EI24_HUMAN
ID EI24_HUMAN Reviewed; 340 AA.
AC O14681; A8K7D6; B4DKL6; Q9BUQ1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Etoposide-induced protein 2.4 homolog;
DE AltName: Full=p53-induced gene 8 protein;
GN Name=EI24; Synonyms=PIG8;
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] (ISOFORM 1), AND INDUCTION BY TP53.
RC TISSUE=Colon cancer;
RX PubMed=9305847; DOI=10.1038/38525;
RA Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.;
RT "A model for p53-induced apoptosis.";
RL Nature 389:300-306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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 POSSIBLE INVOLVEMENT IN BREAST CANCER, AND VARIANTS GLY-30; TRP-195;
RP ASP-196; TYR-197; HIS-199 AND ALA-319.
RX PubMed=11753653; DOI=10.1038/sj.onc.1204993;
RA Gentile M., Ahnstrom M., Schon F., Wingren S.;
RT "Candidate tumour suppressor genes at 11q23-q24 in breast cancer: evidence
RT of alterations in PIG8, a gene involved in p53-induced apoptosis.";
RL Oncogene 20:7753-7760(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP SUBCELLULAR LOCATION, AND POSSIBLE INVOLVEMENT IN CERVICAL CANCER.
RX PubMed=21154811; DOI=10.1002/ijc.25849;
RA Mazumder ' Indra ' D., Mitra S., Singh R.K., Dutta S., Roy A., Mondal R.K.,
RA Basu P.S., Roychoudhury S., Panda C.K.;
RT "Inactivation of CHEK1 and EI24 are associated with the development of
RT invasive cervical carcinoma: Clinical and prognostic implications.";
RL Int. J. Cancer 129:1859-1871(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as a negative growth regulator via p53-mediated
CC apoptosis pathway. Regulates formation of degradative autolysosomes
CC during autophagy (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BCL2. {ECO:0000250}.
CC -!- INTERACTION:
CC O14681; Q12982: BNIP2; NbExp=3; IntAct=EBI-2339413, EBI-752094;
CC O14681; O15173: PGRMC2; NbExp=3; IntAct=EBI-2339413, EBI-1050125;
CC O14681; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-2339413, EBI-712367;
CC O14681; Q6PL24: TMED8; NbExp=3; IntAct=EBI-2339413, EBI-11603430;
CC O14681; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2339413, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:21154811};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21154811}. Cytoplasm
CC {ECO:0000269|PubMed:21154811}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14681-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14681-3; Sequence=VSP_055466;
CC -!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:9305847}.
CC -!- DISEASE: Note=EI24 is on a chromosomal region frequently deleted in
CC solid tumors, and it is thought to play a role in breast and cervical
CC cancer. Particularly, expression analysis of EI24 in cancerous tissues
CC shows that EI24 loss is associated with tumor invasiveness.
CC -!- SIMILARITY: Belongs to the EI24 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC39531.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF010313; AAC39531.2; ALT_INIT; mRNA.
DR EMBL; AK291951; BAF84640.1; -; mRNA.
DR EMBL; AK296620; BAG59228.1; -; mRNA.
DR EMBL; AK315841; BAF98732.1; -; mRNA.
DR EMBL; CH471065; EAW67641.1; -; Genomic_DNA.
DR EMBL; BC002390; AAH02390.1; -; mRNA.
DR CCDS; CCDS73410.1; -. [O14681-1]
DR CCDS; CCDS76493.1; -. [O14681-3]
DR RefSeq; NP_001277064.1; NM_001290135.1. [O14681-3]
DR RefSeq; NP_004870.3; NM_004879.4. [O14681-1]
DR RefSeq; XP_011541371.1; XM_011543069.1. [O14681-1]
DR AlphaFoldDB; O14681; -.
DR BioGRID; 114914; 114.
DR IntAct; O14681; 24.
DR MINT; O14681; -.
DR STRING; 9606.ENSP00000278903; -.
DR TCDB; 2.A.121.3.1; the sulfate transporter (cysz) family.
DR iPTMnet; O14681; -.
DR PhosphoSitePlus; O14681; -.
DR BioMuta; EI24; -.
DR EPD; O14681; -.
DR jPOST; O14681; -.
DR MassIVE; O14681; -.
DR MaxQB; O14681; -.
DR PaxDb; O14681; -.
DR PeptideAtlas; O14681; -.
DR PRIDE; O14681; -.
DR ProteomicsDB; 48164; -. [O14681-1]
DR Antibodypedia; 32951; 177 antibodies from 31 providers.
DR DNASU; 9538; -.
DR Ensembl; ENST00000278903.11; ENSP00000278903.7; ENSG00000149547.15. [O14681-1]
DR Ensembl; ENST00000534546.5; ENSP00000479943.1; ENSG00000149547.15. [O14681-3]
DR Ensembl; ENST00000620753.4; ENSP00000484510.1; ENSG00000149547.15. [O14681-1]
DR GeneID; 9538; -.
DR KEGG; hsa:9538; -.
DR MANE-Select; ENST00000278903.11; ENSP00000278903.7; NM_004879.5; NP_004870.3.
DR UCSC; uc031yiu.2; human. [O14681-1]
DR CTD; 9538; -.
DR DisGeNET; 9538; -.
DR GeneCards; EI24; -.
DR HGNC; HGNC:13276; EI24.
DR HPA; ENSG00000149547; Tissue enhanced (parathyroid).
DR MIM; 605170; gene.
DR neXtProt; NX_O14681; -.
DR OpenTargets; ENSG00000149547; -.
DR PharmGKB; PA134937367; -.
DR VEuPathDB; HostDB:ENSG00000149547; -.
DR eggNOG; KOG3966; Eukaryota.
DR GeneTree; ENSGT00390000018633; -.
DR HOGENOM; CLU_031164_0_0_1; -.
DR InParanoid; O14681; -.
DR OMA; QCCALNG; -.
DR PhylomeDB; O14681; -.
DR TreeFam; TF314441; -.
DR PathwayCommons; O14681; -.
DR SignaLink; O14681; -.
DR BioGRID-ORCS; 9538; 15 hits in 268 CRISPR screens.
DR ChiTaRS; EI24; human.
DR GeneWiki; EI24; -.
DR GenomeRNAi; 9538; -.
DR Pharos; O14681; Tbio.
DR PRO; PR:O14681; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O14681; protein.
DR Bgee; ENSG00000149547; Expressed in secondary oocyte and 202 other tissues.
DR ExpressionAtlas; O14681; baseline and differential.
DR Genevisible; O14681; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:MGI.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:MGI.
DR InterPro; IPR009890; EI24.
DR PANTHER; PTHR21389; PTHR21389; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Autophagy; Cytoplasm;
KW Disease variant; Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..340
FT /note="Etoposide-induced protein 2.4 homolog"
FT /id="PRO_0000086945"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KM77"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KM77"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61070"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 15..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055466"
FT VARIANT 30
FT /note="D -> G (in some patients with early onset breast
FT cancer)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065459"
FT VARIANT 195
FT /note="P -> W (in some patients with early onset breast
FT cancer; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065460"
FT VARIANT 196
FT /note="I -> D (in some patients with early onset breast
FT cancer; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065461"
FT VARIANT 197
FT /note="H -> Y (in some patients with early onset breast
FT cancer)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065462"
FT VARIANT 199
FT /note="V -> H (in some patients with early onset breast
FT cancer; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065463"
FT VARIANT 319
FT /note="T -> A (in some patients with early onset breast
FT cancer; dbSNP:rs375652371)"
FT /evidence="ECO:0000269|PubMed:11753653"
FT /id="VAR_065464"
FT CONFLICT 54
FT /note="A -> P (in Ref. 1; AAC39531)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="E -> G (in Ref. 1; AAC39531)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="L -> V (in Ref. 1; AAC39531)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="L -> V (in Ref. 2; BAF84640)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="A -> S (in Ref. 2; BAG59228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 38965 MW; 928DB15D9B34146E CRC64;
MADSVKTFLQ DLARGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSVLA QRRAQSIERK
QESEPRIVSR IFQCCAWNGG VFWFSLLLFY RVFIPVLQSV TARIIGDPSL HGDVWSWLEF
FLTSIFSALW VLPLFVLSKV VNAIWFQDIA DLAFEVSGRK PHPFPSVSKI IADMLFNLLL
QALFLIQGMF VSLFPIHLVG QLVSLLHMSL LYSLYCFEYR WFNKGIEMHQ RLSNIERNWP
YYFGFGLPLA FLTAMQSSYI ISGCLFSILF PLFIISANEA KTPGKAYLFQ LRLFSLVVFL
SNRLFHKTVY LQSALSSSTS AEKFPSPHPS PAKLKATAGH
