NCOA2_RAT
ID NCOA2_RAT Reviewed; 1465 AA.
AC Q9WUI9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Nuclear receptor coactivator 2;
DE Short=NCoA-2;
DE AltName: Full=Transcriptional intermediary factor 2;
GN Name=Ncoa2; Synonyms=Tif2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9742117; DOI=10.1128/mcb.18.10.6001;
RA Leers J., Treuter E., Gustafsson J.-A.;
RT "Mechanistic principles in NR box-dependent interaction between nuclear
RT hormone receptors and the coactivator TIF2.";
RL Mol. Cell. Biol. 18:6001-6013(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-493; SER-499 AND
RP SER-699, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC receptors. Coactivator of the steroid binding domain (AF-2) but not of
CC the modulating N-terminal domain (AF-1). Required with NCOA1 to control
CC energy balance between white and brown adipose tissues. Critical
CC regulator of glucose metabolism regulation, acts as RORA coactivator to
CC specifically modulate G6PC1 expression. Involved in the positive
CC regulation of the transcriptional activity of the glucocorticoid
CC receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the
CC circadian clock by acting as a transcriptional coactivator for the
CC CLOCK-ARNTL/BMAL1 heterodimer. {ECO:0000250|UniProtKB:Q15596,
CC ECO:0000250|UniProtKB:Q61026}.
CC -!- SUBUNIT: Present in a complex containing NCOA3, IKKA, IKKB, IKBKG and
CC CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with ESR1,
CC HIF1A, NCOA1, APEX1, NR3C1, NR3C2, CARM1, RARA, and RXRA. Present in a
CC complex containing CARM1 and EP300/P300. Interacts with CASP8AP2 and
CC TTLL5/STAMP. Interacts with PSMB9 and DDX5. Interacts (via LXXLL 1, 2
CC and 3 motifs) with RORA and RORC (via AF-2 motif). Interacts with
CC RWDD3. Interacts with CLOCK and ARNTL/BMAL1. Interacts with NR4A3;
CC potentiates the activity of the NR4A3 (By similarity). Interacts with
CC NR1H3 (By similarity). {ECO:0000250|UniProtKB:Q15596,
CC ECO:0000250|UniProtKB:Q61026}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15596}.
CC -!- DOMAIN: Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors and
CC are, at least in part, functionally redundant.
CC {ECO:0000250|UniProtKB:Q15596}.
CC -!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional coactivation
CC and CREBBP/CBP binding. {ECO:0000250|UniProtKB:Q15596}.
CC -!- DOMAIN: Contains 2 C-terminal transcription activation domains (AD1 and
CC AD2) that can function independently. {ECO:0000250|UniProtKB:Q15596}.
CC -!- PTM: Acetylated. Deacetylation at Lys-780 by SIRT6 stimulates its
CC ability to coactivate PPARA. {ECO:0000250|UniProtKB:Q61026}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
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DR EMBL; AF136943; AAD24587.1; -; mRNA.
DR RefSeq; NP_114010.1; NM_031822.1.
DR PDB; 1XLS; X-ray; 2.96 A; I/J/K/L/M/N/O/P=740-756.
DR PDB; 3HLV; X-ray; 3.00 A; C/D=686-698.
DR PDB; 3HM1; X-ray; 2.33 A; C/D=686-698.
DR PDB; 3L03; X-ray; 1.90 A; C/D=686-698.
DR PDBsum; 1XLS; -.
DR PDBsum; 3HLV; -.
DR PDBsum; 3HM1; -.
DR PDBsum; 3L03; -.
DR AlphaFoldDB; Q9WUI9; -.
DR SMR; Q9WUI9; -.
DR STRING; 10116.ENSRNOP00000011026; -.
DR iPTMnet; Q9WUI9; -.
DR PhosphoSitePlus; Q9WUI9; -.
DR PaxDb; Q9WUI9; -.
DR PRIDE; Q9WUI9; -.
DR GeneID; 83724; -.
DR KEGG; rno:83724; -.
DR UCSC; RGD:620108; rat.
DR CTD; 10499; -.
DR RGD; 620108; Ncoa2.
DR eggNOG; KOG3561; Eukaryota.
DR InParanoid; Q9WUI9; -.
DR PhylomeDB; Q9WUI9; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR Reactome; R-RNO-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-RNO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR EvolutionaryTrace; Q9WUI9; -.
DR PRO; PR:Q9WUI9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:RGD.
DR GO; GO:0033142; F:nuclear progesterone receptor binding; IPI:RGD.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:RGD.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:RGD.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0045475; P:locomotor rhythm; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045925; P:positive regulation of female receptivity; IMP:RGD.
DR GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010906; P:regulation of glucose metabolic process; ISO:RGD.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032570; P:response to progesterone; ISO:RGD.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.20; -; 1.
DR IDEAL; IID50249; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR028822; NCOA2.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR014935; SRC/p160_LXXLL.
DR PANTHER; PTHR10684; PTHR10684; 1.
DR PANTHER; PTHR10684:SF2; PTHR10684:SF2; 1.
DR Pfam; PF07469; DUF1518; 1.
DR Pfam; PF16279; DUF4927; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Biological rhythms; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CHAIN 2..1465
FT /note="Nuclear receptor coactivator 2"
FT /id="PRO_0000094404"
FT DOMAIN 26..83
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 119..183
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..743
FT /note="CASP8AP2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT REGION 730..1121
FT /note="Interaction with ARNTL"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT REGION 1052..1075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 641..645
FT /note="LXXLL motif 1"
FT MOTIF 690..694
FT /note="LXXLL motif 2"
FT MOTIF 745..749
FT /note="LXXLL motif 3"
FT MOTIF 878..882
FT /note="LXXLL motif 4"
FT MOTIF 1079..1087
FT /note="LLXXLXXXL motif"
FT COMPBIAS 11..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 338
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 636
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 785
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 864
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 874
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 1173
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1177
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1190
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1196
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1203
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1221
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1240
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 1261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT MOD_RES 1266
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 705
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT CROSSLNK 1455
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15596"
FT HELIX 689..695
FT /evidence="ECO:0007829|PDB:3L03"
FT HELIX 744..748
FT /evidence="ECO:0007829|PDB:1XLS"
SQ SEQUENCE 1465 AA; 159436 MW; 36625B573EB0B39C CRC64;
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRSTEKRNRE QENKYIEELA ELIFANFNDI
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSM
VNGGSWTGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE
EGEDKQSCLI CVARRVPMKE RPALPSSESF TTRQDLQGKI TFLDTSTMRD AMKPGWEDLV
RRCIQKFHTQ HEGESLSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT
TNEPQLVISI HMLHREQNVC VMNPDLTGQA MGKPLSPMSS SSPARQAMCS GNPGQDVALG
SNMNFPMNGP REQMSMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGLNPG
QPSSVLSPRH RMSPGVAGSP RVPPSQFSPA GSLHSPAGVC SSTGNSHSYT NSSLNALQAL
SEGHGVSLGP SLASPDLKMG NSQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
QASCHPEEQK RPNDSSMPQA ASEDRAEGHS RLHESKGQTK LLQLLTTKSD QMEPSPLPSS
LSDTNKDSTG SLPGPGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKELNQESS
GTAPGSEVTV KQEPASPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK
LIAMKTVKEE VSFEPSDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP TGSVDKQAII
NDLMQLTADS SPVTPVGAQK AALRMSQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
PFPPIRNSSP YSVIPQPGMM GNQGMLGSQG NLGNNSTGMI GSSTSRSSMP SGEWAPQSPA
VRVTCAATTG AMNRPIQGGM IRNPTASIPM RANSQPGQRQ MLQPQVMNIG PSELEMNMGG
PQYNQQQAPP NQTAPWPESI LPIDQASFGS QNRHPFGSSP DDLLCPHPAA ESPSDEGALL
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ ESSMMLEQKP PVFPQQYASQ
TQMAQGSYNP MQDPNFHTMG QRPNYTTLRM QPRPGLRPTG IVQNQPNQLR LQLQHRLQAQ
QNRQPLMNQI SGVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ
RTLMMRGQGL NMTPSMVAPT GLPAAMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT
PQSPLMSPRM AHTQSPMMQQ SQANPAYQPA SDINGWAQGS MGGNSMFSQQ SPPHFGQQAN
TSMYNNNMNI NVSMATNTAG LSNMNQMTGQ MSMTSVTSVP TSGLSSMGPE QVNDPALRGS
SLFTTNQLPG MDMIKQEGDG SRKYC
