL2; -.
DR DMDM; 34222651; -.
DR PaxDb; Q9NP60; -.
DR PeptideAtlas; Q9NP60; -.
DR PRIDE; Q9NP60; -.
DR ProteomicsDB; 81891; -.
DR Antibodypedia; 35255; 284 antibodies from 30 providers.
DR DNASU; 26280; -.
DR Ensembl; ENST00000372582.6; ENSP00000361663.1; ENSG00000189108.13.
DR GeneID; 26280; -.
DR KEGG; hsa:26280; -.
DR MANE-Select; ENST00000372582.6; ENSP00000361663.1; NM_017416.2; NP_059112.1.
DR UCSC; uc004elz.1; human.
DR CTD; 26280; -.
DR DisGeNET; 26280; -.
DR GeneCards; IL1RAPL2; -.
DR HGNC; HGNC:5997; IL1RAPL2.
DR HPA; ENSG00000189108; Tissue enhanced (adrenal gland, parathyroid gland).
DR MIM; 300277; gene.
DR neXtProt; NX_Q9NP60; -.
DR OpenTargets; ENSG00000189108; -.
DR PharmGKB; PA29813; -.
DR VEuPathDB; HostDB:ENSG00000189108; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_0_1_1; -.
DR InParanoid; Q9NP60; -.
DR OMA; DYHQADS; -.
DR OrthoDB; 651291at2759; -.
DR PhylomeDB; Q9NP60; -.
DR TreeFam; TF333913; -.
DR PathwayCommons; Q9NP60; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q9NP60; -.
DR SIGNOR; Q9NP60; -.
DR BioGRID-ORCS; 26280; 16 hits in 690 CRISPR screens.
DR ChiTaRS; IL1RAPL2; human.
DR GeneWiki; IL1RAPL2; -.
DR GenomeRNAi; 26280; -.
DR Pharos; Q9NP60; Tbio.
DR PRO; PR:Q9NP60; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NP60; protein.
DR Bgee; ENSG00000189108; Expressed in cortical plate and 89 other tissues.
DR ExpressionAtlas; Q9NP60; baseline and differential.
DR Genevisible; Q9NP60; HS.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004908; F:interleukin-1 receptor activity; TAS:ProtInc.
DR GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
DR SMART; SM00409; IG; 3.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..686
FT /note="X-linked interleukin-1 receptor accessory protein-
FT like 2"
FT /id="PRO_0000015459"
FT TOPO_DOM 17..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..132
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..232
FT /note="Ig-like C2-type 2"
FT DOMAIN 239..347
FT /note="Ig-like C2-type 3"
FT DOMAIN 400..556
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 265..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 606
FT /note="F -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036592"
SQ SEQUENCE 686 AA; 78670 MW; E400F7ECD186957C CRC64;
MKPPFLLALV VCSVVSTNLK MVSKRNSVDG CIDWSVDLKT YMALAGEPVR VKCALFYSYI
RTNYSTAQST GLRLMWYKNK GDLEEPIIFS EVRMSKEEDS IWFHSAEAQD SGFYTCVLRN
STYCMKVSMS LTVAENESGL CYNSRIRYLE KSEVTKRKEI SCPDMDDFKK SDQEPDVVWY
KECKPKMWRS IIIQKGNALL IQEVQEEDGG NYTCELKYEG KLVRRTTELK VTALLTDKPP
KPLFPMENQP SVIDVQLGKP LNIPCKAFFG FSGESGPMIY WMKGEKFIEE LAGHIREGEI
RLLKEHLGEK EVELALIFDS VVEADLANYT CHVENRNGRK HASVLLRKKD LIYKIELAGG
LGAIFLLLVL LVVIYKCYNI ELMLFYRQHF GADETNDDNK EYDAYLSYTK VDQDTLDCDN
PEEEQFALEV LPDVLEKHYG YKLFIPERDL IPSGTYMEDL TRYVEQSRRL IIVLTPDYIL
RRGWSIFELE SRLHNMLVSG EIKVILIECT ELKGKVNCQE VESLKRSIKL LSLIKWKGSK
SSKLNSKFWK HLVYEMPIKK KEMLPRCHVL DSAEQGLFGE LQPIPSIAMT STSATLVSSQ
ADLPEFHPSD SMQIRHCCRG YKHEIPATTL PVPSLGNHHT YCNLPLTLLN GQLPLNNTLK
DTQEFHRNSS LLPLSSKELS FTSDIW
