ERCC6_MOUSE
ID ERCC6_MOUSE Reviewed; 1481 AA.
AC F8VPZ5; A3KMN2;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA excision repair protein ERCC-6;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q03468};
DE AltName: Full=ATP-dependent helicase ERCC6;
DE AltName: Full=Cockayne syndrome protein CSB;
GN Name=Ercc6; Synonyms=Csb;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 325-1481.
RC 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: Essential factor involved in transcription-coupled nucleotide
CC excision repair which allows RNA polymerase II-blocking lesions to be
CC rapidly removed from the transcribed strand of active genes (By
CC similarity). Upon DNA-binding, it locally modifies DNA conformation by
CC wrapping the DNA around itself, thereby modifying the interface between
CC stalled RNA polymerase II and DNA (By similarity). It is required for
CC transcription-coupled repair complex formation. It recruits the CSA
CC complex (DCX(ERCC8) complex), nucleotide excision repair proteins and
CC EP300 to the sites of RNA polymerase II-blocking lesions (By
CC similarity). Plays an important role in regulating the choice of the
CC DNA double-strand breaks (DSBs) repair pathway and G2/M checkpoint
CC activation; DNA-dependent ATPase activity is essential for this
CC function (By similarity). Regulates the DNA repair pathway choice by
CC inhibiting non-homologous end joining (NHEJ), thereby promoting the
CC homologous recombination (HR)-mediated repair of DSBs during the S/G2
CC phases of the cell cycle (By similarity). Mediates the activation of
CC the ATM- and CHEK2-dependent DNA damage responses thus preventing the
CC premature exit from the G2/M checkpoint (By similarity). Acts as a
CC chromatin remodeler at DSBs; DNA-dependent ATPase-dependent activity is
CC essential for this function (By similarity). Remodels chromatin by
CC evicting histones from chromatin flanking DSBs, limiting RIF1
CC accumulation at DSBs thereby promoting BRCA1-mediated HR (By
CC similarity). Required for stable recruitment of ELOA and CUL5 to DNA
CC damage sites (By similarity). Involved in UV-induced translocation of
CC ERCC8 to the nuclear matrix (By similarity). Essential for neuronal
CC differentiation and neuritogenesis; regulates transcription and
CC chromatin remodeling activities required during neurogenesis (By
CC similarity). {ECO:0000250|UniProtKB:Q03468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q03468};
CC -!- SUBUNIT: Homodimer (By similarity). Binds DNA (By similarity).
CC Interacts with ERCC8 (By similarity). Interacts with RNA polymerase II;
CC interaction is enhanced by UV irradiation (By similarity). Component of
CC the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF,
CC SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (By similarity). Interacts
CC with KIAA1530/UVSSA (By similarity). Interacts with ELOA and CUL5; the
CC interaction is induced by DNA damaging agents or by inhibitors of RNA
CC polymerase II elongation (By similarity). Interacts (via WHD region)
CC with RIF1 (By similarity). Interacts with SMARCC2/BAF170, SMARCB1/BAF47
CC and the neuron-specific chromatin remodeling complex (nBAF complex) (By
CC similarity). Interacts with ERCC5/XPG (via C-terminus); the interaction
CC stimulates ERCC6/CSB binding to DNA repair bubble and ERCC6/CSB ATPase
CC activity (By similarity). May form a complex composed of RNA polymerase
CC II, ERCC6/CSB and ERCC5/XPG which associates with the DNA repair bubble
CC during transcription-coupled nucleotide excision repair (By
CC similarity). Interacts with CAND1, CSTF1, DDX3X, DDX5, DDX17, DDX23,
CC DHX36, HDAC1, HNRNPU, MTA2, PRPF3, PSMD3, RBBP4, SFPQ, SMARCA1,
CC SMARCA2, TOP1, USP7 and XRCC5 (By similarity).
CC {ECO:0000250|UniProtKB:Q03468}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q03468}.
CC -!- DOMAIN: A C-terminal ubiquitin-binding domain (UBD) is essential for
CC transcription-coupled nucleotide excision repair activity, interaction
CC with RNA polymerase II, association with chromatin after UV irradiation
CC and for mediating the UV-induced translocation of ERRC8 to the nuclear
CC matrix. {ECO:0000250|UniProtKB:Q03468}.
CC -!- DOMAIN: The N-terminal domain exerts an inhibitory effect on the
CC helicase ATP-binding domain in such a manner that its ATPase activity
CC is restricted (By similarity). Phosphorylation at Ser-158 promotes the
CC intramolecular interaction of the N-terminal domain with the helicase
CC ATP-binding domain, thereby probably releasing the inhibitory effect of
CC the N-terminal domain on its ATPase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q03468}.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner at Ser-158 by
CC cyclin A-CDK2 in response to DNA damage (By similarity).
CC Phosphorylation at this site promotes the intramolecular interaction of
CC the N-terminal domain with the helicase ATP-binding domain, thereby
CC probably releasing the inhibitory effect of the N-terminal domain on
CC its ATPase activity (By similarity). Phosphorylation is essential for
CC its chromatin remodeling activity (By similarity).
CC {ECO:0000250|UniProtKB:Q03468}.
CC -!- PTM: Ubiquitinated at the C-terminus (By similarity). Ubiquitination by
CC the CSA complex leads to ERCC6 proteasomal degradation in a UV-
CC dependent manner (By similarity). Stabilized following interaction with
CC KIAA1530/UVSSA, which promotes recruitment of deubiquitinating enzyme
CC USP7, leading to deubiquitination of ERCC6 thereby preventing UV-
CC induced degradation of ERCC6 by the proteasome (By similarity).
CC {ECO:0000250|UniProtKB:Q03468}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AC154412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132447; AAI32448.1; -; mRNA.
DR CCDS; CCDS36868.1; -.
DR RefSeq; NP_001074690.1; NM_001081221.1.
DR RefSeq; XP_006519183.1; XM_006519120.3.
DR AlphaFoldDB; F8VPZ5; -.
DR SMR; F8VPZ5; -.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR STRING; 10090.ENSMUSP00000066256; -.
DR iPTMnet; F8VPZ5; -.
DR PhosphoSitePlus; F8VPZ5; -.
DR EPD; F8VPZ5; -.
DR MaxQB; F8VPZ5; -.
DR PaxDb; F8VPZ5; -.
DR PRIDE; F8VPZ5; -.
DR ProteomicsDB; 363699; -.
DR Antibodypedia; 34972; 412 antibodies from 35 providers.
DR DNASU; 319955; -.
DR Ensembl; ENSMUST00000066807; ENSMUSP00000066256; ENSMUSG00000054051.
DR GeneID; 319955; -.
DR KEGG; mmu:319955; -.
DR UCSC; uc007sze.1; mouse.
DR CTD; 2074; -.
DR MGI; MGI:1100494; Ercc6.
DR VEuPathDB; HostDB:ENSMUSG00000054051; -.
DR eggNOG; KOG0387; Eukaryota.
DR GeneTree; ENSGT00940000158057; -.
DR HOGENOM; CLU_000315_7_2_1; -.
DR InParanoid; F8VPZ5; -.
DR OMA; HSVVKHD; -.
DR OrthoDB; 372069at2759; -.
DR PhylomeDB; F8VPZ5; -.
DR TreeFam; TF101236; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-MMU-6782135; Dual incision in TC-NER.
DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR BioGRID-ORCS; 319955; 7 hits in 110 CRISPR screens.
DR PRO; PR:F8VPZ5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; F8VPZ5; protein.
DR Bgee; ENSMUSG00000054051; Expressed in superior cervical ganglion and 167 other tissues.
DR ExpressionAtlas; F8VPZ5; baseline and differential.
DR Genevisible; F8VPZ5; MM.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
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:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0042262; P:DNA protection; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:MGI.
DR GO; GO:0006290; P:pyrimidine dimer repair; IMP:MGI.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0009411; P:response to UV; IMP:MGI.
DR GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IMP:MGI.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:MGI.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Isopeptide bond; Methylation; Neurogenesis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1481
FT /note="DNA excision repair protein ERCC-6"
FT /id="PRO_0000448242"
FT DOMAIN 515..691
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 839..998
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..506
FT /note="N-terminal domain; essential for its chromatin
FT remodeling activity"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT REGION 309..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1416
FT /note="Ubiquitin-binding domain (UBD)"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT REGION 1417..1481
FT /note="Winged-helix domain (WHD)"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT REGION 1434..1481
FT /note="Essential for its interaction with RNA polymerase
FT II, transcription-coupled nucleotide excision repair
FT activity, association with chromatin after UV irradiation
FT and for mediating the UV-induced translocation of ERRC8 to
FT the nuclear matrix"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOTIF 642..645
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 363..393
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 528..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 158
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 170
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 298
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 444
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT MOD_RES 1047
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03468"
SQ SEQUENCE 1481 AA; 165958 MW; 8907FDB060B94B73 CRC64;
MFHEEVPNST HPQEQDCLPS QHANAYKDMP VGQENGGVSE AGECLSSTSC EYGPSTSAEA
CVLAATRRGP TLLHIDRHQI PAVEPSAQAL ELQGLGVDVY DQAVLEQGVL QQVDSAMHEA
SCVAQLADAE KEYQSVLDDL MSCTTSLRQI NKIIEQLSPQ AASNRDINRK LDSVKRQKYN
KEQQLKKITA KQKRLQAILG GAGVQVELDH ASLEEDDAEP GPSCLGSMLM PAQETAWEEL
IRTGQMTPFG TPAPQKQEKK PRKIMLNEAS GFEKYLAEQA QLSFERKKQA ATKRTAKKAI
VISESSRAAI ETKADQRSQV LSQTDKRLKK HSRKLQRRAL QFQGKVGLPS GKKPLEPEVR
PEAEGDTEGE ESGSSPTDGE EEEEQEEEEG VASLSSDDVS YELKPLRKRQ KYQKKVPVQE
IDDDFFPSSE EEDEAMEGRG GGRKVARRQD DGDEDYYKQR LRRWNRLRLQ DKEKRLKLED
DSEESDAEFD EGFKVPGFLF KKLFKYQQTG VRWLWELHCQ QAGGILGDEM GLGKTIQIIA
FLAGLSYSKI RTRGSNYRFE GLGPTIIVCP TTVMHQWVKE FHTWWPPFRV AVLHETGSYT
HKKERLIRDI VYCHGVLITS YSYIRLMQDD ISRHDWHYVI LDEGHKIRNP NAAVTLACKQ
FRTPHRIILS GSPMQNNLRE LWSLFDFIFP GKLGTLPVFM EQFSVPITMG GYSNASPVQV
KTAYKCACVL RDTINPYLLR RMKSDVKMSL SLPDKNEQVL FCRLTDEQHK VYQNFIDSKA
VYRILNGENQ IFSGLVALRK ICNHPDLFSG GPKNASGPPE DELEEEQFGH WRRSGKMIVV
ESLLKIWHRQ GQRVLLFSQS RQMLHILEVF LRAHKYSYLK MDGTTTIASR QPLITKYNED
TSIFVFLLTT RVGGLGVNLT GANRVIIYDP DWNPSTDTQA RERAWRIGQK KQVTVYRLLT
AGTIEEKIYH RQIFKQFLTN RVLKDPKQRR FFKSNDLYEL FTLTSPDASQ GTETSAIFAG
TGSSIQTPKC QLKKRTSTVL GTDPKCKKPP VSDTPANAAT LIGEKPKAAG ATGRSVTSGE
SGPFKGDHDT NGNRASSVAF GEETDAGSTL EHLSVMSGDG KHSDSPTVDH TSRPPVEAST
SEKQGSSYAG ARCQAQTEPV PMSEQMEGQF SKYKSKRKHD ASEEETTEKR PQPKQKAKNS
KHCRDAKFEG TRVPHLVKKR RYRQQTSEQE GGAKDRSSDD YVLEKLFKKS VGVHSVVRHD
AIIDGSSPDY VLVEAEANRV AQDALKALRL SRQQCLGAAS GVPTWTGHRG ISGAPTGVKN
RFGQKRDSSL PVQHPSSLTE KTQNNMKKEG KAHTPEHFSG KEDGASVSGA PSSSSLLARM
RARNHMILPE RLESDSEHLA EAAAVPPCGT EHDDLLVDMR NFIAFQAQVD GQASTQEILQ
EFESKLSVAQ SCVFRELLRN LCNFHRTPGG EGIWKLKPEY C
