SLF1_HUMAN
ID SLF1_HUMAN Reviewed; 1058 AA.
AC Q9BQI6; B4DMG4; Q3B7K4; Q6NSA5; Q6PHW9; Q9Y402;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=SMC5-SMC6 complex localization factor protein 1 {ECO:0000312|HGNC:HGNC:25408};
DE AltName: Full=Ankyrin repeat domain-containing protein 32;
DE AltName: Full=BRCT domain-containing protein 1;
DE AltName: Full=Smc5/6 localization factor 1 {ECO:0000303|PubMed:25931565};
GN Name=SLF1 {ECO:0000303|PubMed:25931565, ECO:0000312|HGNC:HGNC:25408};
GN Synonyms=ANKRD32, BRCTD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-328 (ISOFORM 1).
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-267 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 631-1058 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-1058 (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, INTERACTION WITH RAD18; SLF2 AND SMC6, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25931565; DOI=10.1126/science.1253671;
RA Raeschle M., Smeenk G., Hansen R.K., Temu T., Oka Y., Hein M.Y.,
RA Nagaraj N., Long D.T., Walter J.C., Hofmann K., Storchova Z., Cox J.,
RA Bekker-Jensen S., Mailand N., Mann M.;
RT "DNA repair. Proteomics reveals dynamic assembly of repair complexes during
RT bypass of DNA cross-links.";
RL Science 348:1253671-1253671(2015).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-931, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays a role in the DNA damage response (DDR) pathway by
CC regulating postreplication repair of UV-damaged DNA and genomic
CC stability maintenance (PubMed:25931565). The SLF1-SLF2 complex acts to
CC link RAD18 with the SMC5-SMC6 complex at replication-coupled
CC interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites
CC on chromatin during DNA repair in response to stalled replication forks
CC (PubMed:25931565). Promotes the recruitment of SLF2 and the SMC5-SMC6
CC complex to DNA lesions (PubMed:25931565).
CC {ECO:0000269|PubMed:25931565}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SLF2; this interaction links
CC RAD18 to the SMC5-SMC6 complex (PubMed:25931565). Interacts (via BRCT
CC domains) with RAD18; this interaction occurs in a SLF2-independent
CC manner (PubMed:25931565). Interacts with SMC6 (PubMed:25931565).
CC Interacts (via BRCT domains) with RAD18 (via C-terminus and
CC phosphorylated form); this interaction is required for efficient repair
CC of UV-induced DNA damage (By similarity).
CC {ECO:0000250|UniProtKB:Q8R3P9, ECO:0000269|PubMed:25931565}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25931565}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8R3P9}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8R3P9}.
CC Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage.
CC Colocalizes with RAD18 in the nucleus and to centrosomes (By
CC similarity). Associates with chromatin (PubMed:25931565). Accumulates
CC with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA
CC interstrand repair and DNA double-strand breaks (DSBs) sites on
CC chromatin in a ubiquitin-dependent manner (PubMed:25931565).
CC {ECO:0000250|UniProtKB:Q8R3P9, ECO:0000269|PubMed:25931565}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQI6-2; Sequence=VSP_056914, VSP_056915;
CC -!- DOMAIN: BRCT domains are necessary for its targeting to ionizing
CC radiation-induced nuclear foci. {ECO:0000250|UniProtKB:Q8R3P9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54885.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH54885.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH70332.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH70332.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI07572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB66495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK297452; BAG59876.1; -; mRNA.
DR EMBL; AC008534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054885; AAH54885.2; ALT_SEQ; mRNA.
DR EMBL; BC070332; AAH70332.1; ALT_SEQ; mRNA.
DR EMBL; BC107571; AAI07572.1; ALT_INIT; mRNA.
DR EMBL; AL050298; CAB43397.2; -; mRNA.
DR EMBL; AL136560; CAB66495.1; ALT_INIT; mRNA.
DR EMBL; CR533539; CAG38570.1; -; mRNA.
DR CCDS; CCDS4071.2; -. [Q9BQI6-1]
DR PIR; T08704; T08704.
DR RefSeq; NP_115666.2; NM_032290.3. [Q9BQI6-1]
DR RefSeq; XP_016865468.1; XM_017009979.1. [Q9BQI6-1]
DR AlphaFoldDB; Q9BQI6; -.
DR SMR; Q9BQI6; -.
DR BioGRID; 123978; 21.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q9BQI6; 9.
DR MINT; Q9BQI6; -.
DR STRING; 9606.ENSP00000265140; -.
DR iPTMnet; Q9BQI6; -.
DR PhosphoSitePlus; Q9BQI6; -.
DR BioMuta; SLF1; -.
DR DMDM; 193806371; -.
DR EPD; Q9BQI6; -.
DR jPOST; Q9BQI6; -.
DR MassIVE; Q9BQI6; -.
DR MaxQB; Q9BQI6; -.
DR PaxDb; Q9BQI6; -.
DR PeptideAtlas; Q9BQI6; -.
DR PRIDE; Q9BQI6; -.
DR ProteomicsDB; 4606; -.
DR ProteomicsDB; 78690; -. [Q9BQI6-1]
DR Antibodypedia; 24952; 140 antibodies from 20 providers.
DR DNASU; 84250; -.
DR Ensembl; ENST00000265140.10; ENSP00000265140.5; ENSG00000133302.13. [Q9BQI6-1]
DR Ensembl; ENST00000508130.5; ENSP00000424232.1; ENSG00000133302.13. [Q9BQI6-2]
DR GeneID; 84250; -.
DR KEGG; hsa:84250; -.
DR MANE-Select; ENST00000265140.10; ENSP00000265140.5; NM_032290.4; NP_115666.2.
DR UCSC; uc003kkr.5; human. [Q9BQI6-1]
DR CTD; 84250; -.
DR DisGeNET; 84250; -.
DR GeneCards; SLF1; -.
DR HGNC; HGNC:25408; SLF1.
DR HPA; ENSG00000133302; Low tissue specificity.
DR MIM; 618467; gene.
DR neXtProt; NX_Q9BQI6; -.
DR OpenTargets; ENSG00000133302; -.
DR PharmGKB; PA134911523; -.
DR VEuPathDB; HostDB:ENSG00000133302; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1929; Eukaryota.
DR GeneTree; ENSGT00940000158953; -.
DR HOGENOM; CLU_010529_0_0_1; -.
DR InParanoid; Q9BQI6; -.
DR OMA; MLLEIFW; -.
DR OrthoDB; 1003628at2759; -.
DR PhylomeDB; Q9BQI6; -.
DR TreeFam; TF329705; -.
DR PathwayCommons; Q9BQI6; -.
DR SignaLink; Q9BQI6; -.
DR BioGRID-ORCS; 84250; 38 hits in 1067 CRISPR screens.
DR ChiTaRS; SLF1; human.
DR GenomeRNAi; 84250; -.
DR Pharos; Q9BQI6; Tbio.
DR PRO; PR:Q9BQI6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9BQI6; protein.
DR Bgee; ENSG00000133302; Expressed in secondary oocyte and 157 other tissues.
DR ExpressionAtlas; Q9BQI6; baseline and differential.
DR Genevisible; Q9BQI6; HS.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IC:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IDA:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:1990166; P:protein localization to site of double-strand break; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR042479; Slf1.
DR PANTHER; PTHR46677; PTHR46677; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16770; RTT107_BRCT_5; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00292; BRCT; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1058
FT /note="SMC5-SMC6 complex localization factor protein 1"
FT /id="PRO_0000243906"
FT DOMAIN 12..77
FT /note="BRCT 1"
FT DOMAIN 119..196
FT /note="BRCT 2"
FT REPEAT 806..836
FT /note="ANK 1"
FT REPEAT 840..869
FT /note="ANK 2"
FT REPEAT 874..903
FT /note="ANK 3"
FT CROSSLNK 931
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 145..179
FT /note="VLEAGKANVILPKSSPSGITHVIASNARIKAEKEK -> KKFRMMKIPKPIL
FT FGLNIAMKKQTKISGKMQDFLK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056914"
FT VAR_SEQ 180..1058
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056915"
FT VARIANT 288
FT /note="S -> R (in dbSNP:rs6891545)"
FT /id="VAR_059120"
FT CONFLICT 24
FT /note="V -> A (in Ref. 4; CAB43397)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Q -> R (in Ref. 4; CAB43397)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> S (in Ref. 3; AAH54885)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> A (in Ref. 4; CAB43397)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="H -> Q (in Ref. 3; AAH70332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1058 AA; 121050 MW; C624008C7CC25FE6 CRC64;
MEDGTPKHII QMTGFKMEEK EALVKLLLKL DCTFIKSEKY KNCTHLIAER LCKSEKFLAA
CAAGKWILTK DYIIHSAKSG RWLDETTYEW GYKIEKDSRY SPQMQSAPKR WREELKRTGA
PGAFHRWKVV LLVRTDKRSD SLIRVLEAGK ANVILPKSSP SGITHVIASN ARIKAEKEKD
NFKAPFYPIQ YLGDFLLEKE IQNDEDSQTN SVWTEHSNEE TNKDFRKDAG FLEMKGALRE
TMYRTQKEMQ NHEDVNVGSI LIQHHKKEKF SGSSKDLKFV KMRNTFGSHT YENQKEIKKK
DEDIQRSYTL RRKRKKGKES NCKKGVEHEK IKSTLRRHIY NRDQKEMKNS IFAEYAKESK
AMAIKTDVDV VEIKNTLRKH IYRAQAVRYN CIRIDKQPVY NVEVKNAEFP RGVLNLIESL
IEGHFFKEAI EELSTLQAHY IPPVCVLHAL LENVLQDNID TFSGRYFHIL SALLHLHPPW
KSPAMSRYYL ELFQCPTCMK GAWSLVEVLI RSCLFNESFC HQISENIGSK VLHLTLLKFF
FNLIESEVQH LSQKLYDWSD SQNLKITGKA MLLEIFWSGS ETSGLLTKPV NMLLEWTIYS
HKEKFKSNDV FKHELAYLLA GILGAAIDYW IFLGLKMGRN VMRHMSDDLG SYVSLSCDDF
SSQELEIFIC SFSSSWLQMF VAEAVFKKLC LQSSGSVSSE PLSLQKMVYS YLPALGKTGV
LGSGKIQVSK KIGQRPCFDS QRTLLMLNGT KQKQVEGLPE LLDLNLAKCS SSLKKLKKKS
EGELSCSKEN CPSVVKKMNF HKTNLKGETA LHRACINNQV EKLILLLSLP GIDINVKDNA
GWTPLHEACN YGNTVCVQEI LQRCPEVDLL TQVDGVTPLH DALSNGHVEI GKLLLQHGGP
VLLQQRNAKG ELPLDYVVSP QIKEELFAIT KIEDTVENFH AQAEKHFHYQ QLEFGSFLLS
RMLLNFCSIF DLSSEFILAS KGLTHLNELL MACKSHKETT SVHTDWLLDL YAGNIKTLQK
LPHILKELPE NLKVCPGVHT EALMITLEMM CRSVMEFS
