PAXI1_MOUSE
ID PAXI1_MOUSE Reviewed; 1056 AA.
AC Q6NZQ4; Q9Z0W6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=PAX-interacting protein 1;
DE AltName: Full=PAX transactivation activation domain-interacting protein;
GN Name=Paxip1; Synonyms=Ptip;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH PAX2.
RC STRAIN=FVB/NJ;
RX PubMed=10908331; DOI=10.1093/nar/28.14.2741;
RA Lechner M.S., Levitan I., Dressler G.R.;
RT "PTIP, a novel BRCT domain-containing protein interacts with Pax2 and is
RT associated with active chromatin.";
RL Nucleic Acids Res. 28:2741-2751(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12588986; DOI=10.1128/mcb.23.5.1666-1673.2003;
RA Cho E.A., Prindle M.J., Dressler G.R.;
RT "BRCT domain-containing protein PTIP is essential for progression through
RT mitosis.";
RL Mol. Cell. Biol. 23:1666-1673(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17925232; DOI=10.1016/j.devcel.2007.09.004;
RA Patel S.R., Kim D., Levitan I., Dressler G.R.;
RT "The BRCT-domain containing protein PTIP links PAX2 to a histone H3, lysine
RT 4 methyltransferase complex.";
RL Dev. Cell 13:580-592(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PAGR1A.
RX PubMed=19124460; DOI=10.1074/jbc.m809158200;
RA Gong Z., Cho Y.-W., Kim J.-E., Ge K., Chen J.;
RT "Accumulation of Pax2 transactivation domain interaction protein (PTIP) at
RT sites of DNA breaks via RNF8-dependent pathway is required for cell
RT survival after DNA damage.";
RL J. Biol. Chem. 284:7284-7293(2009).
RN [7]
RP FUNCTION.
RX PubMed=19414588; DOI=10.1074/jbc.m109.002527;
RA Wu J., Prindle M.J., Dressler G.R., Yu X.;
RT "PTIP regulates 53BP1 and SMC1 at the DNA damage sites.";
RL J. Biol. Chem. 284:18078-18084(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-230, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [9]
RP FUNCTION.
RX PubMed=20671152; DOI=10.1126/science.1187942;
RA Daniel J.A., Santos M.A., Wang Z., Zang C., Schwab K.R., Jankovic M.,
RA Filsuf D., Chen H.T., Gazumyan A., Yamane A., Cho Y.W., Sun H.W., Ge K.,
RA Peng W., Nussenzweig M.C., Casellas R., Dressler G.R., Zhao K.,
RA Nussenzweig A.;
RT "PTIP promotes chromatin changes critical for immunoglobulin class switch
RT recombination.";
RL Science 329:917-923(2010).
RN [10]
RP FUNCTION, INTERACTION WITH PAGR1A, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=26744420; DOI=10.1101/gad.268797.115;
RA Starnes L.M., Su D., Pikkupeura L.M., Weinert B.T., Santos M.A., Mund A.,
RA Soria R., Cho Y.W., Pozdnyakova I., Kubec Hoejfeldt M., Vala A., Yang W.,
RA Lopez-Mendez B., Lee J.E., Peng W., Yuan J., Ge K., Montoya G.,
RA Nussenzweig A., Choudhary C., Daniel J.A.;
RT "A PTIP-PA1 subcomplex promotes transcription for IgH class switching
RT independently from the associated MLL3/MLL4 methyltransferase complex.";
RL Genes Dev. 30:149-163(2016).
CC -!- FUNCTION: Involved in DNA damage response and in transcriptional
CC regulation through histone methyltransferase (HMT) complexes such as
CC the MLL2/MLL3 complex. Plays a role in early development. In DNA damage
CC response is required for cell survival after ionizing radiation. In
CC vitro shown to be involved in the homologous recombination mechanism
CC for the repair of double-strand breaks (DSBs). Its localization to DNA
CC damage foci requires Rnf8 and Ube2n. Recruits Tp53bp1 to DNA damage
CC foci and, at least in particular repair processes, effective DNA damage
CC response appears to require the association with Tp53bp1 phosphorylated
CC by Atm. Together with Tp53bp1 regulates Atm association (By
CC similarity). Proposed to recruit Pagr1 to sites of DNA damage and the
CC Pagr1:Paxip1 complex is required for cell survival in response to DNA
CC damage independently of the MLL2/MLL3 complex. However, this function
CC has been questioned (PubMed:19124460, PubMed:26744420). Promotes
CC ubiquitination of PCNA following UV irradiation and may regulate
CC recruitment of polymerase eta and Rad51 to chromatin after DNA damage.
CC Proposed to be involved in transcriptional regulation by linking MLL-
CC containing histone methyltransferase (HMT) complexes to gene promoters
CC by interacting with promoter-bound transcription factors such as Pax2.
CC Associates with gene promoters that are known to be regulated by
CC Kmt2d/Mll2 (By similarity). During immunoglobulin class switching in
CC activated B-cells is involved in trimethylation of histone H3 at 'Lys-
CC 4' and in transcription initiation of downstream switch regions at the
CC immunoglobulin heavy-chain (Igh) locus; this function appears to
CC involve the recruitment of MLL-containing HMT complexes. Conflictingly,
CC its function in transcriptional regulation during immunoglobulin class
CC switching is reported to be independent of the MLL2/MLL3 complex
CC (PubMed:20671152, PubMed:26744420). {ECO:0000250,
CC ECO:0000269|PubMed:10908331, ECO:0000269|PubMed:12588986,
CC ECO:0000269|PubMed:17925232, ECO:0000269|PubMed:19124460,
CC ECO:0000269|PubMed:19414588, ECO:0000269|PubMed:20671152,
CC ECO:0000269|PubMed:26744420}.
CC -!- SUBUNIT: Interacts with the C-terminal transactivation domain of PAX2
CC (PubMed:10908331). Forms a constitutive complex with PAGR1
CC independently of the MLL2/MLL3 complex (PubMed:19124460,
CC PubMed:26744420). Interacts with TP53BP1 (when phosphorylated at the N-
CC terminus by ATM) (By similarity). Interacts with HLTF (By similarity).
CC Component of the KMT2 family MLL2/MLL3 complex (also named ASCOM
CC complex), at least composed of the HMTs KMT2D and/or KMT2C, the common
CC subunits ASH2L, RBBP5, WDR5 and DPY30, and the complex type-specific
CC subunits PAXIP1/PTIP, PAGR1, NCOA6 and KDM6A; required for the
CC association of PAGR1 with the MLL2/MLL3 complex (By similarity).
CC Interacts with NUPR1; this interaction prevents PAXIP1 inhibition of
CC PAX2 transcription factor activity (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZW49, ECO:0000269|PubMed:10908331,
CC ECO:0000269|PubMed:19124460, ECO:0000269|PubMed:26744420}.
CC -!- INTERACTION:
CC Q6NZQ4; Q99L02: Pagr1a; NbExp=11; IntAct=EBI-1395317, EBI-11667455;
CC Q6NZQ4; P32114: Pax2; NbExp=3; IntAct=EBI-1395317, EBI-1395232;
CC Q6NZQ4; P32114-2: Pax2; NbExp=2; IntAct=EBI-1395317, EBI-1395250;
CC Q6NZQ4; Q02650: Pax5; NbExp=3; IntAct=EBI-1395317, EBI-296260;
CC Q6NZQ4; Q9BTK6: PAGR1; Xeno; NbExp=5; IntAct=EBI-1395317, EBI-2372223;
CC Q6NZQ4; Q12888: TP53BP1; Xeno; NbExp=5; IntAct=EBI-1395317, EBI-396540;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10908331,
CC ECO:0000269|PubMed:19124460}. Chromosome
CC {ECO:0000250|UniProtKB:Q6ZW49}. Note=Localizes to DNA damage foci upon
CC ionizing radiation. {ECO:0000250|UniProtKB:Q6ZW49}.
CC -!- TISSUE SPECIFICITY: Expression detected in all tissues examined,
CC including brain stem, cerebellum, cortex, heart, spleen, kidney, liver,
CC thymus and lung. {ECO:0000269|PubMed:10908331}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic kidney and brain.
CC {ECO:0000269|PubMed:10908331}.
CC -!- DOMAIN: The BRCT 1 and 2 domains mediate the interaction with PAGR1A.
CC {ECO:0000269|PubMed:26744420}.
CC -!- DOMAIN: The BRCT 5 and 6 domains mediate the association with the
CC MLL2/MLL3 complex (PubMed:26744420). The BRCT 5 and 6 domains function
CC as a single module and are necessary and sufficient for in vitro
CC phospho-specific binding (substrates phosphorylated by the kinases
CC ataxia telangiectasia-mutated (ATM), ataxia telangiectasia and RAD3-
CC related (ATR) in response to gamma irradiation). In contrast, in vivo
CC two pairs of BRCT domains (3-6) bind to phosphorylated TP53BP1 much
CC more efficiently. {ECO:0000269|PubMed:26744420}.
CC -!- DISRUPTION PHENOTYPE: Mice are developmentally retarded, disorganized,
CC and embryonic lethal by 9.5 dpc. Mutant cells appear to replicate DNA
CC but show reduced levels of mitosis and widespread cell death by 8.5
CC dpc. DNA damage appears to precede nuclear condensation at 7 dpc.
CC Reduced levels of histone H3 methylated at 'Lys-4 in developing
CC tissues. {ECO:0000269|PubMed:12588986, ECO:0000269|PubMed:17925232}.
CC -!- CAUTION: The terminology of MLL proteins in mammalia is not consistent
CC also concerning the terminology of MLL protein-containing complexes.
CC The decribed MLL2/MLL3 complex is commonly described as MLL3/MLL4
CC complex in literature. {ECO:0000305}.
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DR EMBL; AF104261; AAD17923.1; -; mRNA.
DR EMBL; AK144606; BAE25965.1; -; mRNA.
DR EMBL; BC066014; AAH66014.1; -; mRNA.
DR CCDS; CCDS39039.1; -.
DR RefSeq; NP_061366.2; NM_018878.3.
DR AlphaFoldDB; Q6NZQ4; -.
DR SMR; Q6NZQ4; -.
DR BioGRID; 207754; 42.
DR IntAct; Q6NZQ4; 40.
DR MINT; Q6NZQ4; -.
DR STRING; 10090.ENSMUSP00000002291; -.
DR iPTMnet; Q6NZQ4; -.
DR PhosphoSitePlus; Q6NZQ4; -.
DR EPD; Q6NZQ4; -.
DR MaxQB; Q6NZQ4; -.
DR PaxDb; Q6NZQ4; -.
DR PeptideAtlas; Q6NZQ4; -.
DR PRIDE; Q6NZQ4; -.
DR ProteomicsDB; 287788; -.
DR Antibodypedia; 1874; 130 antibodies from 25 providers.
DR Ensembl; ENSMUST00000002291; ENSMUSP00000002291; ENSMUSG00000002221.
DR GeneID; 55982; -.
DR KEGG; mmu:55982; -.
DR UCSC; uc033iid.1; mouse.
DR CTD; 22976; -.
DR MGI; MGI:1890430; Paxip1.
DR VEuPathDB; HostDB:ENSMUSG00000002221; -.
DR eggNOG; KOG2043; Eukaryota.
DR GeneTree; ENSGT00940000155757; -.
DR HOGENOM; CLU_009382_0_0_1; -.
DR InParanoid; Q6NZQ4; -.
DR OMA; QGPNSIR; -.
DR OrthoDB; 840249at2759; -.
DR PhylomeDB; Q6NZQ4; -.
DR TreeFam; TF329580; -.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 55982; 29 hits in 118 CRISPR screens.
DR ChiTaRS; Paxip1; mouse.
DR PRO; PR:Q6NZQ4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6NZQ4; protein.
DR Bgee; ENSMUSG00000002221; Expressed in embryonic post-anal tail and 253 other tissues.
DR ExpressionAtlas; Q6NZQ4; baseline and differential.
DR Genevisible; Q6NZQ4; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0060717; P:chorion development; IMP:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:0000416; P:positive regulation of histone H3-K36 methylation; IMP:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:0045830; P:positive regulation of isotype switching; IMP:UniProtKB.
DR GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IMP:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.10190; -; 5.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR037886; Paxip1.
DR PANTHER; PTHR23196:SF31; PTHR23196:SF31; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF12738; PTCB-BRCT; 2.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00292; BRCT; 6.
DR SUPFAM; SSF52113; SSF52113; 5.
DR PROSITE; PS50172; BRCT; 5.
PE 1: Evidence at protein level;
KW Chromosome; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1056
FT /note="PAX-interacting protein 1"
FT /id="PRO_0000296263"
FT DOMAIN 8..93
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 94..183
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 588..681
FT /note="BRCT 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 688..776
FT /note="BRCT 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 853..934
FT /note="BRCT 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 955..989
FT /note="BRCT 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 94..183
FT /note="Interaction with PAGR1"
FT /evidence="ECO:0000269|PubMed:19124460,
FT ECO:0000269|PubMed:26744420"
FT REGION 188..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..1056
FT /note="Interaction with TP53BP1"
FT /evidence="ECO:0000250"
FT MOTIF 655..672
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 189..205
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1056 AA; 119269 MW; 86762841515A07AB CRC64;
MSEPAPEVPE ELFREVKYYA VGDIDPQVIQ LLKAGKAKEV SYNALASHII SEDGDNPEVG
EAREVFDLPV VKPSWVTLSV QCGALLPVNG FSPESCQIFF GLTACLSQVS SEDRSALWAL
VTFHGGSCQL NLNKKCTHLI VPEPKGEKYE RAVKRTSIKI VTPDWVLDCV SEKRRKDEAF
YHPRLIIYEE EEEEEEEGDN EEQDSQNEGS TEKSSVASSA VASPAEQPCS PKPRAEVSKG
ELMFDDSSDS SPEKQERSLN WAPAEAPPLN TAQRRLPQGK GPGLINLCAN VPPVPGDILP
PDMRGNLMAP GQNLQNSERS EILGTWSPAV RTLRNITNNA DIQQINRPSN VAHILQSLSA
PTKSLEQQVA RGQQGHPNAS AVLFGQAKGA PETHVLQQHH PPQQPQQQHP ALHLQPQIMQ
LQQQQQQQQQ QQQQPQPYPQ PPSHQFPQQV HQHQFSQQQL QFPQQPLHPQ QQLHRPQQQL
QPFQQQHALQ QQLHQLQQQQ LQHHQLAQLQ QQQQQQHNLL QQQQQQQQLQ RLQQQQQMQN
QAAHLSQASQ ALQHQVLPQQ PLQLSLQPPP QQQQQQQLFG HDPAVEIPEE SFLLGCVFAI
ADYPEQMSDK QLLATWKRII QAHGGTVDPT FTSRCTHLLC ASQVSSMYTQ ALRERKRCVT
AHWLNTVLKK KKLMPPHRAL HFPVAFPPGG KPCSQHIISV TGFVDNDRDD LKLMAYLAGA
KYTGYLCRSN TVLICKEPSG LKYEKAKEWR IPCVNAQWLG DILLGNFEAL RQVQYSRYTA
FNMPDPFVPT PHLVLGLLDA WRTPVKVTAE LLMGVRLPPK LKPNEVANIQ PSSKRARIED
LPPPTKKLTP ELTPLVLFTG FEPVQVQQYI KKLYILGGEV AECTKKCTHL IASKVTRTVK
FLTAISVVKH IVTPDWLEEC FKRQTFIDEQ NYILRDAEAE VLFSFSLEES LKRAHVSPLF
KTKYFYITPG ICPSLATMKA IVECAGGKVL AKQPSFRKLM EHKQNKSLSE IILISCENDL
HLCREYFARG IDVHNAEFVL TGVLTQTLDY ESYKFN
