TAB2_MOUSE
ID TAB2_MOUSE Reviewed; 693 AA.
AC Q99K90; Q3UGP1; Q8BTP4; Q8CHD3; Q99KP4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 2;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 2;
DE AltName: Full=TAK1-binding protein 2;
DE Short=TAB-2;
DE AltName: Full=TGF-beta-activated kinase 1-binding protein 2;
GN Name=Tab2; Synonyms=Kiaa0733, Map3k7ip2;
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], SUBUNIT, TISSUE SPECIFICITY, PHOSPHORYLATION,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=12150997; DOI=10.1016/s0092-8674(02)00809-7;
RA Baek S.H., Ohgi K.A., Rose D.W., Koo E.H., Glass C.K., Rosenfeld M.G.;
RT "Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene
RT expression by NF-kappaB and beta-amyloid precursor protein.";
RL Cell 110:55-67(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=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 [LARGE SCALE MRNA] OF 1-595.
RC STRAIN=C57BL/6J, and NOD;
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 MRNA] OF 9-693.
RC TISSUE=Embryonic tail;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 665-693 IN COMPLEX WITH ZINC IONS
RP AND 'LYS-63'-LINKED UBIQUITIN, FUNCTION, LINKAGE-SPECIFIC INTERACTION WITH
RP UBIQUITIN, NZF DOMAIN, SUBUNIT, AND MUTAGENESIS OF THR-674; PHE-675;
RP HIS-678; LEU-681; GLU-685 AND GLN-686.
RX PubMed=19927120; DOI=10.1038/emboj.2009.345;
RA Sato Y., Yoshikawa A., Yamashita M., Yamagata A., Fukai S.;
RT "Structural basis for specific recognition of Lys 63-linked polyubiquitin
RT chains by NZF domains of TAB2 and TAB3.";
RL EMBO J. 28:3903-3909(2009).
CC -!- FUNCTION: Adapter required to activate the JNK and NF-kappa-B signaling
CC pathways through the specific recognition of 'Lys-63'-linked
CC polyubiquitin chains by its RanBP2-type zinc finger (NZF) (By
CC similarity). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-
CC 63'-linked polyubiquitin chains (By similarity). The RanBP2-type zinc
CC finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin
CC chains unanchored or anchored to the substrate proteins such as
CC RIPK1/RIP1: this acts as a scaffold to organize a large signaling
CC complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent
CC activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1
CC (PubMed:19927120). Regulates the IL1-mediated translocation of NCOR1
CC out of the nucleus (PubMed:12150997). Involved in heart development (By
CC similarity). {ECO:0000250|UniProtKB:Q9NYJ8,
CC ECO:0000269|PubMed:12150997, ECO:0000269|PubMed:19927120}.
CC -!- SUBUNIT: Interacts with MAP3K7 and TRAF6. Identified in the TRIKA2
CC complex composed of MAP3K7, TAB1 and TAB2. Binds 'Lys-63'-linked
CC polyubiquitin chains (By similarity). Interacts with NCOR1 and HDAC3 to
CC form a ternary complex (PubMed:12150997). Interacts (via C-terminal)
CC with NUMBL (via PTB domain). Interacts (via the C-terminus) with
CC DYNC2I2 (via WD domains). Interacts with RBCK1. Interacts with TRIM5
CC (By similarity). Interacts with TRIM38 (via B30.2/SPRY domain), leading
CC to its translocation to lysosomes and degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NYJ8, ECO:0000269|PubMed:12150997}.
CC -!- INTERACTION:
CC Q99K90; Q62073: Map3k7; NbExp=8; IntAct=EBI-1775124, EBI-1775345;
CC Q99K90; P62991: Ubc; NbExp=9; IntAct=EBI-1775124, EBI-413074;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NYJ8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9NYJ8}. Endosome
CC membrane {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9NYJ8}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9NYJ8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9NYJ8}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:12150997}. Nucleus {ECO:0000269|PubMed:12150997}.
CC Note=Following IL1 stimulation, translocation occurs from the membrane
CC to cytosol. Interaction with TRIM38 promotes translocation from cytosol
CC to endosome and lysosome. {ECO:0000250|UniProtKB:Q9NYJ8}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12150997}.
CC -!- DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two
CC consecutive 'Lys-63'-linked ubiquitins. {ECO:0000269|PubMed:19927120}.
CC -!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression.
CC Ubiquitination involves RBCK1 leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9NYJ8}.
CC -!- PTM: Degraded in a lysosome-dependent manner following interactiuon
CC with TRIM38. {ECO:0000250|UniProtKB:Q9NYJ8}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:12150997}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40772.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY093701; AAM10487.1; -; mRNA.
DR EMBL; BC004072; AAH04072.1; -; mRNA.
DR EMBL; BC004813; AAH04813.1; -; mRNA.
DR EMBL; AK089164; BAC40772.1; ALT_FRAME; mRNA.
DR EMBL; AK147830; BAE28166.1; -; mRNA.
DR EMBL; AB093262; BAC41446.1; -; mRNA.
DR CCDS; CCDS23691.1; -.
DR RefSeq; NP_619608.1; NM_138667.3.
DR RefSeq; XP_017169562.1; XM_017314073.1.
DR PDB; 3A9J; X-ray; 1.18 A; C=665-693.
DR PDB; 7E62; X-ray; 1.99 A; C/J=644-693.
DR PDBsum; 3A9J; -.
DR PDBsum; 7E62; -.
DR AlphaFoldDB; Q99K90; -.
DR BMRB; Q99K90; -.
DR SMR; Q99K90; -.
DR BioGRID; 212973; 11.
DR IntAct; Q99K90; 4.
DR MINT; Q99K90; -.
DR STRING; 10090.ENSMUSP00000121266; -.
DR iPTMnet; Q99K90; -.
DR PhosphoSitePlus; Q99K90; -.
DR EPD; Q99K90; -.
DR jPOST; Q99K90; -.
DR MaxQB; Q99K90; -.
DR PaxDb; Q99K90; -.
DR PRIDE; Q99K90; -.
DR ProteomicsDB; 254488; -.
DR Antibodypedia; 19871; 237 antibodies from 36 providers.
DR DNASU; 68652; -.
DR Ensembl; ENSMUST00000146444; ENSMUSP00000121266; ENSMUSG00000015755.
DR GeneID; 68652; -.
DR KEGG; mmu:68652; -.
DR UCSC; uc007eir.2; mouse.
DR CTD; 23118; -.
DR MGI; MGI:1915902; Tab2.
DR VEuPathDB; HostDB:ENSMUSG00000015755; -.
DR eggNOG; ENOG502QRAY; Eukaryota.
DR GeneTree; ENSGT00940000158473; -.
DR HOGENOM; CLU_025065_0_0_1; -.
DR InParanoid; Q99K90; -.
DR OMA; GPTFIHH; -.
DR OrthoDB; 324984at2759; -.
DR PhylomeDB; Q99K90; -.
DR TreeFam; TF332021; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-MMU-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR BioGRID-ORCS; 68652; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Tab2; mouse.
DR EvolutionaryTrace; Q99K90; -.
DR PRO; PR:Q99K90; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99K90; protein.
DR Bgee; ENSMUSG00000015755; Expressed in plantaris and 262 other tissues.
DR ExpressionAtlas; Q99K90; baseline and differential.
DR Genevisible; Q99K90; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR CDD; cd14362; CUE_TAB2_TAB3; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041911; TAB2/3_CUE.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Endosome; Lysosome; Membrane;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..693
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 2"
FT /id="PRO_0000225696"
FT DOMAIN 8..51
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 663..693
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 90..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..685
FT /note="Interaction with polyubiquitin"
FT /evidence="ECO:0000269|PubMed:19927120"
FT COILED 532..619
FT /evidence="ECO:0000255"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYJ8"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYJ8"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYJ8"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYJ8"
FT MUTAGEN 674
FT /note="T->A: Loss of interaction with 'Lys-63'-linked
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:19927120"
FT MUTAGEN 675
FT /note="F->A: Loss of interaction with 'Lys-63'-linked
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:19927120"
FT MUTAGEN 678
FT /note="H->Q: Loss of interaction with 'Lys-63'-linked
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:19927120"
FT MUTAGEN 681
FT /note="L->T: Loss of interaction with 'Lys-63'-linked
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:19927120"
FT MUTAGEN 685
FT /note="E->V: Loss of interaction with 'Lys-63'-linked
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:19927120"
FT MUTAGEN 686
FT /note="Q->I,M: Confers ability to bind monoubiquitin and
FT polyubiquitin, irrespective of the type of linkage."
FT /evidence="ECO:0000269|PubMed:19927120"
FT CONFLICT 183
FT /note="P -> T (in Ref. 3; BAE28166)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="V -> F (in Ref. 3; BAC40772)"
FT /evidence="ECO:0000305"
FT CONFLICT 580
FT /note="S -> L (in Ref. 3; BAE28166)"
FT /evidence="ECO:0000305"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:3A9J"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:3A9J"
SQ SEQUENCE 693 AA; 76442 MW; 810F17CBE6F80BA8 CRC64;
MAQGSHQIDF QVLHDLRQKF PEVPEVVVSR CMLQNNNNLD ACCAVLSQES TRYLYGEGDL
NFSDESGISG LRNHMTSLNL DLQSQNVYHH GREGSRVNGS RTLTHSVSDG QLHGGQSNNE
LFQQEPQTAP AQVPQGFNVF GMPSTSGASN STPHLGFHLG SKGTSNLSQQ TPRFNPIMVT
LAPNIQTGRS TPTSLHIHGV PPPVLNSPQG NSIYIRPYIT TPSGTARQTQ QHSGWVSQFN
PMNPQQAYQP SQPGPWTTYP ASNPLPHTST QQPNQQGHQT SHVYMPISSP TTPQPPTIHS
SGSSQSSAHS QYNIQNISTG PRKNQIEIKL EPPQRNSSSK LRSSGPRTAS TSSLVNSQTL
NRNQPTVYIA ASPPNTDEMI SRSQPKVYIS ANATAGDEQG MRNQPTLFIS TNSGPSAASR
NMSGQVSMGP AFIHHHPPKS RVLGGNSATS PRVVVTQPNT KYTFKITVSP NKPPAVSPGV
VSPTFELTNL LNHPDHYVET ENIQHLTDPA LAHVDRISEA RKLSMGSDDA AYTQALLVHQ
KARMERLQRE LEMQKKKLDK LKSEVNEMEN NLTRRRLKRS NSISQIPSLE EMQQLRSCNR
QLQIDIDCLT KEIDLFQARG PHFNPSAIHN FYDNIGFVGP VPPKPKDQRS TIKAPKTQDA
EDEEGAQWNC TACTFLNHPA LIRCEQCEMP RHF
