Z518A_HUMAN
ID Z518A_HUMAN Reviewed; 1483 AA.
AC Q6AHZ1; A0PJI5; O15044; Q32MP4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Zinc finger protein 518A;
GN Name=ZNF518A; Synonyms=KIAA0335, ZNF518;
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 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-338 (ISOFORM 1).
RC TISSUE=Lung;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-713 AND LYS-994, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-357; LYS-713; LYS-994 AND
RP LYS-1446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-357; LYS-392; LYS-425;
RP LYS-433; LYS-524; LYS-596; LYS-713; LYS-798; LYS-889; LYS-902; LYS-928;
RP LYS-994; LYS-1015; LYS-1048; LYS-1060; LYS-1083; LYS-1121; LYS-1185 AND
RP LYS-1446, AND IDENTIFICATION BY MASS 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: Through its association with the EHMT1-EHMT2/G9A and
CC PRC2/EED-EZH2 histone methyltransferase complexes may function in gene
CC silencing, regulating repressive post-translational methylation of
CC histone tails at promoters of target genes.
CC {ECO:0000250|UniProtKB:B2RRF6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B2RRF6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AHZ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AHZ1-2; Sequence=VSP_019436;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30967.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA20793.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002333; BAA20793.2; ALT_INIT; mRNA.
DR EMBL; CR627437; CAH10523.1; -; mRNA.
DR EMBL; BC030967; AAH30967.1; ALT_SEQ; mRNA.
DR EMBL; BC109045; AAI09046.1; -; mRNA.
DR EMBL; BC109046; AAI09047.1; -; mRNA.
DR CCDS; CCDS73170.1; -. [Q6AHZ1-1]
DR RefSeq; NP_001265453.1; NM_001278524.1. [Q6AHZ1-1]
DR RefSeq; NP_001265454.1; NM_001278525.1. [Q6AHZ1-1]
DR RefSeq; NP_001265455.1; NM_001278526.1. [Q6AHZ1-2]
DR RefSeq; NP_001317661.1; NM_001330732.1. [Q6AHZ1-1]
DR RefSeq; NP_001317662.1; NM_001330733.1. [Q6AHZ1-1]
DR RefSeq; NP_001317663.1; NM_001330734.1. [Q6AHZ1-1]
DR RefSeq; NP_001317664.1; NM_001330735.1. [Q6AHZ1-1]
DR RefSeq; NP_001317665.1; NM_001330736.1. [Q6AHZ1-1]
DR RefSeq; NP_001317666.1; NM_001330737.1. [Q6AHZ1-1]
DR RefSeq; NP_001317667.1; NM_001330738.1. [Q6AHZ1-1]
DR RefSeq; NP_055618.2; NM_014803.3. [Q6AHZ1-1]
DR RefSeq; XP_011538708.1; XM_011540406.2. [Q6AHZ1-1]
DR RefSeq; XP_011538710.1; XM_011540408.2.
DR RefSeq; XP_011538712.1; XM_011540410.2. [Q6AHZ1-1]
DR RefSeq; XP_011538714.1; XM_011540412.2. [Q6AHZ1-1]
DR RefSeq; XP_011538715.1; XM_011540413.2. [Q6AHZ1-1]
DR RefSeq; XP_011538717.1; XM_011540415.2. [Q6AHZ1-1]
DR RefSeq; XP_011538720.1; XM_011540418.2. [Q6AHZ1-1]
DR RefSeq; XP_011538721.1; XM_011540419.2. [Q6AHZ1-1]
DR RefSeq; XP_011538722.1; XM_011540420.2. [Q6AHZ1-1]
DR RefSeq; XP_016872475.1; XM_017016986.1. [Q6AHZ1-1]
DR RefSeq; XP_016872478.1; XM_017016989.1. [Q6AHZ1-1]
DR RefSeq; XP_016872481.1; XM_017016992.1. [Q6AHZ1-1]
DR RefSeq; XP_016872483.1; XM_017016994.1. [Q6AHZ1-1]
DR RefSeq; XP_016872486.1; XM_017016997.1.
DR RefSeq; XP_016872487.1; XM_017016998.1. [Q6AHZ1-1]
DR RefSeq; XP_016872488.1; XM_017016999.1. [Q6AHZ1-1]
DR AlphaFoldDB; Q6AHZ1; -.
DR BioGRID; 115184; 40.
DR IntAct; Q6AHZ1; 39.
DR MINT; Q6AHZ1; -.
DR STRING; 9606.ENSP00000485614; -.
DR GlyGen; Q6AHZ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6AHZ1; -.
DR PhosphoSitePlus; Q6AHZ1; -.
DR BioMuta; ZNF518A; -.
DR DMDM; 109896331; -.
DR EPD; Q6AHZ1; -.
DR jPOST; Q6AHZ1; -.
DR MassIVE; Q6AHZ1; -.
DR MaxQB; Q6AHZ1; -.
DR PeptideAtlas; Q6AHZ1; -.
DR PRIDE; Q6AHZ1; -.
DR ProteomicsDB; 66181; -. [Q6AHZ1-1]
DR ProteomicsDB; 66182; -. [Q6AHZ1-2]
DR Antibodypedia; 30696; 24 antibodies from 10 providers.
DR DNASU; 9849; -.
DR Ensembl; ENST00000316045.10; ENSP00000479684.1; ENSG00000177853.15. [Q6AHZ1-1]
DR Ensembl; ENST00000614149.2; ENSP00000481657.1; ENSG00000177853.15. [Q6AHZ1-1]
DR Ensembl; ENST00000624776.4; ENSP00000485614.1; ENSG00000177853.15. [Q6AHZ1-1]
DR GeneID; 9849; -.
DR KEGG; hsa:9849; -.
DR MANE-Select; ENST00000316045.10; ENSP00000479684.1; NM_001330736.2; NP_001317665.1.
DR UCSC; uc031wpm.2; human. [Q6AHZ1-1]
DR CTD; 9849; -.
DR DisGeNET; 9849; -.
DR GeneCards; ZNF518A; -.
DR HGNC; HGNC:29009; ZNF518A.
DR HPA; ENSG00000177853; Low tissue specificity.
DR MIM; 617733; gene.
DR neXtProt; NX_Q6AHZ1; -.
DR OpenTargets; ENSG00000177853; -.
DR PharmGKB; PA162410182; -.
DR VEuPathDB; HostDB:ENSG00000177853; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162006; -.
DR HOGENOM; CLU_005711_0_0_1; -.
DR InParanoid; Q6AHZ1; -.
DR OMA; LVTCELC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6AHZ1; -.
DR PathwayCommons; Q6AHZ1; -.
DR SignaLink; Q6AHZ1; -.
DR BioGRID-ORCS; 9849; 17 hits in 222 CRISPR screens.
DR ChiTaRS; ZNF518A; human.
DR GenomeRNAi; 9849; -.
DR Pharos; Q6AHZ1; Tdark.
DR PRO; PR:Q6AHZ1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q6AHZ1; protein.
DR Bgee; ENSG00000177853; Expressed in buccal mucosa cell and 198 other tissues.
DR ExpressionAtlas; Q6AHZ1; baseline and differential.
DR Genevisible; Q6AHZ1; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR027760; ZNF518A.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403:SF81; PTHR24403:SF81; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1483
FT /note="Zinc finger protein 518A"
FT /id="PRO_0000240849"
FT ZN_FING 150..172
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 207..229
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 234..256
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 262..285
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1449..1471
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 350..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 433
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 524
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 713
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 798
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 889
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 902
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 928
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 994
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 1015
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1048
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1060
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1083
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1446
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..530
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019436"
FT VARIANT 946
FT /note="N -> H (in dbSNP:rs3814228)"
FT /id="VAR_046310"
FT VARIANT 1328
FT /note="R -> Q (in dbSNP:rs3814226)"
FT /id="VAR_046311"
FT CONFLICT 231
FT /note="E -> G (in Ref. 4; AAH30967)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="M -> V (in Ref. 3; CAH10523)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1483 AA; 166782 MW; 8202CFBDD12F9CB0 CRC64;
MPSEQKQLFC DEKQTTLKKD YDVKNEIVDR SAPKPKISGS IHYALKNVKI DLPKINIPNE
VLLKHEVDKY RKLFQSKQQT ARKSISIKTV SCVEECTLLH KSERAEEEGV KMSAKILNFS
CLKCRDNTRY SPNDLQKHFQ MWHHGELPSY PCEMCNFSAN DFQVFKQHRR THRSTLVKCD
ICNNESVYTL LNLTKHFTST HCVNGNFQCE KCKFSTQDVG TFVQHIHRHN EIHYKCGKCH
HVCFTKGELQ KHLHIHSGTF PFTCQYCSYG ATRREHLVRH VITLHKEHLY AKEKLEKDKY
EKRMAKTSAG LKLILKRYKI GASRKTFWKR KKINSGSDRS IEKNTQVLKK MNKTQTKSED
QSHVVQEHLS EEKDERLHCE NNDKAPESES EKPTPLSTGQ GNRAEEGPNA SSGFMKTAVL
GPTLKNVMMK NNKLAVSPNY NATFMGFKMM DGKQHIVLKL VPIKQNVCSP GSQSGAAKDG
TANLQPQTLD TNGFLTGVTT ELNDTVYMKA ATPFSCSSSI LSGKASSEKE MTLISQRNNM
LQTMDYEKSV SSLSATSELV TASVNLTTKF ETRDNVDFWG NHLTQSHPEV LGTTIKSPDK
VNCVAKPNAY NSGDMHNYCI NYGNCELPVE SSNQGSLPFH NYSKVNNSNK RRRFSGTAVY
ENPQRESSSS KTVVQQPISE SFLSLVRQES SKPDSLLASI SLLNDKDGTL KAKSEIEEQY
VLEKGQNIDG QNLYSNENQN LECATEKSKW EDFSNVDSPM MPRITSVFSL QSQQASEFLP
PEVNQLLQDV LKIKPDVKQD SSNTPNKGLP LHCDQSFQKH EREGKIVESS KDFKVQGIFP
VPPGSVGINV PTNDLNLKFG KEKQVSSIPQ DVRDSEKMPR ISGFGTLLKT QSDAIITQQL
VKDKLRATTQ NLGSFYMQSP LLNSEQKKTI IVQTSKGFLI PLNITNKPGL PVIPGNALPL
VNSQGIPASL FVNKKPGMVL TLNNGKLEGV SAVKTEGAPA RGTVTKEPCK TPILKVEPNN
NCLTPGLCSS IGSCLSMKSS SENTLPLKGP YILKPTSSVK AVLIPNMLSE QQSTKLNISD
SVKQQNEIFP KPPLYTFLPD GKQAVFLKCV MPNKTELLKP KLVQNSTYQN IQPKKPEGTP
QRILLKIFNP VLNVTAANNL SVSNSASSLQ KDNVPSNQII GGEQKEPESR DALPFLLDDL
MPANEIVITS TATCPESSEE PICVSDCSES RVLRCKTNCR IERNFNRKKT SKKIFSKTKT
HGSKDSETAF VSRNRNCKRK CRDSYQEPPR RKATLHRKCK EKAKPEDVRE TFGFSRPRLS
KDSIRTLRLF PFSSKQLVKC PRRNQPVVVL NHPDADAPEV VSVMKTIAKF NGHVLKVSLS
KRTINALLKP VCYNPPKTTY DDFSKRHKTF KPVSSVKERF VLKLTLKKTS KNNYQIVKTT
SENILKAKFN CWFCGRVFDN QDTWAGHGQR HLMEATRDWN MLE
