P63_RAT
ID P63_RAT Reviewed; 680 AA.
AC Q9JJP6; Q99JD6; Q99JD7; Q99JD8; Q99JD9; Q99JE0; Q99JE1; Q99JE2; Q99JE3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Tumor protein 63;
DE Short=p63;
DE AltName: Full=Keratinocyte transcription factor KET;
DE AltName: Full=Transformation-related protein 63;
DE Short=TP63;
DE AltName: Full=Tumor protein p73-like;
DE Short=p73L;
GN Name=Tp63; Synonyms=Ket, P63, Tp73l, Trp63;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Tongue epithelium;
RX PubMed=9315105; DOI=10.1038/sj.onc.1201500;
RA Schmale H., Bamberger C.;
RT "A novel protein with strong homology to the tumor suppressor p53.";
RL Oncogene 15:1363-1367(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9), FUNCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Tongue;
RX PubMed=11470269; DOI=10.1016/s0014-5793(01)02643-6;
RA Bamberger C., Schmale H.;
RT "Identification and tissue distribution of novel KET/p63 splice variants.";
RL FEBS Lett. 501:121-126(2001).
CC -!- FUNCTION: Acts as a sequence specific DNA binding transcriptional
CC activator or repressor. The isoforms contain a varying set of
CC transactivation and auto-regulating transactivation inhibiting domains
CC thus showing an isoform specific activity. May be required in
CC conjunction with TP73/p73 for initiation of p53/TP53 dependent
CC apoptosis in response to genotoxic insults and the presence of
CC activated oncogenes. Involved in Notch signaling by probably inducing
CC JAG1 and JAG2. Activates RIPK4 transcription (By similarity). Plays a
CC role in the regulation of epithelial morphogenesis. The ratio of
CC DeltaN-type and TA*-type isoforms may govern the maintenance of
CC epithelial stem cell compartments and regulate the initiation of
CC epithelial stratification from the undifferentiated embryonal ectoderm.
CC Required for limb formation from the apical ectodermal ridge. Activates
CC transcription of the p21 promoter (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11470269}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Binds DNA as a homotetramer. Isoform composition of the
CC tetramer may determine transactivation activity. Interacts with HIPK2.
CC Interacts with SSRP1, leading to stimulate coactivator activity.
CC Interacts with WWP1. Interacts with PDS5A. Interacts (via activation
CC domain) with NOC2L (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=TA2-alpha;
CC IsoId=Q9JJP6-1; Sequence=Displayed;
CC Name=2; Synonyms=DeltaN-alpha;
CC IsoId=Q9JJP6-2; Sequence=VSP_012475;
CC Name=3; Synonyms=TA2-beta;
CC IsoId=Q9JJP6-3; Sequence=VSP_012478;
CC Name=4; Synonyms=DeltaN-beta;
CC IsoId=Q9JJP6-4; Sequence=VSP_012475, VSP_012478;
CC Name=5; Synonyms=TA2-gamma;
CC IsoId=Q9JJP6-5; Sequence=VSP_012477;
CC Name=6; Synonyms=DeltaN-gamma;
CC IsoId=Q9JJP6-6; Sequence=VSP_012475, VSP_012477;
CC Name=7; Synonyms=TA1-alpha;
CC IsoId=Q9JJP6-7; Sequence=VSP_012476;
CC Name=8; Synonyms=TA1-beta;
CC IsoId=Q9JJP6-8; Sequence=VSP_012476, VSP_012478;
CC Name=9; Synonyms=TA1-gamma;
CC IsoId=Q9JJP6-9; Sequence=VSP_012476, VSP_012477;
CC -!- TISSUE SPECIFICITY: Widely expressed, notably in thymus, prostate,
CC placenta, and skeletal muscle, although the precise isoform varies
CC according to tissue type. Progenitor cell layers of skin, breast and
CC prostate express high levels of DeltaN-type isoforms.
CC {ECO:0000269|PubMed:11470269, ECO:0000269|PubMed:9315105}.
CC -!- DOMAIN: The transactivation inhibitory domain (TID) can interact with,
CC and inhibit the activity of the N-terminal transcriptional activation
CC domain of TA*-type isoforms. {ECO:0000250}.
CC -!- PTM: May be sumoylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
CC proteasomal degradation of this protein (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform
CC 2. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing of isoform
CC 7. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform
CC 7. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
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DR EMBL; Y10258; CAB88216.1; -; mRNA.
DR EMBL; AJ277446; CAC37098.1; -; mRNA.
DR EMBL; AJ277447; CAC37099.1; -; mRNA.
DR EMBL; AJ277448; CAC37100.1; -; mRNA.
DR EMBL; AJ277449; CAC37101.1; -; mRNA.
DR EMBL; AJ277450; CAC37102.1; -; mRNA.
DR EMBL; AJ277451; CAC37103.1; -; mRNA.
DR EMBL; AJ277452; CAC37104.1; -; mRNA.
DR EMBL; AJ277453; CAC37105.1; -; mRNA.
DR RefSeq; NP_001120811.1; NM_001127339.1. [Q9JJP6-3]
DR RefSeq; NP_001120813.1; NM_001127341.1. [Q9JJP6-5]
DR RefSeq; NP_001120814.1; NM_001127342.1. [Q9JJP6-2]
DR RefSeq; NP_001120815.1; NM_001127343.1. [Q9JJP6-4]
DR RefSeq; NP_001120816.1; NM_001127344.1. [Q9JJP6-6]
DR RefSeq; NP_062094.1; NM_019221.3. [Q9JJP6-1]
DR RefSeq; XP_008767013.1; XM_008768791.2. [Q9JJP6-1]
DR AlphaFoldDB; Q9JJP6; -.
DR BMRB; Q9JJP6; -.
DR SMR; Q9JJP6; -.
DR STRING; 10116.ENSRNOP00000033463; -.
DR PhosphoSitePlus; Q9JJP6; -.
DR PaxDb; Q9JJP6; -.
DR Ensembl; ENSRNOT00000002636; ENSRNOP00000002636; ENSRNOG00000001924. [Q9JJP6-2]
DR Ensembl; ENSRNOT00000036179; ENSRNOP00000032308; ENSRNOG00000001924. [Q9JJP6-5]
DR Ensembl; ENSRNOT00000067251; ENSRNOP00000059178; ENSRNOG00000001924. [Q9JJP6-3]
DR Ensembl; ENSRNOT00000068116; ENSRNOP00000061884; ENSRNOG00000001924. [Q9JJP6-1]
DR GeneID; 246334; -.
DR KEGG; rno:246334; -.
DR CTD; 8626; -.
DR RGD; 620863; Tp63.
DR eggNOG; ENOG502QQ48; Eukaryota.
DR GeneTree; ENSGT00950000183153; -.
DR HOGENOM; CLU_019621_1_1_1; -.
DR InParanoid; Q9JJP6; -.
DR OMA; IRMQDSE; -.
DR OrthoDB; 257530at2759; -.
DR PhylomeDB; Q9JJP6; -.
DR TreeFam; TF106101; -.
DR Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR PRO; PR:Q9JJP6; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001924; Expressed in esophagus and 7 other tissues.
DR Genevisible; Q9JJP6; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003684; F:damaged DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0050699; F:WW domain binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0060197; P:cloacal septation; ISO:RGD.
DR GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR GO; GO:0007499; P:ectoderm and mesoderm interaction; ISO:RGD.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0009913; P:epidermal cell differentiation; ISO:RGD.
DR GO; GO:0010481; P:epidermal cell division; ISO:RGD.
DR GO; GO:0008544; P:epidermis development; ISO:RGD.
DR GO; GO:0002064; P:epithelial cell development; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0001736; P:establishment of planar polarity; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0048807; P:female genitalia morphogenesis; ISO:RGD.
DR GO; GO:0001942; P:hair follicle development; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISO:RGD.
DR GO; GO:2000381; P:negative regulation of mesoderm development; ISO: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:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:RGD.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:1904674; P:positive regulation of somatic stem cell population maintenance; ISO:RGD.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0036342; P:post-anal tail morphogenesis; ISO:RGD.
DR GO; GO:0030850; P:prostate gland development; ISO:RGD.
DR GO; GO:0060513; P:prostatic bud formation; ISO:RGD.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0098773; P:skin epidermis development; ISO:RGD.
DR GO; GO:0043589; P:skin morphogenesis; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; ISO:RGD.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0048485; P:sympathetic nervous system development; ISO:RGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd08367; P53; 1.
DR CDD; cd09572; SAM_tumor-p63; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR011615; p53_DNA-bd.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR010991; p53_tetrameristn.
DR InterPro; IPR002117; p53_tumour_suppressor.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR032645; Tp63.
DR InterPro; IPR037611; Tumor-p63_SAM.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR PANTHER; PTHR11447:SF8; PTHR11447:SF8; 1.
DR Pfam; PF00870; P53; 1.
DR Pfam; PF07710; P53_tetramer; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR00386; P53SUPPRESSR.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47719; SSF47719; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative promoter usage; Alternative splicing; Apoptosis;
KW Developmental protein; DNA-binding; Isopeptide bond; Metal-binding;
KW Notch signaling pathway; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..680
FT /note="Tumor protein 63"
FT /id="PRO_0000185731"
FT DOMAIN 541..607
FT /note="SAM"
FT DNA_BIND 170..362
FT /evidence="ECO:0000250"
FT REGION 1..107
FT /note="Transcription activation"
FT /evidence="ECO:0000250"
FT REGION 122..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..388
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT REGION 394..443
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 436..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..680
FT /note="Transactivation inhibition"
FT /evidence="ECO:0000250"
FT COMPBIAS 122..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..108
FT /note="MNFETSRCATLQYCPDPYIQRFIETPSHFSWKESYYRSAMSQSTQTSEFLSP
FT EVFQHIWDFLEQPICSVQPIDLNFVDEPSENGATNKIEISMDCIRMQDSDLSDPMW ->
FT MLYLESNAQTQFSE (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:11470269"
FT /id="VSP_012475"
FT VAR_SEQ 1..21
FT /note="MNFETSRCATLQYCPDPYIQR -> MPSC (in isoform 7, isoform
FT 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11470269"
FT /id="VSP_012476"
FT VAR_SEQ 450..680
FT /note="QTSMQSQSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTMPEGMGA
FT NIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSS
FT CLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHDFSSPPHLLRT
FT PSGASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDSRRNKQQRIKEE
FT GE -> HLLSACFRNELVESRREAPTQSDVFFRHSNPPNHSVYP (in isoform 5,
FT isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:11470269"
FT /id="VSP_012477"
FT VAR_SEQ 551..680
FT /note="SFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGIL
FT DHRQLHDFSSPPHLLRTPSGASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDF
FT NFDMDSRRNKQQRIKEEGE -> RIWQV (in isoform 3, isoform 4 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:11470269"
FT /id="VSP_012478"
SQ SEQUENCE 680 AA; 76760 MW; AC45DABB88F61400 CRC64;
MNFETSRCAT LQYCPDPYIQ RFIETPSHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD
FLEQPICSVQ PIDLNFVDEP SENGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNGM
DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS
FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV
VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT
TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR
KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES
LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ
LINPQQRNAL TPTTMPEGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP
PPYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG
ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND
FNFDMDSRRN KQQRIKEEGE
