XRCC1_MOUSE
ID XRCC1_MOUSE Reviewed; 631 AA.
AC Q60596; Q3THC5; Q5U435; Q7TNQ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=DNA repair protein XRCC1;
DE AltName: Full=X-ray repair cross-complementing protein 1;
GN Name=Xrcc1; Synonyms=Xrcc-1;
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=7959765; DOI=10.1006/geno.1994.1359;
RA Brookman K.W., Tebbs R.S., Allen S.A., Tucker J.D., Swiger R.R.,
RA Lamerdin J.E., Carrano A.V., Thompson L.H.;
RT "Isolation and characterization of mouse Xrcc-1, a DNA repair gene
RT affecting ligation.";
RL Genomics 22:180-188(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=DBA/2J;
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, and FVB/N; TISSUE=Colon, and Egg;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, 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-446 AND THR-452, AND
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, 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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28002403; DOI=10.1038/nature20790;
RG Care4Rare Canada Consortium;
RA Hoch N.C., Hanzlikova H., Rulten S.L., Tetreault M., Komulainen E., Ju L.,
RA Hornyak P., Zeng Z., Gittens W., Rey S.A., Staras K., Mancini G.M.,
RA McKinnon P.J., Wang Z.Q., Wagner J.D., Yoon G., Caldecott K.W.;
RT "XRCC1 mutation is associated with PARP1 hyperactivation and cerebellar
RT ataxia.";
RL Nature 541:87-91(2017).
CC -!- FUNCTION: Involved in DNA single-strand break repair by mediating the
CC assembly of DNA break repair protein complexes (By similarity).
CC Probably during DNA repair, negatively regulates ADP-ribose levels by
CC modulating ADP-ribosyltransferase PARP1 activity (PubMed:28002403).
CC {ECO:0000250|UniProtKB:P18887, ECO:0000269|PubMed:28002403}.
CC -!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK), DNA
CC polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX
CC and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and
CC increases with the acetylated form of APEX1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18887}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P18887}. Note=Moves from the nucleoli
CC to the global nuclear chromatin upon DNA damage.
CC {ECO:0000250|UniProtKB:P18887}.
CC -!- PTM: Phosphorylation of Ser-371 causes dimer dissociation.
CC Phosphorylation by CK2 promotes interaction with APTX and APLF (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal. Conditional knockout in brain
CC causes cerebellar histopathology including increased apoptosis of
CC cerebellar granule neurons, reduced numbers of cerebellar interneurons
CC and decreased electrophysiological spike activity in Purkinje cells.
CC Mutant mice exhibit cerebellar ataxia and elevated levels of ADP-ribose
CC in cerebellum. Double knockout with PARP1 restores the normal
CC interneuron density and ADP-ribose levels, reducing cerebellar ataxia
CC in comparison to the single XRCC1 knockout mice.
CC {ECO:0000269|PubMed:28002403}.
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DR EMBL; U02887; AAA93115.1; -; mRNA.
DR EMBL; AK168334; BAE40272.1; -; mRNA.
DR EMBL; BC055900; AAH55900.1; -; mRNA.
DR EMBL; BC085281; AAH85281.1; -; mRNA.
DR CCDS; CCDS20955.1; -.
DR PIR; A54659; A54659.
DR RefSeq; NP_033558.3; NM_009532.4.
DR RefSeq; XP_017177620.1; XM_017322131.1.
DR PDB; 3PC6; X-ray; 1.90 A; A/B=535-631.
DR PDB; 3PC8; X-ray; 2.31 A; A/B=534-631.
DR PDB; 3QVG; X-ray; 2.26 A; B/D=531-631.
DR PDBsum; 3PC6; -.
DR PDBsum; 3PC8; -.
DR PDBsum; 3QVG; -.
DR AlphaFoldDB; Q60596; -.
DR SMR; Q60596; -.
DR BioGRID; 204607; 12.
DR IntAct; Q60596; 3.
DR MINT; Q60596; -.
DR STRING; 10090.ENSMUSP00000070995; -.
DR iPTMnet; Q60596; -.
DR PhosphoSitePlus; Q60596; -.
DR EPD; Q60596; -.
DR jPOST; Q60596; -.
DR MaxQB; Q60596; -.
DR PaxDb; Q60596; -.
DR PRIDE; Q60596; -.
DR ProteomicsDB; 297569; -.
DR Antibodypedia; 1863; 594 antibodies from 44 providers.
DR DNASU; 22594; -.
DR Ensembl; ENSMUST00000063249; ENSMUSP00000070995; ENSMUSG00000051768.
DR Ensembl; ENSMUST00000205573; ENSMUSP00000146105; ENSMUSG00000051768.
DR GeneID; 22594; -.
DR KEGG; mmu:22594; -.
DR UCSC; uc009fpx.2; mouse.
DR CTD; 7515; -.
DR MGI; MGI:99137; Xrcc1.
DR VEuPathDB; HostDB:ENSMUSG00000051768; -.
DR eggNOG; KOG3226; Eukaryota.
DR GeneTree; ENSGT00390000004140; -.
DR HOGENOM; CLU_030026_0_0_1; -.
DR InParanoid; Q60596; -.
DR OMA; LFFNRDN; -.
DR OrthoDB; 539462at2759; -.
DR PhylomeDB; Q60596; -.
DR TreeFam; TF101201; -.
DR Reactome; R-MMU-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR Reactome; R-MMU-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR BioGRID-ORCS; 22594; 17 hits in 112 CRISPR screens.
DR ChiTaRS; Xrcc1; mouse.
DR EvolutionaryTrace; Q60596; -.
DR PRO; PR:Q60596; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q60596; protein.
DR Bgee; ENSMUSG00000051768; Expressed in saccule of membranous labyrinth and 225 other tissues.
DR Genevisible; Q60596; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0032356; F:oxidized DNA binding; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR GO; GO:0021587; P:cerebellum morphogenesis; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:BHF-UCL.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IMP:BHF-UCL.
DR GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; IMP:UniProtKB.
DR GO; GO:1904877; P:positive regulation of DNA ligase activity; ISO:MGI.
DR GO; GO:1903518; P:positive regulation of single strand break repair; IGI:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; ISO:MGI.
DR GO; GO:0033194; P:response to hydroperoxide; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IMP:BHF-UCL.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:UniProtKB.
DR CDD; cd17725; BRCT_XRCC1_rpt1; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR045080; BRCT_XRCC1_rpt1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002706; Xrcc1_N.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF01834; XRCC1_N; 1.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52113; SSF52113; 2.
DR PROSITE; PS50172; BRCT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..631
FT /note="DNA repair protein XRCC1"
FT /id="PRO_0000066045"
FT DOMAIN 315..403
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 536..627
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 225..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 518
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P18887"
FT CONFLICT 28
FT /note="D -> G (in Ref. 3; AAH85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="V -> L (in Ref. 2; BAE40272)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="N -> S (in Ref. 3; AAH85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="L -> F (in Ref. 3; AAH85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="I -> V (in Ref. 3; AAH85281)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="P -> H (in Ref. 2; BAE40272)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="V -> I (in Ref. 1; AAA93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="R -> G (in Ref. 2; BAE40272)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="H -> R (in Ref. 1; AAA93115)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="V -> A (in Ref. 3; AAH85281)"
FT /evidence="ECO:0000305"
FT TURN 540..543
FT /evidence="ECO:0007829|PDB:3PC6"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:3PC6"
FT HELIX 556..566
FT /evidence="ECO:0007829|PDB:3PC6"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:3PC8"
FT STRAND 581..586
FT /evidence="ECO:0007829|PDB:3PC6"
FT HELIX 590..596
FT /evidence="ECO:0007829|PDB:3PC6"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:3PC6"
FT HELIX 607..616
FT /evidence="ECO:0007829|PDB:3PC6"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:3PC6"
SQ SEQUENCE 631 AA; 68971 MW; 1A730F206E5B8879 CRC64;
MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI
GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE SRSGSNPNRV RIFGPDKLVR
AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK FHSPPDKDEA EATSQKVTVT KLGQFRVKEE
DDSANSLKPG ALFFSRINKT SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP
QEPPKGKRKL DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR
GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTPDSTHL
ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR YLMAGLGSSS EDEGDSHSES
GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP PTPKETKAPS PGPQDNSDTE GEESEGRDNG
AEDSGDTEDE LRRVAKQREQ RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF
FEGKHFFLYG EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP
SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A
