ZN143_HUMAN
ID ZN143_HUMAN Reviewed; 638 AA.
AC P52747; A8K518; B4DLY5; E7ER34; O75559; Q8WUK9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Zinc finger protein 143;
DE AltName: Full=SPH-binding factor;
DE AltName: Full=Selenocysteine tRNA gene transcription-activating factor;
DE Short=hStaf;
GN Name=ZNF143; Synonyms=SBF, STAF;
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] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP GLN-561.
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=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-561.
RC TISSUE=Muscle;
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 [MRNA] OF 3-638 (ISOFORM 1).
RC TISSUE=Insulinoma;
RX PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA Tommerup N., Vissing H.;
RT "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT identify putative candidate genes for developmental and malignant
RT disorders.";
RL Genomics 27:259-264(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-638 (ISOFORMS 1/2), VARIANT GLN-561, AND
RP FUNCTION.
RX PubMed=9776743; DOI=10.1093/nar/26.21.4846;
RA Rincon J.C., Engler S.K., Hargrove B.W., Kunkel G.R.;
RT "Molecular cloning of a cDNA encoding human SPH-binding factor, a conserved
RT protein that binds to the enhancer-like region of the U6 small nuclear RNA
RT gene promoter.";
RL Nucleic Acids Res. 26:4846-4852(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH CHD8.
RX PubMed=17938208; DOI=10.1128/mcb.00846-07;
RA Yuan C.-C., Zhao X., Florens L., Swanson S.K., Washburn M.P., Hernandez N.;
RT "CHD8 associates with human Staf and contributes to efficient U6 RNA
RT polymerase III transcription.";
RL Mol. Cell. Biol. 27:8729-8738(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-213 AND LYS-406, AND
RP 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: Transcriptional activator. Activates the gene for
CC selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear
CC RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase
CC III transcription via its interaction with CHD8.
CC {ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:9776743}.
CC -!- SUBUNIT: Interacts with CHD8. {ECO:0000269|PubMed:17938208}.
CC -!- INTERACTION:
CC P52747; Q96JC9: EAF1; NbExp=3; IntAct=EBI-2849334, EBI-769261;
CC P52747; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2849334, EBI-744099;
CC P52747; Q9Y3B2: EXOSC1; NbExp=3; IntAct=EBI-2849334, EBI-371892;
CC P52747; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2849334, EBI-6658203;
CC P52747; Q14192: FHL2; NbExp=3; IntAct=EBI-2849334, EBI-701903;
CC P52747; Q14005-2: IL16; NbExp=3; IntAct=EBI-2849334, EBI-17178971;
CC P52747; Q8NA54: IQUB; NbExp=3; IntAct=EBI-2849334, EBI-10220600;
CC P52747; Q6MZP7: LIN54; NbExp=3; IntAct=EBI-2849334, EBI-1389411;
CC P52747; P25800: LMO1; NbExp=3; IntAct=EBI-2849334, EBI-8639312;
CC P52747; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2849334, EBI-11742507;
CC P52747; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-2849334, EBI-10297093;
CC P52747; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2849334, EBI-1389308;
CC P52747; P14678-2: SNRPB; NbExp=3; IntAct=EBI-2849334, EBI-372475;
CC P52747; Q5MJ09: SPANXN3; NbExp=3; IntAct=EBI-2849334, EBI-12037215;
CC P52747; P51687: SUOX; NbExp=3; IntAct=EBI-2849334, EBI-3921347;
CC P52747; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-2849334, EBI-358708;
CC P52747; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-2849334, EBI-11974855;
CC P52747; Q9BW85: YJU2; NbExp=3; IntAct=EBI-2849334, EBI-10300345;
CC P52747; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-2849334, EBI-11962468;
CC P52747; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-2849334, EBI-1049952;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P52747-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52747-2; Sequence=VSP_036978;
CC Name=3;
CC IsoId=P52747-3; Sequence=VSP_055109;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with the strongest
CC expression in ovary.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH20219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAF83822.1; Type=Erroneous initiation; Evidence={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; AK291133; BAF83822.1; ALT_INIT; mRNA.
DR EMBL; AK297214; BAG59697.1; -; mRNA.
DR EMBL; AK313330; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC127030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020219; AAH20219.1; ALT_INIT; mRNA.
DR EMBL; U09850; AAC50266.1; ALT_INIT; mRNA.
DR EMBL; AF071771; AAC96102.1; -; mRNA.
DR CCDS; CCDS60720.1; -. [P52747-3]
DR CCDS; CCDS60721.1; -. [P52747-2]
DR CCDS; CCDS7799.2; -. [P52747-1]
DR PIR; I38618; I38618.
DR RefSeq; NP_001269585.1; NM_001282656.1. [P52747-3]
DR RefSeq; NP_001269586.1; NM_001282657.1. [P52747-2]
DR RefSeq; NP_003433.3; NM_003442.5. [P52747-1]
DR RefSeq; XP_011518651.1; XM_011520349.2. [P52747-1]
DR RefSeq; XP_016873743.1; XM_017018254.1. [P52747-3]
DR RefSeq; XP_016873744.1; XM_017018255.1. [P52747-3]
DR AlphaFoldDB; P52747; -.
DR SMR; P52747; -.
DR BioGRID; 113496; 45.
DR CORUM; P52747; -.
DR IntAct; P52747; 31.
DR MINT; P52747; -.
DR STRING; 9606.ENSP00000379847; -.
DR GlyGen; P52747; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52747; -.
DR PhosphoSitePlus; P52747; -.
DR BioMuta; ZNF143; -.
DR DMDM; 229462806; -.
DR EPD; P52747; -.
DR jPOST; P52747; -.
DR MassIVE; P52747; -.
DR MaxQB; P52747; -.
DR PaxDb; P52747; -.
DR PeptideAtlas; P52747; -.
DR PRIDE; P52747; -.
DR ProteomicsDB; 17706; -.
DR ProteomicsDB; 56522; -. [P52747-1]
DR ProteomicsDB; 56523; -. [P52747-2]
DR Antibodypedia; 927; 90 antibodies from 24 providers.
DR DNASU; 7702; -.
DR Ensembl; ENST00000396597.7; ENSP00000379843.3; ENSG00000166478.10. [P52747-2]
DR Ensembl; ENST00000396602.7; ENSP00000379847.2; ENSG00000166478.10. [P52747-1]
DR Ensembl; ENST00000396604.5; ENSP00000379849.1; ENSG00000166478.10. [P52747-3]
DR Ensembl; ENST00000530463.5; ENSP00000432154.1; ENSG00000166478.10. [P52747-3]
DR GeneID; 7702; -.
DR KEGG; hsa:7702; -.
DR MANE-Select; ENST00000396602.7; ENSP00000379847.2; NM_003442.6; NP_003433.3.
DR UCSC; uc001mhr.3; human. [P52747-1]
DR CTD; 7702; -.
DR DisGeNET; 7702; -.
DR GeneCards; ZNF143; -.
DR GeneReviews; ZNF143; -.
DR HGNC; HGNC:12928; ZNF143.
DR HPA; ENSG00000166478; Low tissue specificity.
DR MalaCards; ZNF143; -.
DR MIM; 603433; gene.
DR neXtProt; NX_P52747; -.
DR OpenTargets; ENSG00000166478; -.
DR PharmGKB; PA37515; -.
DR VEuPathDB; HostDB:ENSG00000166478; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157584; -.
DR HOGENOM; CLU_027168_0_0_1; -.
DR InParanoid; P52747; -.
DR OMA; GTEGQQX; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P52747; -.
DR TreeFam; TF333498; -.
DR PathwayCommons; P52747; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; P52747; -.
DR SIGNOR; P52747; -.
DR BioGRID-ORCS; 7702; 139 hits in 1099 CRISPR screens.
DR ChiTaRS; ZNF143; human.
DR GeneWiki; ZNF143; -.
DR GenomeRNAi; 7702; -.
DR Pharos; P52747; Tbio.
DR PRO; PR:P52747; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P52747; protein.
DR Bgee; ENSG00000166478; Expressed in calcaneal tendon and 172 other tissues.
DR ExpressionAtlas; P52747; baseline and differential.
DR Genevisible; P52747; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; EXP:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; TAS:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 5.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; 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..638
FT /note="Zinc finger protein 143"
FT /id="PRO_0000047426"
FT ZN_FING 237..261
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 267..291
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 297..321
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..351
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..381
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 387..411
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 417..440
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 39..69
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036978"
FT VAR_SEQ 97..98
FT /note="TG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055109"
FT VARIANT 461
FT /note="G -> D (in dbSNP:rs34972213)"
FT /id="VAR_061937"
FT VARIANT 561
FT /note="E -> Q (in dbSNP:rs10743108)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9776743"
FT /id="VAR_027254"
FT CONFLICT 433
FT /note="A -> V (in Ref. 3; AAH20219)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="T -> A (in Ref. 1; AK313330)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="Missing (in Ref. 1; BAG59697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 68896 MW; D149030016A6058A CRC64;
MLLAQINRDS QGMTEFPGGG MEAQHVTLCL TEAVTVADGD NLENMEGVSL QAVTLADGST
AYIQHNSKDA KLIDGQVIQL EDGSAAYVQH VPIPKSTGDS LRLEDGQAVQ LEDGTTAFIH
HTSKDSYDQS ALQAVQLEDG TTAYIHHAVQ VPQSDTILAI QADGTVAGLH TGDATIDPDT
ISALEQYAAK VSIDGSESVA GTGMIGENEQ EKKMQIVLQG HATRVTAKSQ QSGEKAFRCE
YDGCGKLYTT AHHLKVHERS HTGDRPYQCE HAGCGKAFAT GYGLKSHVRT HTGEKPYRCS
EDNCTKSFKT SGDLQKHIRT HTGERPFKCP FEGCGRSFTT SNIRKVHVRT HTGERPYYCT
EPGCGRAFAS ATNYKNHVRI HTGEKPYVCT VPGCDKRFTE YSSLYKHHVV HTHSKPYNCN
HCGKTYKQIS TLAMHKRTAH NDTEPIEEEQ EAFFEPPPGQ GEDVLKGSQI TYVTGVEGDD
VVSTQVATVT QSGLSQQVTL ISQDGTQHVN ISQADMQAIG NTITMVTQDG TPITVPAHDA
VISSAGTHSV AMVTAEGTEG EQVAIVAQDL AAFHTASSEM GHQQHSHHLV TTETRPLTLV
ATSNGTQIAV QLGEQPSLEE AIRIASRIQQ GETPGLDD
