PP1B_MOUSE
ID PP1B_MOUSE Reviewed; 327 AA.
AC P62141; P37140; Q3TBE5; Q3TL90; Q542E7; Q8C285; Q9DBY2;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE Short=PP-1B;
DE EC=3.1.3.16;
DE EC=3.1.3.53;
GN Name=Ppp1cb;
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].
RC TISSUE=Brain;
RX PubMed=2544298; DOI=10.1016/0092-8674(89)90338-3;
RA Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.;
RT "The fission yeast dis2+ gene required for chromosome disjoining encodes
RT one of two putative type 1 protein phosphatases.";
RL Cell 57:997-1007(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryonic head, Embryonic heart, Embryonic kidney,
RC Lung, Mammary gland, Morula, and Thymus;
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 PROTEIN SEQUENCE OF 26-35; 60-73 AND 150-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH PPP1R15B.
RX PubMed=14638860; DOI=10.1083/jcb.200308075;
RA Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.;
RT "Inhibition of a constitutive translation initiation factor 2alpha
RT phosphatase, CReP, promotes survival of stressed cells.";
RL J. Cell Biol. 163:767-775(2003).
RN [6]
RP IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
RX PubMed=16835242; DOI=10.1074/jbc.m513556200;
RA Latreille M., Larose L.;
RT "Nck in a complex containing the catalytic subunit of protein phosphatase 1
RT regulates eukaryotic initiation factor 2alpha signaling and cell survival
RT to endoplasmic reticulum stress.";
RL J. Biol. Chem. 281:26633-26644(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [8]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21712997; DOI=10.1371/journal.pone.0021325;
RA Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.;
RT "Protein phosphatase 1 (PP1) is a post-translational regulator of the
RT mammalian circadian clock.";
RL PLoS ONE 6:E21325-E21325(2011).
RN [9]
RP FUNCTION IN CIRCADIAN CLOCK.
RX PubMed=21930935; DOI=10.1073/pnas.1107178108;
RA Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.;
RT "The period of the circadian oscillator is primarily determined by the
RT balance between casein kinase 1 and protein phosphatase 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011).
CC -!- FUNCTION: Protein phosphatase that associates with over 200 regulatory
CC proteins to form highly specific holoenzymes which dephosphorylate
CC hundreds of biological targets. Protein phosphatase (PP1) is essential
CC for cell division, it participates in the regulation of glycogen
CC metabolism, muscle contractility and protein synthesis. Involved in
CC regulation of ionic conductances and long-term synaptic plasticity.
CC Component of the PTW/PP1 phosphatase complex, which plays a role in the
CC control of chromatin structure and cell cycle progression during the
CC transition from mitosis into interphase. In balance with CSNK1D and
CC CSNK1E, determines the circadian period length, through the regulation
CC of the speed and rhythmicity of PER1 and PER2 phosphorylation. May
CC dephosphorylate CSNK1D and CSNK1E. {ECO:0000269|PubMed:21712997,
CC ECO:0000269|PubMed:21930935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[myosin light chain] = L-seryl-[myosin
CC light chain] + phosphate; Xref=Rhea:RHEA:12849, Rhea:RHEA-COMP:13684,
CC Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.53;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[myosin light chain] = L-threonyl-
CC [myosin light chain] + phosphate; Xref=Rhea:RHEA:53988, Rhea:RHEA-
CC COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.53;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by the toxins okadaic acid, tautomycin
CC and microcystin Leu-Arg. The phosphatase activity of the PPP1R15A-PP1
CC complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug
CC that protects cells from endoplasmic reticulum stress (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC,
CC which is folded into its native form by inhibitor 2 and glycogen
CC synthetase kinase 3, and then complexed to one or several targeting or
CC regulatory subunits. The targeting or regulatory subunits determine the
CC substrate specificity of PP1. PPP1R12A, PPP1R12B and PPP1R12C mediate
CC binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver),
CC PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen.
CC Interacts with PPP1R7 and PPP1R12C. Interacts with PPP1R12A and NUAK1;
CC the interaction is direct. Interacts with TRIM28; the interaction is
CC weak (By similarity). Interacts with PPP1R15A; the interaction mediates
CC binding to EIF2S1. Interacts with PPP1R16B. Component of the PTW/PP1
CC phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA
CC or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with TRIM28; the
CC interaction is weak (By similarity). Part of a complex containing
CC PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction
CC mediates binding to EIF2S1. Interacts with FOXP3 (By similarity).
CC Interacts with RRP1B (By similarity). Interacts with SERPINE1.
CC Interacts with LZTR1 (By similarity). {ECO:0000250|UniProtKB:P62140,
CC ECO:0000269|PubMed:14638860, ECO:0000269|PubMed:16835242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62140}. Nucleus
CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P62140}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P62140}. Note=Highly mobile in cells and can be
CC relocalized through interaction with targeting subunits. In the
CC presence of PPP1R8 relocalizes from the nucleus to nuclear speckles.
CC {ECO:0000250|UniProtKB:P62140}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget - Issue
CC 32 of March 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/032";
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DR EMBL; M27073; AAA37527.1; -; mRNA.
DR EMBL; AK004686; BAB23473.1; -; mRNA.
DR EMBL; AK088893; BAC40636.1; -; mRNA.
DR EMBL; AK089067; BAC40733.1; -; mRNA.
DR EMBL; AK147112; BAE27684.1; -; mRNA.
DR EMBL; AK160743; BAE35984.1; -; mRNA.
DR EMBL; AK166168; BAE38608.1; -; mRNA.
DR EMBL; AK166623; BAE38902.1; -; mRNA.
DR EMBL; AK168141; BAE40108.1; -; mRNA.
DR EMBL; AK169379; BAE41126.1; -; mRNA.
DR EMBL; AK171283; BAE42366.1; -; mRNA.
DR EMBL; BC046832; AAH46832.1; -; mRNA.
DR CCDS; CCDS19193.1; -.
DR PIR; D32550; D32550.
DR RefSeq; NP_766295.2; NM_172707.3.
DR AlphaFoldDB; P62141; -.
DR SMR; P62141; -.
DR BioGRID; 202336; 97.
DR IntAct; P62141; 82.
DR MINT; P62141; -.
DR STRING; 10090.ENSMUSP00000015100; -.
DR iPTMnet; P62141; -.
DR PhosphoSitePlus; P62141; -.
DR SwissPalm; P62141; -.
DR EPD; P62141; -.
DR jPOST; P62141; -.
DR MaxQB; P62141; -.
DR PaxDb; P62141; -.
DR PeptideAtlas; P62141; -.
DR PRIDE; P62141; -.
DR ProteomicsDB; 291641; -.
DR Antibodypedia; 28856; 521 antibodies from 33 providers.
DR DNASU; 19046; -.
DR Ensembl; ENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956.
DR Ensembl; ENSMUST00000201360; ENSMUSP00000144047; ENSMUSG00000014956.
DR GeneID; 19046; -.
DR KEGG; mmu:19046; -.
DR UCSC; uc008wzq.2; mouse.
DR CTD; 5500; -.
DR MGI; MGI:104871; Ppp1cb.
DR VEuPathDB; HostDB:ENSMUSG00000014956; -.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000154644; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P62141; -.
DR OMA; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; P62141; -.
DR TreeFam; TF354243; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR Reactome; R-MMU-5673000; RAF activation.
DR BioGRID-ORCS; 19046; 25 hits in 68 CRISPR screens.
DR ChiTaRS; Ppp1cb; mouse.
DR PRO; PR:P62141; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P62141; protein.
DR Bgee; ENSMUSG00000014956; Expressed in blood and 261 other tissues.
DR ExpressionAtlas; P62141; baseline and differential.
DR Genevisible; P62141; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042587; C:glycogen granule; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; ISO:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
DR GO; GO:0050115; F:myosin-light-chain-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:UniProtKB.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; ISO:MGI.
DR GO; GO:0005981; P:regulation of glycogen catabolic process; ISO:MGI.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Carbohydrate metabolism; Cell cycle;
KW Cell division; Cytoplasm; Direct protein sequencing; Glycogen metabolism;
KW Hydrolase; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62140"
FT CHAIN 2..327
FT /note="Serine/threonine-protein phosphatase PP1-beta
FT catalytic subunit"
FT /id="PRO_0000058780"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62140"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62140"
FT CONFLICT 64
FT /note="I -> N (in Ref. 2; BAC40733)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="W -> R (in Ref. 2; BAE42366)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="S -> F (in Ref. 2; BAE38902)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="V -> E (in Ref. 2; BAB23473)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="P -> S (in Ref. 2; BAE42366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 327 AA; 37187 MW; E8356022E9B94ECD CRC64;
MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
KAKYQYGGLN SGRPVTPPRT ANPPKKR
