HAKAI_MOUSE
ID HAKAI_MOUSE Reviewed; 491 AA.
AC Q9JIY2; Q3TMC0; Q8C7W5; Q8VCL9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase Hakai {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:11836526};
DE AltName: Full=Casitas B-lineage lymphoma-transforming sequence-like protein 1 {ECO:0000303|PubMed:11836526};
DE Short=c-Cbl-like protein 1 {ECO:0000303|PubMed:11836526};
DE AltName: Full=E-cadherin binding protein E7;
DE AltName: Full=RING-type E3 ubiquitin transferase Hakai {ECO:0000305};
GN Name=Cbll1 {ECO:0000312|MGI:MGI:2144842};
GN Synonyms=Hakai {ECO:0000303|PubMed:11836526};
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] (ISOFORM 1), FUNCTION, INTERACTION WITH CDH1,
RP PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=11836526; DOI=10.1038/ncb758;
RA Fujita Y., Krause G., Scheffner M., Zechner D., Molina Leddy H.E.,
RA Behrens J., Sommer T., Birchmeier W.;
RT "Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the
RT E-cadherin complex.";
RL Nat. Cell Biol. 4:222-231(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and 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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Colon;
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 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 106-206, FUNCTION, DOMAIN HYB, AND
RP SUBUNIT.
RX PubMed=22252131; DOI=10.1038/emboj.2011.496;
RA Mukherjee M., Chow S.Y., Yusoff P., Seetharaman J., Ng C., Sinniah S.,
RA Koh X.W., Asgar N.F., Li D., Yim D., Jackson R.A., Yew J., Qian J., Iyu A.,
RA Lim Y.P., Zhou X., Sze S.K., Guy G.R., Sivaraman J.;
RT "Structure of a novel phosphotyrosine-binding domain in Hakai that targets
RT E-cadherin.";
RL EMBO J. 31:1308-1319(2012).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=29535189; DOI=10.1101/gad.309146.117;
RA Knuckles P., Lence T., Haussmann I.U., Jacob D., Kreim N., Carl S.H.,
RA Masiello I., Hares T., Villasenor R., Hess D., Andrade-Navarro M.A.,
RA Biggiogera M., Helm M., Soller M., Buehler M., Roignant J.Y.;
RT "Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-
RT binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d.";
RL Genes Dev. 32:415-429(2018).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE WMM COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=29547716; DOI=10.1016/j.molcel.2018.02.015;
RA Wen J., Lv R., Ma H., Shen H., He C., Wang J., Jiao F., Liu H., Yang P.,
RA Tan L., Lan F., Shi Y.G., He C., Shi Y., Diao J.;
RT "Zc3h13 regulates nuclear RNA m6A methylation and mouse embryonic stem cell
RT self-renewal.";
RL Mol. Cell 69:1028-1038(2018).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC several tyrosine-phosphorylated Src substrates, including CDH1, CTTN
CC and DOK1 (PubMed:11836526, PubMed:22252131). Targets CDH1 for
CC endocytosis and degradation (PubMed:11836526). Associated component of
CC the WMM complex, a complex that mediates N6-methyladenosine (m6A)
CC methylation of RNAs, a modification that plays a role in the efficiency
CC of mRNA splicing and RNA processing (PubMed:29535189, PubMed:29547716).
CC Its function in the WMM complex is unknown (PubMed:29535189,
CC PubMed:29547716). {ECO:0000269|PubMed:11836526,
CC ECO:0000269|PubMed:22252131, ECO:0000269|PubMed:29535189,
CC ECO:0000269|PubMed:29547716}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11836526};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:11836526}.
CC -!- SUBUNIT: Homodimer (PubMed:22252131). Interacts with tyrosine-
CC phosphorylated SRC substrates (PubMed:11836526, PubMed:22252131).
CC Component of the WMM complex, a N6-methyltransferase complex composed
CC of a catalytic subcomplex, named MAC, and of an associated subcomplex,
CC named MACOM (PubMed:29535189, PubMed:29547716). The MAC subcomplex is
CC composed of METTL3 and METTL14 (PubMed:29535189, PubMed:29547716). The
CC MACOM subcomplex is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and,
CC in some cases of RBM15 (RBM15 or RBM15B) (PubMed:29535189,
CC PubMed:29547716). Also a component of a MACOM-like complex, named WTAP
CC complex, composed of WTAP, ZC3H13, CBLL1, VIRMA, RBM15, BCLAF1 and
CC THRAP3 (By similarity). {ECO:0000250|UniProtKB:Q75N03,
CC ECO:0000269|PubMed:11836526, ECO:0000269|PubMed:22252131,
CC ECO:0000269|PubMed:29535189, ECO:0000269|PubMed:29547716}.
CC -!- INTERACTION:
CC Q9JIY2; Q9JIY2: Cbll1; NbExp=7; IntAct=EBI-7644904, EBI-7644904;
CC Q9JIY2; Q60598: Cttn; NbExp=4; IntAct=EBI-7644904, EBI-397955;
CC Q9JIY2; P12830: CDH1; Xeno; NbExp=21; IntAct=EBI-7644904, EBI-727477;
CC Q9JIY2; Q14247: CTTN; Xeno; NbExp=8; IntAct=EBI-7644904, EBI-351886;
CC Q9JIY2; Q99704: DOK1; Xeno; NbExp=2; IntAct=EBI-7644904, EBI-1384360;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q75N03}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm
CC {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction
CC located in the cytoplasm (PubMed:29547716). ZC3H13 is required to
CC anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus
CC (PubMed:29547716). {ECO:0000269|PubMed:29547716}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9JIY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JIY2-2; Sequence=VSP_024416;
CC Name=3;
CC IsoId=Q9JIY2-3; Sequence=VSP_024416, VSP_024418, VSP_024419;
CC Name=4;
CC IsoId=Q9JIY2-4; Sequence=VSP_024415, VSP_024417;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:11836526}.
CC -!- DOMAIN: The HYB domain forms a phosphotyrosine-binding pocket upon
CC dimerization, and mediates as well the recognition of its flanking
CC acidic amino acids. {ECO:0000269|PubMed:22252131}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:11836526}.
CC -!- SIMILARITY: Belongs to the Hakai family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE38522.1; Type=Frameshift; Evidence={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; AF167441; AAF89617.1; -; mRNA.
DR EMBL; AK049141; BAC33568.1; -; mRNA.
DR EMBL; AK166017; BAE38522.1; ALT_FRAME; mRNA.
DR EMBL; BC019529; AAH19529.1; -; mRNA.
DR CCDS; CCDS56834.1; -. [Q9JIY2-1]
DR CCDS; CCDS56835.1; -. [Q9JIY2-4]
DR CCDS; CCDS88321.1; -. [Q9JIY2-2]
DR RefSeq; NP_001240776.1; NM_001253847.1. [Q9JIY2-1]
DR RefSeq; NP_001240777.1; NM_001253848.1. [Q9JIY2-4]
DR RefSeq; NP_598809.1; NM_134048.2. [Q9JIY2-2]
DR PDB; 2MQ1; NMR; -; A=106-194.
DR PDB; 3VK6; X-ray; 1.90 A; A=106-206.
DR PDBsum; 2MQ1; -.
DR PDBsum; 3VK6; -.
DR AlphaFoldDB; Q9JIY2; -.
DR BMRB; Q9JIY2; -.
DR SMR; Q9JIY2; -.
DR BioGRID; 222714; 4.
DR ComplexPortal; CPX-1609; WMM N6-adenosine-methyltransferase complex.
DR IntAct; Q9JIY2; 26.
DR MINT; Q9JIY2; -.
DR STRING; 10090.ENSMUSP00000099038; -.
DR iPTMnet; Q9JIY2; -.
DR PhosphoSitePlus; Q9JIY2; -.
DR EPD; Q9JIY2; -.
DR MaxQB; Q9JIY2; -.
DR PaxDb; Q9JIY2; -.
DR PeptideAtlas; Q9JIY2; -.
DR PRIDE; Q9JIY2; -.
DR ProteomicsDB; 270933; -. [Q9JIY2-1]
DR ProteomicsDB; 270934; -. [Q9JIY2-2]
DR ProteomicsDB; 270935; -. [Q9JIY2-3]
DR ProteomicsDB; 270936; -. [Q9JIY2-4]
DR Antibodypedia; 17227; 208 antibodies from 30 providers.
DR DNASU; 104836; -.
DR Ensembl; ENSMUST00000101499; ENSMUSP00000099038; ENSMUSG00000020659. [Q9JIY2-1]
DR Ensembl; ENSMUST00000185739; ENSMUSP00000141007; ENSMUSG00000020659. [Q9JIY2-2]
DR Ensembl; ENSMUST00000188326; ENSMUSP00000139809; ENSMUSG00000020659. [Q9JIY2-4]
DR GeneID; 104836; -.
DR KEGG; mmu:104836; -.
DR UCSC; uc007nhl.2; mouse. [Q9JIY2-2]
DR UCSC; uc007nhm.2; mouse. [Q9JIY2-1]
DR UCSC; uc007nhn.2; mouse. [Q9JIY2-4]
DR CTD; 79872; -.
DR MGI; MGI:2144842; Cbll1.
DR VEuPathDB; HostDB:ENSMUSG00000020659; -.
DR eggNOG; KOG2932; Eukaryota.
DR GeneTree; ENSGT00510000047522; -.
DR HOGENOM; CLU_031291_1_0_1; -.
DR InParanoid; Q9JIY2; -.
DR OMA; EFDYNKE; -.
DR OrthoDB; 765364at2759; -.
DR PhylomeDB; Q9JIY2; -.
DR TreeFam; TF332910; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 104836; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Cbll1; mouse.
DR PRO; PR:Q9JIY2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9JIY2; protein.
DR Bgee; ENSMUSG00000020659; Expressed in rostral migratory stream and 251 other tissues.
DR ExpressionAtlas; Q9JIY2; baseline and differential.
DR Genevisible; Q9JIY2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0080009; P:mRNA methylation; ISO:MGI.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IBA:GO_Central.
DR CDD; cd16508; RING-HC_HAKAI_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040380; HAKAI-like_RING-HC.
DR InterPro; IPR040383; HAKAI/CBLL2.
DR InterPro; IPR041042; Znf_Hakai.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13480; PTHR13480; 1.
DR Pfam; PF18408; zf_Hakai; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..491
FT /note="E3 ubiquitin-protein ligase Hakai"
FT /id="PRO_0000284050"
FT ZN_FING 109..149
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 164..190
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..206
FT /note="HYB domain"
FT /evidence="ECO:0000269|PubMed:22252131"
FT REGION 255..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N03"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N03"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N03"
FT VAR_SEQ 58..61
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024415"
FT VAR_SEQ 61
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024416"
FT VAR_SEQ 277..431
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024417"
FT VAR_SEQ 311..374
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024418"
FT VAR_SEQ 398..409
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024419"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3VK6"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:3VK6"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:2MQ1"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3VK6"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3VK6"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:3VK6"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:3VK6"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3VK6"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3VK6"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3VK6"
SQ SEQUENCE 491 AA; 54444 MW; AD2A3C188781A7DA CRC64;
MDHTDNELQG TNSSGSLGGL DVRRRIPIKL ISKQASKVKP APRTQRTVSR MPAKAPQGDE
EGFDYNEEQR YDCKGGELFG NQRRFPGHLF WDFKINILGE KDDTPVHFCD KCGLPIKVYG
RMIPCKHVFC YDCAILHEKK GDKMCPGCSD PVQRIEQCTR GSLFMCSIVQ GCKRTYLSQR
DLQAHINHRH MRAGKPVTRA SLENVHPPIA PPPTDIPDRF IMPPDKHHMS HIPPKQHIMM
PPPPLQHVPH EHYNQPHEDI RAPPAELSMA PPPPRSVSQE TFRISTRKHS NLITVPIQDD
SSSGAREPPP PAPAPAHHHP EYQGQPVVSH PHHIMPPQQH YAPPPPPPPP ISHPMPHPPQ
AAGTPHLVYS QAPPPPMTSA PPPITPPPGH IIAQMPPYMN HPPPGPPPPQ HGGPPVTAPP
PHHYNPNSLP QFTEDQGTLS PPFTQPGGMS PGIWPAPRGP PPPPRMQGPP SQTPLPGPHH
PDQTRYRPYY Q
