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 02-SEP-2026, entry version 174. 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, RC Pancreas, 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 (DSB) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 FunCoup; P35689; 2217. DR STRING; 10090.ENSMUSP00000027214; -. DR iPTMnet; P35689; -. DR PhosphoSitePlus; P35689; -. DR jPOST; P35689; -. DR PaxDb; 10090-ENSMUSP00000027214; -. DR ProteomicsDB; 275938; -. DR Pumba; P35689; -. DR AGR; MGI:103582; -. DR MGI; MGI:103582; Ercc5. DR eggNOG; KOG2520; Eukaryota. DR InParanoid; P35689; -. DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-MMU-5696400; Dual Incision in GG-NER. DR Reactome; R-MMU-6782135; Dual incision in TC-NER. DR PRO; PR:P35689; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P35689; protein. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0000109; C:nucleotide-excision repair complex; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:GO_Central. DR GO; GO:0000405; F:bubble DNA binding; ISO:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; ISO:GO_Central. DR GO; GO:0004520; F:DNA endonuclease activity; ISO:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:GO_Central. DR GO; GO:0004519; F:endonuclease activity; ISO:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; ISO:GO_Central. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB. DR GO; GO:0000993; F:RNA polymerase II complex binding; ISO:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; ISO:GO_Central. DR GO; GO:0006285; P:base-excision repair, AP site formation; ISO:GO_Central. 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:GO_Central. DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:GO_Central. DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI. DR GO; GO:0009411; P:response to UV; IMP:MGI. DR GO; GO:0010225; P:response to UV-C; ISO:GO_Central. DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISO:GO_Central. DR GO; GO:0009650; P:UV protection; IDA:MGI. DR CDD; cd09904; H3TH_XPG; 1. DR CDD; cd09868; PIN_XPG_RAD2; 2. DR FunFam; 3.40.50.1010:FF:000023; DNA repair protein complementing XP-G cells; 1. DR FunFam; 1.10.150.20:FF:000037; DNA repair protein complementing XP-G cells homolog; 1. DR FunFam; 3.40.50.1010:FF:000022; DNA repair protein complementing XP-G cells homolog; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.40.50.1010; 5'-nuclease; 2. 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 NCBIfam; TIGR00600; rad2; 1. DR PANTHER; PTHR16171:SF11; DNA EXCISION REPAIR PROTEIN ERCC-5; 1. DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1. 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; 5' to 3' exonuclease, C-terminal subdomain; 1. DR SUPFAM; SSF88723; PIN domain-like; 1. DR PROSITE; PS52064; UBM; 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 DOMAIN 180..215 FT /note="UBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01409" 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 306..323 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..336 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..373 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..474 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 539..551 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..676 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 677..698 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1041..1060 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1094..1110 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; FT AAA91039/AAB17885)" FT /evidence="ECO:0000305" FT CONFLICT 462 FT /note="G -> E (in Ref. 2; BAA03813 and 3; FT AAA91039/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; FT AAA91039/AAB17885)" FT /evidence="ECO:0000305" FT CONFLICT 958..959 FT /note="ST -> RE (in Ref. 2; BAA03813 and 3; FT AAA91039/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; FT AAA91039/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; FT AAA91039/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 //