NOL9_HUMAN
ID NOL9_HUMAN Reviewed; 702 AA.
AC Q5SY16; Q2NL84; Q4VBY3; Q6P472; Q7L4D6; Q96EE0; Q9H5L4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Polynucleotide 5'-hydroxyl-kinase NOL9;
DE EC=2.7.1.-;
DE AltName: Full=Nucleolar protein 9;
GN Name=NOL9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-10; ARG-50 AND
RP ALA-58.
RC TISSUE=Amygdala, and Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TRP-10; ARG-50 AND
RP ALA-58.
RC TISSUE=Kidney, Lymph, Ovary, and Skin;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, ATP-BINDING, RNA-BINDING, AND MUTAGENESIS
RP OF LYS-312 AND SER-313.
RX PubMed=21063389; DOI=10.1038/emboj.2010.275;
RA Heindl K., Martinez J.;
RT "Nol9 is a novel polynucleotide 5'-kinase involved in ribosomal RNA
RT processing.";
RL EMBO J. 29:4161-4171(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-485, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. The
CC kinase activity is required for the processing of the 32S precursor
CC into 5.8S and 28S rRNAs, more specifically for the generation of the
CC major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase
CC activities. Probably binds RNA. {ECO:0000269|PubMed:21063389}.
CC -!- SUBUNIT: Interacts with PELP1, WDR18 and SENP3. {ECO:0000250}.
CC -!- INTERACTION:
CC Q5SY16; Q09666-2: AHNAK; NbExp=3; IntAct=EBI-1055462, EBI-10245106;
CC Q5SY16; P53041: PPP5C; NbExp=2; IntAct=EBI-1055462, EBI-716663;
CC Q5SY16; Q04864: REL; NbExp=3; IntAct=EBI-1055462, EBI-307352;
CC Q5SY16; P15884: TCF4; NbExp=3; IntAct=EBI-1055462, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:21063389}.
CC Note=Colocalizes with pre-60S rRNP particles.
CC -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK026976; BAB15611.1; ALT_INIT; mRNA.
DR EMBL; AK289653; BAF82342.1; -; mRNA.
DR EMBL; AL591866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009257; AAH09257.2; -; mRNA.
DR EMBL; BC012439; AAH12439.1; -; mRNA.
DR EMBL; BC063639; AAH63639.1; -; mRNA.
DR EMBL; BC094836; AAH94836.1; -; mRNA.
DR EMBL; BC105095; AAI05096.1; -; mRNA.
DR EMBL; BC110849; AAI10850.1; -; mRNA.
DR EMBL; BC112278; AAI12279.1; -; mRNA.
DR CCDS; CCDS80.1; -.
DR RefSeq; NP_078930.3; NM_024654.4.
DR RefSeq; XP_011540449.1; XM_011542147.2.
DR RefSeq; XP_016857827.1; XM_017002338.1.
DR RefSeq; XP_016857828.1; XM_017002339.1.
DR AlphaFoldDB; Q5SY16; -.
DR SMR; Q5SY16; -.
DR BioGRID; 122825; 133.
DR CORUM; Q5SY16; -.
DR IntAct; Q5SY16; 50.
DR MINT; Q5SY16; -.
DR STRING; 9606.ENSP00000366934; -.
DR iPTMnet; Q5SY16; -.
DR PhosphoSitePlus; Q5SY16; -.
DR SwissPalm; Q5SY16; -.
DR BioMuta; NOL9; -.
DR DMDM; 73921242; -.
DR SWISS-2DPAGE; Q5SY16; -.
DR EPD; Q5SY16; -.
DR jPOST; Q5SY16; -.
DR MassIVE; Q5SY16; -.
DR MaxQB; Q5SY16; -.
DR PaxDb; Q5SY16; -.
DR PeptideAtlas; Q5SY16; -.
DR PRIDE; Q5SY16; -.
DR ProteomicsDB; 64010; -.
DR Antibodypedia; 53093; 59 antibodies from 24 providers.
DR DNASU; 79707; -.
DR Ensembl; ENST00000377705.6; ENSP00000366934.5; ENSG00000162408.11.
DR GeneID; 79707; -.
DR KEGG; hsa:79707; -.
DR MANE-Select; ENST00000377705.6; ENSP00000366934.5; NM_024654.5; NP_078930.4.
DR UCSC; uc001ans.4; human.
DR CTD; 79707; -.
DR DisGeNET; 79707; -.
DR GeneCards; NOL9; -.
DR HGNC; HGNC:26265; NOL9.
DR HPA; ENSG00000162408; Low tissue specificity.
DR neXtProt; NX_Q5SY16; -.
DR OpenTargets; ENSG00000162408; -.
DR PharmGKB; PA142671256; -.
DR VEuPathDB; HostDB:ENSG00000162408; -.
DR eggNOG; KOG2750; Eukaryota.
DR GeneTree; ENSGT00940000153668; -.
DR HOGENOM; CLU_021128_2_0_1; -.
DR OMA; CLYGQVE; -.
DR OrthoDB; 1217334at2759; -.
DR PhylomeDB; Q5SY16; -.
DR TreeFam; TF313802; -.
DR PathwayCommons; Q5SY16; -.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q5SY16; -.
DR SIGNOR; Q5SY16; -.
DR BioGRID-ORCS; 79707; 717 hits in 1088 CRISPR screens.
DR ChiTaRS; NOL9; human.
DR GeneWiki; NOL9; -.
DR GenomeRNAi; 79707; -.
DR Pharos; Q5SY16; Tdark.
DR PRO; PR:Q5SY16; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SY16; protein.
DR Bgee; ENSG00000162408; Expressed in tibialis anterior and 212 other tissues.
DR Genevisible; Q5SY16; HS.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; TAS:UniProtKB.
DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045116; Clp1/Grc3.
DR InterPro; IPR032319; CLP1_P.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12755; PTHR12755; 1.
DR Pfam; PF16575; CLP1_P; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Isopeptide bond; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..702
FT /note="Polynucleotide 5'-hydroxyl-kinase NOL9"
FT /id="PRO_0000096939"
FT REGION 69..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 306..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 10
FT /note="R -> W (in dbSNP:rs4908923)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054777"
FT VARIANT 50
FT /note="W -> R (in dbSNP:rs6693400)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054778"
FT VARIANT 58
FT /note="S -> A (in dbSNP:rs6693391)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054779"
FT VARIANT 420
FT /note="I -> V (in dbSNP:rs17029613)"
FT /id="VAR_056955"
FT MUTAGEN 312
FT /note="K->A: Abolishes kinase activity and rRNA
FT processing."
FT /evidence="ECO:0000269|PubMed:21063389"
FT MUTAGEN 313
FT /note="S->A: Abolishes kinase activity and rRNA
FT processing."
FT /evidence="ECO:0000269|PubMed:21063389"
SQ SEQUENCE 702 AA; 79323 MW; 5D42AF5F7F292997 CRC64;
MADSGLLLKR GSCRSTWLRV RKARPQLILS RRPRRRLGSL RWCGRRRLRW RLLQAQASGV
DWREGARQVS RAAAARRPNT ATPSPIPSPT PASEPESEPE LESASSCHRP LLIPPVRPVG
PGRALLLLPV EQGFTFSGIC RVTCLYGQVQ VFGFTISQGQ PAQDIFSVYT HSCLSIHALH
YSQPEKSKKE LKREARNLLK SHLNLDDRRW SMQNFSPQCS IVLLEHLKTA TVNFITSYPG
SSYIFVQESP TPQIKPEYLA LRSVGIRREK KRKGLQLTES TLSALEELVN VSCEEVDGCP
VILVCGSQDV GKSTFNRYLI NHLLNSLPCV DYLECDLGQT EFTPPGCISL LNITEPVLGP
PFTHLRTPQK MVYYGKPSCK NNYENYIDIV KYVFSAYKRE SPLIVNTMGW VSDQGLLLLI
DLIRLLSPSH VVQFRSDHSK YMPDLTPQYV DDMDGLYTKS KTKMRNRRFR LAAFADALEF
ADEEKESPVE FTGHKLIGVY TDFAFRITPR NRESHNKILR DLSILSYLSQ LQPPMPKPLS
PLHSLTPYQV PFNAVALRIT HSDVAPTHIL YAVNASWVGL CKIQDDVRGY TNGPILLAQT
PICDCLGFGI CRGIDMEKRL YHILTPVPPE ELRTVNCLLV GAIAIPHCVL KCQRGIEGTV
PYVTTDYNFK LPGASEKIGA REPEEAHKEK PYRRPKFCRK MK
