SLX4_MOUSE
ID SLX4_MOUSE Reviewed; 1565 AA.
AC Q6P1D7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Structure-specific endonuclease subunit SLX4;
DE AltName: Full=BTB/POZ domain-containing protein 12;
GN Name=Slx4; Synonyms=Btbd12;
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 MRNA].
RC STRAIN=C57BL/6J; 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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-926; SER-940; SER-1249;
RP SER-1254 AND SER-1384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, 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 [3]
RP MUTAGENESIS OF PRO-202; GLU-602; GLN-1324 AND ARG-1545.
RX PubMed=22911665; DOI=10.1002/humu.22206;
RA Bakker J.L., van Mil S.E., Crossan G., Sabbaghian N., De Leeneer K.,
RA Poppe B., Adank M., Gille H., Verheul H., Meijers-Heijboer H.,
RA de Winter J.P., Claes K., Tischkowitz M., Waisfisz Q.;
RT "Analysis of the novel Fanconi anemia gene SLX4/FANCP in familial breast
RT cancer cases.";
RL Hum. Mutat. 34:70-73(2013).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=27010503; DOI=10.1371/journal.pone.0152278;
RA Braun J., Meixner A., Brachner A., Foisner R.;
RT "The GIY-YIG type endonuclease ankyrin repeat and LEM domain-containing
RT protein 1 (ANKLE1) is dispensable for mouse hematopoiesis.";
RL PLoS ONE 11:E0152278-E0152278(2016).
CC -!- FUNCTION: Regulatory subunit that interacts with and increases the
CC activity of different structure-specific endonucleases. Has several
CC distinct roles in protecting genome stability by resolving diverse
CC forms of deleterious DNA structures originating from replication and
CC recombination intermediates and from DNA damage. Component of the SLX1-
CC SLX4 structure-specific endonuclease that resolves DNA secondary
CC structures generated during DNA repair and recombination. Has
CC endonuclease activity towards branched DNA substrates, introducing
CC single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a
CC preference for 5'-flap structures, and promotes symmetrical cleavage of
CC static and migrating Holliday junctions (HJs). Resolves HJs by
CC generating two pairs of ligatable, nicked duplex products. Interacts
CC with the structure-specific ERCC4-ERCC1 endonuclease and promotes the
CC cleavage of bubble structures. Interacts with the structure-specific
CC MUS81-EME1 endonuclease and promotes the cleavage of 3'-flap and
CC replication fork-like structures. SLX4 is required for recovery from
CC alkylation-induced DNA damage and is involved in the resolution of DNA
CC double-strand breaks (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SLX1A/GIYD1. Interacts with
CC ERCC4/XPF; catalytic subunit of the ERCC4-ERCC1 endonuclease. Interacts
CC with MUS81; catalytic subunit of the MUS81-EME1 endonuclease. Interacts
CC with MSH2; component of the MSH2-MSH3 mismatch repair complex.
CC Interacts with TERF2-TERF2IP. Interacts with PLK1 and SLX4IP (By
CC similarity). {ECO:0000250|UniProtKB:Q8IY92}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IY92}.
CC Note=Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q8IY92}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed in bone
CC marrow, brain, thymus and weakly in heart, kidney and spleen.
CC {ECO:0000269|PubMed:27010503}.
CC -!- SIMILARITY: Belongs to the SLX4 family. {ECO:0000305}.
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DR EMBL; BC065125; AAH65125.1; -; mRNA.
DR CCDS; CCDS37240.1; -.
DR RefSeq; NP_803423.2; NM_177472.5.
DR AlphaFoldDB; Q6P1D7; -.
DR SMR; Q6P1D7; -.
DR BioGRID; 206862; 14.
DR ComplexPortal; CPX-498; Slx4-Terf2 complex.
DR STRING; 10090.ENSMUSP00000038871; -.
DR CarbonylDB; Q6P1D7; -.
DR iPTMnet; Q6P1D7; -.
DR PhosphoSitePlus; Q6P1D7; -.
DR EPD; Q6P1D7; -.
DR jPOST; Q6P1D7; -.
DR MaxQB; Q6P1D7; -.
DR PaxDb; Q6P1D7; -.
DR PeptideAtlas; Q6P1D7; -.
DR PRIDE; Q6P1D7; -.
DR ProteomicsDB; 257200; -.
DR Antibodypedia; 24180; 91 antibodies from 14 providers.
DR Ensembl; ENSMUST00000040790; ENSMUSP00000038871; ENSMUSG00000039738.
DR GeneID; 52864; -.
DR KEGG; mmu:52864; -.
DR UCSC; uc007xzg.2; mouse.
DR CTD; 84464; -.
DR MGI; MGI:106299; Slx4.
DR VEuPathDB; HostDB:ENSMUSG00000039738; -.
DR eggNOG; ENOG502R4G8; Eukaryota.
DR GeneTree; ENSGT00390000014091; -.
DR HOGENOM; CLU_003520_0_0_1; -.
DR InParanoid; Q6P1D7; -.
DR OMA; QMMDESD; -.
DR OrthoDB; 288384at2759; -.
DR PhylomeDB; Q6P1D7; -.
DR TreeFam; TF106446; -.
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 52864; 9 hits in 108 CRISPR screens.
DR ChiTaRS; Slx4; mouse.
DR PRO; PR:Q6P1D7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6P1D7; protein.
DR Bgee; ENSMUSG00000039738; Expressed in animal zygote and 121 other tissues.
DR ExpressionAtlas; Q6P1D7; baseline and differential.
DR Genevisible; Q6P1D7; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; ISO:MGI.
DR GO; GO:0048476; C:Holliday junction resolvase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0033557; C:Slx1-Slx4 complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:MGI.
DR GO; GO:1904431; P:positive regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0090656; P:t-circle formation; IMP:BHF-UCL.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR018574; Structure-sp_endonuc_su_Slx4.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF09494; Slx4; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51908; ZF_UBZ4; 2.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1565
FT /note="Structure-specific endonuclease subunit SLX4"
FT /id="PRO_0000383567"
FT DOMAIN 506..579
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 117..147
FT /note="UBZ4-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT ZN_FING 157..185
FT /note="UBZ4-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..1565
FT /note="Interaction with PLK1 and TERF2-TERF2IP"
FT /evidence="ECO:0000250"
FT REGION 683..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1413
FT /note="Interaction with MUS81"
FT /evidence="ECO:0000250"
FT REGION 1128..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1565
FT /note="Interaction with SLX1"
FT /evidence="ECO:0000250"
FT REGION 1546..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 886
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 898
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 925
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 983
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 1349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT CROSSLNK 1350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IY92"
FT MUTAGEN 202
FT /note="P->T: Does not modify the functional properties of
FT the protein."
FT /evidence="ECO:0000269|PubMed:22911665"
FT MUTAGEN 602
FT /note="E->K: Does not modify the functional properties of
FT the protein."
FT /evidence="ECO:0000269|PubMed:22911665"
FT MUTAGEN 1324
FT /note="Q->W: Does not modify the functional properties of
FT the protein."
FT /evidence="ECO:0000269|PubMed:22911665"
FT MUTAGEN 1545
FT /note="R->C: Does not modify the functional properties of
FT the protein."
FT /evidence="ECO:0000269|PubMed:22911665"
SQ SEQUENCE 1565 AA; 172412 MW; AB4CB4EB57CA6394 CRC64;
MVPESAPNGN SQPLPSCFTT TGVPSPSKPR VSELVLQRMK QFKRADPERL RHASEESPQK
TALGDDVPRS PPEETVGENE YKLDATDSDA AMALALQQEF RREEASSHHD SLEEKGLFFC
QMCQKNLSAM NVTRREQHVN RCLDEAEKAQ RPASPRIPDC PICGKPFLTT KSRISHLKQC
AVRMEVGPQL LLQAVRLQTA QPEVDGSPQV PSFSNNVGGL KRKGVTTKRE PRRRKVNKPE
APSEDLLVAM ALSRSEVEHC PVVPPLRLEN AFSEKIRLGA EKKSRKKRPP VCPPQLVTQD
SETTGRQIED RVAQLLSEEA ELSCTPPLLA SKISKEELEP AGWRARLPEG KRNFLWELSA
LTGAWAEESF YTVGLFPPIV SQCPSKEPQL PLELPKQGEP SPRRPPASQS SLPVSHSPKI
RLLSSSQRER QALQDLVDLA VEGLSSSPQP GSRGVPTGLD LVPSSLPLTG FVLPCKKTLK
KDDSASLSLG LLVTDFGAMV NNPHLSDVQF QLDSGEVLYA HKFVLYARCP LLIQYVSTES
FSSEEDGDLT QRALLSDVSS EAAHAFLNYL YMADTDMPPS LVPDLRSLAL RFGVSDLVQL
CEQVPAVVDL EGEQPEETSE DCESRAETFL ELLRSVWVDN EEEVETLLKP ELCEEERERV
NEAEMEEIYE FAATQRKLLQ WGRAADPDGS TNPHGEDGAV SEPSLAGVQS NRQLENTEHM
ESSGLEKEEA LASWEQEGHS TPLQDQCPDW AGKAEAQDAL GEATDDPSFC SRHRRGKECL
PLHPNKAHGC KQPLPSNPRV SSELSQITVD HEEQSDHVRE TQADMAQAPT PHSCSLVSQS
SVDGSPSQSW LHLYHTSHLS PSVSQSHSSI SRVASPRSLS PTTPTKQRRG SNIVTLRKDA
GHHRGQQSSP IAGHRNRGIL ISPAKSPPID LTQSVPEPLS PRAQDPLHFV KKEDEVILLL
DSDEELEHTK TESVSKDSPE GRKVPEFSPR SSELFSVIDV EEDHEHFQSP LKREAGLQHG
EEGQLGNQSA LGCRDIPWLL CSQKTSLDED SATDTSWLVP ATPGVSRSRD CSSQTQIKSL
KTRIPSDETA QQTPRPNLER RTMLETAQQF SVIMPHTQPI TLGAFDSGRQ AYRSPSHPYP
RHHRLSSSQP SCPGPDFTRW SQKSSAPRPC LPNLPAADDV VEVGDSDDEV ASHQGNSSPV
LDGDPPGPMG DYCWNEPLSP IPIDHLNLER TGPLTTSSPS SQVLEALHSD DCHSPGLGTT
PIRGSCGTLR ESQERSSLAG SPEALWDDWN EEEGQSPEAP PVAQMLSTRT RKPDRPETPK
GANQKKNLPP KVPITPMPRY SIMETPVLKK ELDRFGVRAL PKRQMVLKLK EIFQYTHQTL
ESDSEDEVQS PQIPAELPCR QASTTETCNP SRLPTGEPSH PDGDAQLPAS QESMATSVDG
SDNSFSSKSS SAEFGAAFEY SDEDKDEEVG VTASQAAIQA ADTEEAVRRY IRSKPALHRQ
VLRYQPVELA ELQAELKQNG IPVAMGKLSD ILDAQCITFT TAAARKEKLK HKRRQPSGRK
KKDQK
