PR15B_HUMAN
ID PR15B_HUMAN Reviewed; 713 AA.
AC Q5SWA1; Q53GQ4; Q658M2; Q6P156; Q96SN1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein phosphatase 1 regulatory subunit 15B;
GN Name=PPP1R15B;
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 VARIANT SER-308.
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 MRNA], AND VARIANT SER-308.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-308 AND GLU-589.
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 307-713, AND VARIANT SER-308.
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH PP1.
RX PubMed=15705855; DOI=10.1126/science.1101902;
RA Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D.,
RA Kaufman R.J., Ma D., Coen D.M., Ron D., Yuan J.;
RT "A selective inhibitor of eIF2alpha dephosphorylation protects cells from
RT ER stress.";
RL Science 307:935-939(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205 AND SER-508, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP INVOLVEMENT IN MSSGM2, VARIANT MSSGM2 CYS-658, CHARACTERIZATION OF VARIANT
RP MSSGM2 CYS-658, AND FUNCTION.
RX PubMed=26159176; DOI=10.2337/db15-0477;
RA Abdulkarim B., Nicolino M., Igoillo-Esteve M., Daures M., Romero S.,
RA Philippi A., Senee V., Lopes M., Cunha D.A., Harding H.P., Derbois C.,
RA Bendelac N., Hattersley A.T., Eizirik D.L., Ron D., Cnop M., Julier C.;
RT "A missense mutation in PPP1R15B causes a syndrome including diabetes,
RT short stature and microcephaly.";
RL Diabetes 64:3951-3962(2015).
RN [10]
RP INVOLVEMENT IN MSSGM2, VARIANT MSSGM2 CYS-658, CHARACTERIZATION OF VARIANT
RP MSSGM2 CYS-658, AND FUNCTION.
RX PubMed=26307080; DOI=10.1093/hmg/ddv337;
RG Care4Rare Canada Consortium;
RA Kernohan K.D., Tetreault M., Liwak-Muir U., Geraghty M.T., Qin W.,
RA Venkateswaran S., Davila J., Holcik M., Majewski J., Richer J.,
RA Boycott K.M.;
RT "Homozygous mutation in the eukaryotic translation initiation factor 2alpha
RT phosphatase gene, PPP1R15B, is associated with severe microcephaly, short
RT stature and intellectual disability.";
RL Hum. Mol. Genet. 24:6293-6300(2015).
RN [11]
RP VARIANT SER-134.
RX PubMed=28493397; DOI=10.1002/humu.23246;
RG UK10K;
RA Rainger J., Williamson K.A., Soares D.C., Truch J., Kurian D.,
RA Gillessen-Kaesbach G., Seawright A., Prendergast J., Halachev M.,
RA Wheeler A., McTeir L., Gill A.C., van Heyningen V., Davey M.G.,
RA FitzPatrick D.R.;
RT "A recurrent de novo mutation in ACTG1 causes isolated ocular coloboma.";
RL Hum. Mutat. 38:942-946(2017).
CC -!- FUNCTION: Maintains low levels of EIF2S1 phosphorylation in unstressed
CC cells by promoting its dephosphorylation by PP1.
CC {ECO:0000269|PubMed:26159176, ECO:0000269|PubMed:26307080}.
CC -!- SUBUNIT: Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By
CC similarity). Interacts with PP1. {ECO:0000250,
CC ECO:0000269|PubMed:15705855}.
CC -!- INTERACTION:
CC Q5SWA1; P62136: PPP1CA; NbExp=5; IntAct=EBI-2815482, EBI-357253;
CC Q5SWA1; P36873: PPP1CC; NbExp=4; IntAct=EBI-2815482, EBI-356283;
CC Q5SWA1; P36406: TRIM23; NbExp=3; IntAct=EBI-2815482, EBI-740098;
CC -!- DISEASE: Microcephaly, short stature, and impaired glucose metabolism 2
CC (MSSGM2) [MIM:616817]: An autosomal recessive disease characterized by
CC microcephaly, intellectual disability, short stature, and disturbed
CC glucose metabolism. {ECO:0000269|PubMed:26159176,
CC ECO:0000269|PubMed:26307080}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in PPP1R15B has been found in a patient with
CC isolated coloboma, a defect of the eye characterized by the absence of
CC ocular structures due to abnormal morphogenesis of the optic cup and
CC stalk, and the fusion of the fetal fissure (optic fissure). Isolated
CC colobomas may be associated with an abnormally small eye
CC (microphthalmia) or small cornea. {ECO:0000269|PubMed:28493397}.
CC -!- MISCELLANEOUS: The phosphatase activity of the PPP1R15B-PP1 complex
CC toward EIF2S1 is specifically inhibited by Salubrinal, a drug that
CC protects cells from endoplasmic reticulum stress.
CC -!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
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DR EMBL; AK027650; BAB55266.1; -; mRNA.
DR EMBL; AK222877; BAD96597.1; -; mRNA.
DR EMBL; AL606489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065280; AAH65280.1; -; mRNA.
DR EMBL; AL833746; CAH56240.1; -; mRNA.
DR CCDS; CCDS1445.1; -.
DR PDB; 4V0U; X-ray; 7.88 A; E/G/I/K/O=631-701.
DR PDB; 4V0V; X-ray; 1.61 A; B/D=631-660.
DR PDB; 4V0W; X-ray; 1.55 A; B/D=631-669.
DR PDB; 4V0X; X-ray; 1.85 A; B=631-684.
DR PDBsum; 4V0U; -.
DR PDBsum; 4V0V; -.
DR PDBsum; 4V0W; -.
DR PDBsum; 4V0X; -.
DR AlphaFoldDB; Q5SWA1; -.
DR SMR; Q5SWA1; -.
DR IntAct; Q5SWA1; 20.
DR MINT; Q5SWA1; -.
DR STRING; 9606.ENSP00000356156; -.
DR BindingDB; Q5SWA1; -.
DR ChEMBL; CHEMBL4630830; -.
DR iPTMnet; Q5SWA1; -.
DR PhosphoSitePlus; Q5SWA1; -.
DR BioMuta; PPP1R15B; -.
DR DMDM; 74743925; -.
DR EPD; Q5SWA1; -.
DR jPOST; Q5SWA1; -.
DR MassIVE; Q5SWA1; -.
DR MaxQB; Q5SWA1; -.
DR PaxDb; Q5SWA1; -.
DR PeptideAtlas; Q5SWA1; -.
DR PRIDE; Q5SWA1; -.
DR ProteomicsDB; 63971; -.
DR Antibodypedia; 34557; 111 antibodies from 25 providers.
DR Ensembl; ENST00000367188.5; ENSP00000356156.4; ENSG00000158615.10.
DR UCSC; uc001hav.5; human.
DR GeneCards; PPP1R15B; -.
DR HGNC; HGNC:14951; PPP1R15B.
DR HPA; ENSG00000158615; Tissue enhanced (bone).
DR MalaCards; PPP1R15B; -.
DR MIM; 613257; gene.
DR MIM; 616817; phenotype.
DR neXtProt; NX_Q5SWA1; -.
DR Orphanet; 391408; Primary microcephaly-mild intellectual disability-young-onset diabetes syndrome.
DR PharmGKB; PA33633; -.
DR VEuPathDB; HostDB:ENSG00000158615; -.
DR eggNOG; ENOG502QV9K; Eukaryota.
DR HOGENOM; CLU_014797_0_0_1; -.
DR InParanoid; Q5SWA1; -.
DR PhylomeDB; Q5SWA1; -.
DR TreeFam; TF105548; -.
DR PathwayCommons; Q5SWA1; -.
DR SignaLink; Q5SWA1; -.
DR ChiTaRS; PPP1R15B; human.
DR Pharos; Q5SWA1; Tchem.
DR PRO; PR:Q5SWA1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SWA1; protein.
DR Bgee; ENSG00000158615; Expressed in ileal mucosa and 190 other tissues.
DR Genevisible; Q5SWA1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IDA:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006983; P:ER overload response; IEA:Ensembl.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
DR InterPro; IPR019512; Prot_Pase1_reg-su15B_N.
DR Pfam; PF10472; CReP_N; 1.
DR Pfam; PF10488; PP1c_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Diabetes mellitus; Disease variant; Dwarfism;
KW Intellectual disability; Phosphoprotein; Reference proteome;
KW Translation regulation.
FT CHAIN 1..713
FT /note="Protein phosphatase 1 regulatory subunit 15B"
FT /id="PRO_0000320520"
FT REGION 22..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 26
FT /note="P -> S (in dbSNP:rs12094135)"
FT /id="VAR_039196"
FT VARIANT 134
FT /note="P -> S (found in a patient with isolated coloboma;
FT unknown pathological significance; dbSNP:rs755194116)"
FT /evidence="ECO:0000269|PubMed:28493397"
FT /id="VAR_079851"
FT VARIANT 144
FT /note="E -> K (in dbSNP:rs4492688)"
FT /id="VAR_039197"
FT VARIANT 308
FT /note="N -> S (in dbSNP:rs3014626)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.2"
FT /id="VAR_039198"
FT VARIANT 363
FT /note="E -> G (in dbSNP:rs2089891)"
FT /id="VAR_039199"
FT VARIANT 589
FT /note="K -> E (in dbSNP:rs17855962)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_039200"
FT VARIANT 658
FT /note="R -> C (in MSSGM2; no effect on localization;
FT increased protein abundance; loss of interaction with
FT protein phosphatase catalytic subunit PP1; decreased
FT dephosphorylation of EIF2S1; dbSNP:rs869025335)"
FT /evidence="ECO:0000269|PubMed:26159176,
FT ECO:0000269|PubMed:26307080"
FT /id="VAR_074072"
FT CONFLICT 28
FT /note="R -> Q (in Ref. 2; BAD96597)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="N -> D (in Ref. 1; BAB55266)"
FT /evidence="ECO:0000305"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:4V0W"
SQ SEQUENCE 713 AA; 79152 MW; 193679F622E34257 CRC64;
MEPGTGGSRK RLGPRAGFRF WPPFFPRRSQ AGSSKFPTPL GPENSGNPTL LSSAQPETRV
SYWTKLLSQL LAPLPGLLQK VLIWSQLFGG MFPTRWLDFA GVYSALRALK GREKPAAPTA
QKSLSSLQLD SSDPSVTSPL DWLEEGIHWQ YSPPDLKLEL KAKGSALDPA AQAFLLEQQL
WGVELLPSSL QSRLYSNREL GSSPSGPLNI QRIDNFSVVS YLLNPSYLDC FPRLEVSYQN
SDGNSEVVGF QTLTPESSCL REDHCHPQPL SAELIPASWQ GCPPLSTEGL PEIHHLRMKR
LEFLQQANKG QDLPTPDQDN GYHSLEEEHS LLRMDPKHCR DNPTQFVPAA GDIPGNTQES
TEEKIELLTT EVPLALEEES PSEGCPSSEI PMEKEPGEGR ISVVDYSYLE GDLPISARPA
CSNKLIDYIL GGASSDLETS SDPEGEDWDE EAEDDGFDSD SSLSDSDLEQ DPEGLHLWNS
FCSVDPYNPQ NFTATIQTAA RIVPEEPSDS EKDLSGKSDL ENSSQSGSLP ETPEHSSGEE
DDWESSADEA ESLKLWNSFC NSDDPYNPLN FKAPFQTSGE NEKGCRDSKT PSESIVAISE
CHTLLSCKVQ LLGSQESECP DSVQRDVLSG GRHTHVKRKK VTFLEEVTEY YISGDEDRKG
PWEEFARDGC RFQKRIQETE DAIGYCLTFE HRERMFNRLQ GTCFKGLNVL KQC
