ETAA1_HUMAN
ID ETAA1_HUMAN Reviewed; 926 AA.
AC Q9NY74; Q05BT7; Q53SC4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ewing's tumor-associated antigen 1 {ECO:0000312|HGNC:HGNC:24648};
DE AltName: Full=Ewing's tumor-associated antigen 16 {ECO:0000303|PubMed:16003559};
GN Name=ETAA1 {ECO:0000312|HGNC:HGNC:24648};
GN Synonyms=ETAA16 {ECO:0000303|PubMed:16003559};
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Ewing sarcoma;
RX PubMed=16003559; DOI=10.1007/s00262-005-0017-6;
RA Borowski A., Dirksen U., Lixin L., Shi R.L., Goebel U., Schneider E.M.;
RT "Structure and function of ETAA16: a novel cell surface antigen in Ewing's
RT tumours.";
RL Cancer Immunol. Immunother. 55:363-374(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-221; ASN-389 AND
RP SER-771.
RC TISSUE=Prostate, and Uterus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-464, AND
RP IDENTIFICATION BY 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-442, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-414; LYS-442; LYS-480;
RP LYS-507; LYS-533 AND LYS-535, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-50.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH RPA1 AND RPA2.
RX PubMed=27601467; DOI=10.1074/jbc.c116.747758;
RA Feng S., Zhao Y., Xu Y., Ning S., Huo W., Hou M., Gao G., Ji J., Guo R.,
RA Xu D.;
RT "Ewing Tumor-associated Antigen 1 interacts with replication protein A to
RT promote restart of stalled replication forks.";
RL J. Biol. Chem. 291:21956-21962(2016).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION, INTERACTION WITH
RP RPA1; RPA2 AND ATR, AND MUTAGENESIS OF TRP-107.
RX PubMed=27723720; DOI=10.1038/ncb3415;
RA Bass T.E., Luzwick J.W., Kavanaugh G., Carroll C., Dungrawala H.,
RA Glick G.G., Feldkamp M.D., Putney R., Chazin W.J., Cortez D.;
RT "ETAA1 acts at stalled replication forks to maintain genome integrity.";
RL Nat. Cell Biol. 18:1185-1195(2016).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH RPA1; RPA2 AND
RP ATR, PHOSPHORYLATION, AND MUTAGENESIS OF 106-PHE-TRP-107.
RX PubMed=27723717; DOI=10.1038/ncb3422;
RA Haahr P., Hoffmann S., Tollenaere M.A., Ho T., Toledo L.I., Mann M.,
RA Bekker-Jensen S., Raeschle M., Mailand N.;
RT "Activation of the ATR kinase by the RPA-binding protein ETAA1.";
RL Nat. Cell Biol. 18:1196-1207(2016).
CC -!- FUNCTION: Replication stress response protein that accumulates at DNA
CC damage sites and promotes replication fork progression and integrity
CC (PubMed:27601467, PubMed:27723720, PubMed:27723717). Recruited to
CC stalled replication forks via interaction with the RPA complex and
CC directly stimulates ATR kinase activity independently of TOPBP1
CC (PubMed:27723720, PubMed:27723717). Probably only regulates a subset of
CC ATR targets (PubMed:27723720, PubMed:27723717).
CC {ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717,
CC ECO:0000269|PubMed:27723720}.
CC -!- SUBUNIT: Interacts (via RBM1 motif) with RPA1 (PubMed:27601467,
CC PubMed:27723720, PubMed:27723717). Interacts (via RBM2 motif) with RPA2
CC (PubMed:27601467, PubMed:27723720, PubMed:27723717). Interacts (via the
CC ATR-activation domain motif) with ATR (PubMed:27723720,
CC PubMed:27723717). {ECO:0000269|PubMed:27601467,
CC ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27601467,
CC ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}.
CC Note=Localizes at sites of DNA damage following replication stress
CC (PubMed:27601467, PubMed:27723720, PubMed:27723717). Recruited to
CC stalled replication forks via interaction with RPA1 and RPA2 subunits
CC of the RPA complex (PubMed:27601467, PubMed:27723720).
CC {ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717,
CC ECO:0000269|PubMed:27723720}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the brain, liver kidney
CC and Ewing tumor cell lines. {ECO:0000269|PubMed:16003559}.
CC -!- DOMAIN: The RBM1 (RPA1-binding, also named RPA70N-binding) motif
CC mediates interaction with RPA1 (PubMed:27601467, PubMed:27723720,
CC PubMed:27723717). The RBM2 (RPA2-binding, also named RPA32C-binding)
CC motif mediates interaction with RPA2 (PubMed:27601467, PubMed:27723720,
CC PubMed:27723717). {ECO:0000269|PubMed:27601467,
CC ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}.
CC -!- DOMAIN: The ATR-activation domain (AAD) motif is required to bind and
CC activate ATR (PubMed:27723720, PubMed:27723717).
CC {ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}.
CC -!- PTM: Phosphorylated by ATR. {ECO:0000305|PubMed:27723717}.
CC -!- CAUTION: Initially reported to localize in the cytoplasm
CC (PubMed:16003559). A number of studies showed that it accumulates at
CC DNA damage sites in the nucleus (PubMed:27601467, PubMed:27723720,
CC PubMed:27723717). {ECO:0000269|PubMed:16003559,
CC ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717,
CC ECO:0000269|PubMed:27723720}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33075.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=AAX93100.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ242682; CAB76378.2; -; mRNA.
DR EMBL; AC023668; AAX93100.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC033075; AAH33075.1; ALT_SEQ; mRNA.
DR EMBL; BC040001; AAH40001.1; -; mRNA.
DR CCDS; CCDS1882.1; -.
DR RefSeq; NP_061875.2; NM_019002.3.
DR AlphaFoldDB; Q9NY74; -.
DR SMR; Q9NY74; -.
DR BioGRID; 119971; 142.
DR DIP; DIP-47294N; -.
DR IntAct; Q9NY74; 13.
DR MINT; Q9NY74; -.
DR STRING; 9606.ENSP00000272342; -.
DR GlyGen; Q9NY74; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NY74; -.
DR PhosphoSitePlus; Q9NY74; -.
DR BioMuta; ETAA1; -.
DR DMDM; 74734709; -.
DR EPD; Q9NY74; -.
DR jPOST; Q9NY74; -.
DR MassIVE; Q9NY74; -.
DR MaxQB; Q9NY74; -.
DR PaxDb; Q9NY74; -.
DR PeptideAtlas; Q9NY74; -.
DR PRIDE; Q9NY74; -.
DR ProteomicsDB; 83186; -.
DR Antibodypedia; 47441; 57 antibodies from 19 providers.
DR DNASU; 54465; -.
DR Ensembl; ENST00000272342.6; ENSP00000272342.5; ENSG00000143971.9.
DR GeneID; 54465; -.
DR KEGG; hsa:54465; -.
DR MANE-Select; ENST00000272342.6; ENSP00000272342.5; NM_019002.4; NP_061875.2.
DR UCSC; uc002sdz.2; human.
DR CTD; 54465; -.
DR DisGeNET; 54465; -.
DR GeneCards; ETAA1; -.
DR HGNC; HGNC:24648; ETAA1.
DR HPA; ENSG00000143971; Low tissue specificity.
DR MIM; 613196; gene.
DR neXtProt; NX_Q9NY74; -.
DR OpenTargets; ENSG00000143971; -.
DR PharmGKB; PA162385444; -.
DR VEuPathDB; HostDB:ENSG00000143971; -.
DR eggNOG; ENOG502QTMP; Eukaryota.
DR GeneTree; ENSGT00390000009597; -.
DR HOGENOM; CLU_015351_0_0_1; -.
DR OMA; CITGSMS; -.
DR OrthoDB; 365628at2759; -.
DR PhylomeDB; Q9NY74; -.
DR TreeFam; TF333863; -.
DR PathwayCommons; Q9NY74; -.
DR SignaLink; Q9NY74; -.
DR BioGRID-ORCS; 54465; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; ETAA1; human.
DR GenomeRNAi; 54465; -.
DR Pharos; Q9NY74; Tbio.
DR PRO; PR:Q9NY74; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NY74; protein.
DR Bgee; ENSG00000143971; Expressed in secondary oocyte and 145 other tissues.
DR ExpressionAtlas; Q9NY74; baseline and differential.
DR Genevisible; Q9NY74; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IDA:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR InterPro; IPR029406; ETAA1.
DR PANTHER; PTHR16434; PTHR16434; 2.
DR Pfam; PF15350; ETAA1; 2.
PE 1: Evidence at protein level;
KW Coiled coil; DNA damage; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..926
FT /note="Ewing's tumor-associated antigen 1"
FT /id="PRO_0000280099"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..214
FT /evidence="ECO:0000255"
FT MOTIF 105..111
FT /note="ATR-activation domain (AAD)"
FT /evidence="ECO:0000269|PubMed:27723717,
FT ECO:0000269|PubMed:27723720"
FT MOTIF 603..618
FT /note="RBM1 motif"
FT /evidence="ECO:0000269|PubMed:27601467,
FT ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720"
FT MOTIF 891..913
FT /note="RBM2 motif"
FT /evidence="ECO:0000269|PubMed:27601467,
FT ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 533
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 535
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 50
FT /note="E -> D (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035916"
FT VARIANT 221
FT /note="M -> T (in dbSNP:rs13036061)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031053"
FT VARIANT 389
FT /note="S -> N (in dbSNP:rs3770657)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031054"
FT VARIANT 715
FT /note="P -> L (in dbSNP:rs3770656)"
FT /id="VAR_031055"
FT VARIANT 771
FT /note="P -> S (in dbSNP:rs3770655)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031056"
FT MUTAGEN 106..107
FT /note="FW->AA: Reduced ability to promote replication fork
FT progression and integrity following DNA damage."
FT /evidence="ECO:0000269|PubMed:27723717"
FT MUTAGEN 107
FT /note="W->A: Reduced interaction with ATR."
FT /evidence="ECO:0000269|PubMed:27723720"
FT CONFLICT 439
FT /note="G -> R (in Ref. 3; AAH33075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 103440 MW; 4AD88EDD71BADED0 CRC64;
MSRRRKHDDS PSPKKTPHKT VAAEECGSVV EPGRRRLRSA RGSWPCGARE GPPGPVRQRE
QPPTAALCSK SNPEERYETP KRALKMDSLS SSFSSPNDPD GQNDIFWDQN SPLTKQLGKG
RKKQIYTTDS DEISHIVNRI APQDEKPTTN SMLDMWIGET AIPCTPSVAK GKSRAKISCT
KLKTQSQEEE LMKLAKQFDK NMEELDVIQE QNKRNYDFTQ MISETEILSN YKDNIQMWSL
HNIVPEIDNA TKKPIKGNTK ISVANNQNSS QKPFDQIAEA AFNAIFDGST QKCSGQLSQE
LPEAFWSTSN TTFVKTNALK EEKIITNETL VIEKLSNKTP RSLSSQVDTP IMTKSCVTSC
TKEPETSNKY IDAFTTSDFE DDWENLLGSE PFAMQNIDMP ELFPSKTAHV TDQKEICTFN
SKTVKNTSRA NTSPDARLGD SKVLQDLSSK TYDRELIDAE YRFSPNSNKS NKLSTGNKMK
FENSSNKIVI QDEIQNCIVT SNLTKIKEDI LTNSTEASER KSALNTRYSN EQKNKCILNQ
SIKAPVNTDL FGSANLGSKT SVSNPNQTSA SKVGSFFDDW NDPSFANEII KACHQLDNTW
EADDVDDDLL YQACDDIERL TQQQDIRKDS KTSESICEIN NNSEHGAKLT QQQDIRKDSK
TSESICEINN NSEHGAKNMF AISKQGSNLV QSKHLNPGSI SVQTSLTNSS QIDKPMKMEK
GEMYGNSPRF LGATNLTMYS KISNCQINNL HVSYTNTDVP IQVNSSKLVL PGSSSLNVTS
DHMNTEITTY KKKLSTNQPC HKTVTDEAQS NLNTTVGFSK FTFTRMKNSQ ILSQFNQNCI
TGSMSDTKIT QGVEKKKGVN PLLEEAVGQQ SLVKLSESLK QSSKEEEEKN RKCSPEEIQR
KRQEALVRRM AKARASSVNA APTSFL
