ERCC5_MOUSE
ID ERCC5_MOUSE Reviewed; 1170 AA.
AC P35689; Q61528; Q64248;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DNA excision repair protein ERCC-5 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P28715};
DE AltName: Full=DNA repair protein complementing XP-G cells homolog;
DE AltName: Full=Xeroderma pigmentosum group G-complementing protein homolog;
GN Name=Ercc5; Synonyms=Ercc-5, Xpg;
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].
RX PubMed=7510366; DOI=10.1016/0921-8777(94)90080-9;
RA Shiomi T., Harada Y.-N., Saito T., Shiomi N., Okuno Y., Yamaizumi M.;
RT "An ERCC5 gene with homology to yeast RAD2 is involved in group G Xeroderma
RT pigmentosum.";
RL Mutat. Res. 314:167-175(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10; TISSUE=Liver;
RX PubMed=7590748; DOI=10.1006/geno.1995.1106;
RA Harada Y.N., Matsuda Y., Shiomi N., Shiomi T.;
RT "Complementary DNA sequence and chromosomal localization of xpg, the mouse
RT counterpart of human repair gene XPG/ERCC5.";
RL Genomics 28:59-65(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=DBA/2J;
RX PubMed=8703115; DOI=10.1007/s003359900198;
RA Ludwig D.L., Mudgett J.S., Park M.S., Perez-Castro A.V., Macinnes M.A.;
RT "Molecular cloning and structural analysis of the functional mouse genomic
RT XPG gene.";
RL Mamm. Genome 7:644-649(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-704 AND SER-705, AND
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).
CC -!- FUNCTION: Single-stranded structure-specific DNA endonuclease involved
CC in DNA excision repair. Makes the 3'incision in DNA nucleotide excision
CC repair (NER). Binds and bends DNA repair bubble substrate and breaks
CC base stacking at the single-strand/double-strand DNA junction of the
CC DNA bubble. Plays a role in base excision repair (BER) by promoting the
CC binding of DNA glycosylase NTHL1 to its substrate and increasing NTHL1
CC catalytic activity that removes oxidized pyrimidines from DNA. Involved
CC in transcription-coupled nucleotide excision repair (TCR) which allows
CC RNA polymerase II-blocking lesions to be rapidly removed from the
CC transcribed strand of active genes. Functions during the initial step
CC of TCR in cooperation with ERCC6/CSB to recognized stalled RNA
CC polymerase II. Also, stimulates ERCC6/CSB binding to the DNA repair
CC bubble and ERCC6/CSB ATPase activity. Required for DNA replication fork
CC maintenance and preservation of genomic stability. Involved in
CC homologous recombination repair (HRR) induced by DNA replication stress
CC by recruiting RAD51, BRCA2, and PALB2 to the damaged DNA site. During
CC HRR, binds to the replication fork with high specificity and stabilizes
CC it. Also, acts upstream of HRR, to promote the release of BRCA1 from
CC DNA. {ECO:0000250|UniProtKB:P28715}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P28715};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250};
CC -!- SUBUNIT: Monomer. Homodimer. Component of the homologous recombination
CC repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2, DSS1 and
CC RAD51. Within the complex, interacts with BRCA2 and PALB2. Interacts
CC with RNA polymerase II. Interacts (via C-terminus) with ERCC6/CSB; the
CC interaction stimulates ERCC6/CSB binding to the DNA repair bubble and
CC ERCC6/CSB ATPase activity. May form a complex composed of RNA
CC polymerase II, ERCC6/CSB and ERCC5/XPG which associates with the DNA
CC repair bubble during transcription-coupled nucleotide excision repair.
CC Interacts with BRCA1; the interaction promotes the release of BRCA1
CC from DNA. Interacts with PCNA. Interacts with NTHL1; the interaction
CC stimulates NTHL1 activity and NTHL1 binding to its DNA substrate.
CC {ECO:0000250|UniProtKB:P28715}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28715}.
CC Chromosome {ECO:0000250|UniProtKB:P28715}. Note=Colocalizes with RAD51
CC to nuclear foci in S phase. Localizes to DNA double-strand breaks (DBS)
CC during replication stress. Colocalizes with BRCA2 to nuclear foci
CC following DNA replication stress. {ECO:0000250|UniProtKB:P28715}.
CC -!- DOMAIN: Both nuclear localization signals 1 and 2 act as a monopartite
CC signal which binds to the high affinity site on KPNA2/importin-alpha.
CC {ECO:0000250|UniProtKB:P28715}.
CC -!- DOMAIN: Both the spacer region (also known as the recognition (R)
CC domain) and C-terminal domain are required for stable binding to the
CC DNA repair bubble. However, both domains are dispensable for incision
CC of DNA bubble structures. {ECO:0000250|UniProtKB:P28715}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000305}.
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DR EMBL; D16306; BAA03813.1; -; mRNA.
DR EMBL; U40796; AAA91039.1; -; mRNA.
DR EMBL; U40795; AAB17885.1; -; Genomic_DNA.
DR EMBL; U39892; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U39893; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U39894; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U39896; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40073; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40431; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40432; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40668; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40669; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40670; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40792; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40793; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; U40794; AAB17885.1; JOINED; Genomic_DNA.
DR EMBL; AC123800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35553.1; -.
DR PIR; A57650; A57650.
DR AlphaFoldDB; P35689; -.
DR SMR; P35689; -.
DR STRING; 10090.ENSMUSP00000027214; -.
DR iPTMnet; P35689; -.
DR PhosphoSitePlus; P35689; -.
DR EPD; P35689; -.
DR jPOST; P35689; -.
DR MaxQB; P35689; -.
DR PaxDb; P35689; -.
DR PRIDE; P35689; -.
DR ProteomicsDB; 275938; -.
DR MGI; MGI:103582; Ercc5.
DR eggNOG; KOG2520; Eukaryota.
DR InParanoid; P35689; -.
DR ChiTaRS; Ercc5; mouse.
DR PRO; PR:P35689; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35689; protein.
DR GO; GO:0005662; C:DNA replication factor A complex; ISO:MGI.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000405; F:bubble DNA binding; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; ISO:MGI.
DR GO; GO:0004519; F:endonuclease activity; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0006285; P:base-excision repair, AP site formation; ISO:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:MGI.
DR GO; GO:0009411; P:response to UV; IMP:MGI.
DR GO; GO:0010225; P:response to UV-C; ISO:MGI.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISO:MGI.
DR GO; GO:0009650; P:UV protection; IDA:MGI.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00600; rad2; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1170
FT /note="DNA excision repair protein ERCC-5"
FT /id="PRO_0000154032"
FT REGION 1..78
FT /note="N-domain"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 31..67
FT /note="DNA-binding; may bind to the undamaged single-strand
FT DNA of the DNA repair bubble"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 79..784
FT /note="Spacer region"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 304..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..880
FT /note="I-domain"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 819..835
FT /note="DNA-binding; may bind to the undamaged single-strand
FT DNA of the DNA repair bubble"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 847..879
FT /note="DNA-binding; H2TH (helix-2turn-helix) motif which
FT binds double-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 911..917
FT /note="DNA-binding; may bind double-stranded DNA"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 980..1008
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 1010..1170
FT /note="Interaction with ERCC6/CSB"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT REGION 1033..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1049..1065
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT MOTIF 1153..1170
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT COMPBIAS 305..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 788
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 790
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 809
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 811
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT BINDING 860
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P39748"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28715"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 388
FT /note="C -> R (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="G -> R (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="G -> E (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="R -> S (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="T -> I (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="T -> S (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
FT CONFLICT 958..959
FT /note="ST -> RE (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="N -> S (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="I -> M (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="S -> G (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121
FT /note="P -> S (in Ref. 2; BAA03813)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="D -> G (in Ref. 2; BAA03813 and 3; AAA91039/
FT AAB17885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1170 AA; 130715 MW; B4B9F93ACEBC3729 CRC64;
MGVQGLWKLL ECSGHRVSPE ALEGKVLAVD ISIWLNQALK GVRDSHGNVI ENAHLLTLFH
RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRQRKDSASI DSRKTTEKLL KTFLKRQALK
TAFRSSRHEA PPSLTQVQRQ DDIYVLPPLP EEEKHSSEEE DEKQWQARMD QKQALQEEFF
HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK
NYLNQHIENV QKEMNQQHSG QIQRQYQDEG GFLKEVESRR VVSEDTSHYI LIKGIQGKKV
MDVDSESLPS SSNVHSVSSN LKSSPHEKVK PEREPEAAPP SPRTLLAIQA AMLGSSSEDE
PESREGRQSK ERNSGATADA GSISPRTCAA IQKALDDDND EKVSGSSDDL AEKMLLGSGL
EQEEHADETA ERGGGVPFDT APLTPSVTEV KECVTSGSSA NGQTDSAHSF TTASHRCDTP
KETVSLARAV KEASQISSEC EVEGRPAALS PAFIGTPSSH VSGVLSEREP TLAPPTTRTH
SDQGIDIHPE DPELQNGLYP LETKCNSSRL SSDDETEGGQ NPAPKACSTV HVPAEAMSNL
ENALPSNAEE RGDFQETIQL REVPEAAARE LISAPKPMGP MEMESEESES DGSFIEVQSV
VSNSELQTES SEASTHLSEK DAEEPRETLE EGTSRDTECL LQDSSDIEAM EGHREADIDA
EDMPNEWQDI NLEELDALES NLLAEQNSLK AQKQQQDRIA ASVTGQMFLE SQELLRLFGV
PYIQAPMEAE AQCAMLDLTD QTSGTITDDS DIWLFGARHV YKNFFNKNKF VEYYQYVDFY
SQLGLDRNKL INLAYLLGSD YTEGIPTVGC VTAMEILNEF PGRGLDPLLK FSEWWHEAQN
NKKVAENPYD TKVKKKLRKL QLTPGFPNPA VADAYLRPVV DDSRGSFLWG KPDVDKISTF
CQRYFGWNRM KTDESLYPVL KHLNAHQTQL RIDSFFRLAQ QEKQDAKLIK SHRLNRAVTC
ILRKEREEKA PELTKVTEAL DDAKGKTQKR ELPYKKETSV PKRRRPSGNG GFLGDPYCSE
SPQESSCEDG EGSSVMSARQ RSAAESSKIS CSDVPDLVRD PPHGRQGCVS TSSSSEDDED
KAKTVLVTAR PVFGKKKLKL KSMKRRKKKT
