PININ_MOUSE
ID PININ_MOUSE Reviewed; 725 AA.
AC O35691; Q8CD89; Q8CGU3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Pinin;
GN Name=Pnn;
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=Embryo;
RX PubMed=9332356; DOI=10.1016/s0378-1119(97)00249-7;
RA Ouyang P., Zhen Y.Y., Sugrue S.P.;
RT "Cloning and analysis of cDNA encoding murine pinin.";
RL Gene 197:115-120(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Leu S., Ouyang P.;
RT "Mouse pinin gene.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-380 AND SER-442, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Transcriptional activator binding to the E-box 1 core
CC sequence of the E-cadherin promoter gene; the core-binding sequence is
CC 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription
CC repression. Auxiliary component of the splicing-dependent multiprotein
CC exon junction complex (EJC) deposited at splice junction on mRNAs. The
CC EJC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. Participates in the regulation of
CC alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt
CC upstream of the 5'-splice sites. Component of the PSAP complex which
CC binds RNA in a sequence-independent manner and is proposed to be
CC recruited to the EJC prior to or during the splicing process and to
CC regulate specific excision of introns in specific transcription
CC subsets. Involved in the establishment and maintenance of epithelia
CC cell-cell adhesion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Found in a complex with SR proteins. Found in a mRNP complex
CC with RNPS1. Component of the PSAP complex consisting of RNPS1, SAP18
CC and PNN. Interacts with PNISR, CTBP1, CTBP2, KRT8, KRT18, KRT19,
CC PS1D/PNO40, PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome
CC C complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Cell junction,
CC desmosome {ECO:0000250}. Note=Cell-cell contact area, predominantly
CC desmosome of intercellular adherens junction. Not a nucleocytoplasmic
CC shuttling protein (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pinin family. {ECO:0000305}.
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DR EMBL; Y08701; CAA69960.1; -; mRNA.
DR EMBL; AY129403; AAN05017.1; -; Genomic_DNA.
DR EMBL; AK030978; BAC27200.1; -; mRNA.
DR RefSeq; NP_032917.2; NM_008891.2.
DR AlphaFoldDB; O35691; -.
DR SMR; O35691; -.
DR BioGRID; 202283; 15.
DR IntAct; O35691; 3.
DR STRING; 10090.ENSMUSP00000021381; -.
DR iPTMnet; O35691; -.
DR PhosphoSitePlus; O35691; -.
DR EPD; O35691; -.
DR jPOST; O35691; -.
DR MaxQB; O35691; -.
DR PaxDb; O35691; -.
DR PeptideAtlas; O35691; -.
DR PRIDE; O35691; -.
DR ProteomicsDB; 289576; -.
DR DNASU; 18949; -.
DR GeneID; 18949; -.
DR KEGG; mmu:18949; -.
DR CTD; 5411; -.
DR MGI; MGI:1100514; Pnn.
DR eggNOG; KOG3756; Eukaryota.
DR InParanoid; O35691; -.
DR OrthoDB; 881609at2759; -.
DR PhylomeDB; O35691; -.
DR BioGRID-ORCS; 18949; 28 hits in 76 CRISPR screens.
DR ChiTaRS; Pnn; mouse.
DR PRO; PR:O35691; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35691; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030057; C:desmosome; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR039853; Pinin.
DR InterPro; IPR006786; Pinin_SDK_MemA.
DR InterPro; IPR006787; Pinin_SDK_N.
DR PANTHER; PTHR12707; PTHR12707; 1.
DR Pfam; PF04696; Pinin_SDK_memA; 1.
DR Pfam; PF04697; Pinin_SDK_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell junction; Coiled coil; DNA-binding;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CHAIN 2..725
FT /note="Pinin"
FT /id="PRO_0000190243"
FT REGION 46..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..283
FT /note="Sufficient for PSAP complex assembly"
FT /evidence="ECO:0000250"
FT REGION 278..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..32
FT /evidence="ECO:0000255"
FT COILED 162..233
FT /evidence="ECO:0000255"
FT COILED 286..373
FT /evidence="ECO:0000255"
FT COILED 444..467
FT /evidence="ECO:0000255"
FT COMPBIAS 82..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..660
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 54
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 237
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 237
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 279
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CROSSLNK 561
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H307"
FT CONFLICT 31
FT /note="G -> A (in Ref. 2; AAN05017)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..43
FT /note="AR -> GT (in Ref. 1; CAA69960)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="R -> RR (in Ref. 3; BAC27200)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="QL -> HV (in Ref. 2; AAN05017)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="Q -> P (in Ref. 1; CAA69960)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="D -> H (in Ref. 2; AAN05017)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="T -> I (in Ref. 1; CAA69960)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="M -> V (in Ref. 3; BAC27200)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="R -> T (in Ref. 3; BAC27200)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 82436 MW; DB99FF2DB17AAF5E CRC64;
MAVAVRALQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL
LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS
KERTRDLIQD QNMDEKGKQR NRRIFGLLMG TLQKFKQEST VATERQKRRQ EIEQKLEVQA
EEERKQVENE RRELFEERRA KQTELRLLEQ KVELAQLQEE WNEHNAKIIK YIRTKTKPHL
FYIPGRMCPA TQKLIEESQR KMNALFEGRR IEFAEQINKM EARPRRQSMK EKEHQVVRNE
EQKAEQEEGK VAQREEELEE TGNQHNDVEV EEAGEEEEKE AGIVHSDAEK EQEEEEQKQE
MEVKTEEEAE VREGEKQQDS QPEEVMDVLE MVESVKHVIA EQEVMETNQV ESIEPSENET
SKELEPEMEF DVEPDKECKS LSPGKENINS QEVEKESEEK EEKEEKEPEP QPEPVAQPQP
PPQPLPQSQP HSQPHSQPQP VLQSQPLCQP ETLPLAVLQP PPQVIQEQGN LLPERKDFPL
ESIKLPEVSV EPVLTVHSEN KSKNKTRSRS RGRARNKTSK SRSRSSSSSS SSSSSTSSSS
GSSSSSGSSS SRSSSSSSSS TSGSSSRDSS SSTSSSSESR SRSRGRGHNR DRKHRRSMDR
KRRDTSGLER SHKSSKGGSS RDRKGSKDKS SRPDRKRSIS ESSRSGKRSS RSERDRKSDR
KDKRR
