RETR2_HUMAN
ID RETR2_HUMAN Reviewed; 543 AA.
AC Q8NC44; Q6P1P5; Q9H0K7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Reticulophagy regulator 2 {ECO:0000312|HGNC:HGNC:28450};
GN Name=RETREG2 {ECO:0000312|HGNC:HGNC:28450};
GN Synonyms=C2orf17, FAM134A, MAG2 {ECO:0000312|HGNC:HGNC:28450};
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], AND VARIANT GLN-419.
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=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] OF 262-543, AND VARIANT GLN-419.
RC TISSUE=Skin;
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 431-543.
RC TISSUE=Testis;
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 [5]
RP SEQUENCE REVISION.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-385, AND
RP IDENTIFICATION BY 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-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-281 AND SER-283,
RP VARIANT [LARGE SCALE ANALYSIS] GLN-419, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-347, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-311; SER-347 AND
RP SER-385, AND IDENTIFICATION BY 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).
RN [15]
RP INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP AND GABARAPL1, AND DOMAIN.
RX PubMed=26040720; DOI=10.1038/nature14498;
RA Khaminets A., Heinrich T., Mari M., Grumati P., Huebner A.K., Akutsu M.,
RA Liebmann L., Stolz A., Nietzsche S., Koch N., Mauthe M., Katona I.,
RA Qualmann B., Weis J., Reggiori F., Kurth I., Huebner C.A., Dikic I.;
RT "Regulation of endoplasmic reticulum turnover by selective autophagy.";
RL Nature 522:354-358(2015).
CC -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
CC MAP1LC3B, GABARAP, and GABARAPL1. {ECO:0000269|PubMed:26040720}.
CC -!- INTERACTION:
CC Q8NC44; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-712899, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins.
CC {ECO:0000269|PubMed:26040720}.
CC -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR EMBL; AK074983; BAC11332.1; -; mRNA.
DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC064950; AAH64950.1; -; mRNA.
DR EMBL; AL136758; CAB66692.2; -; mRNA.
DR CCDS; CCDS2434.1; -.
DR RefSeq; NP_077269.3; NM_024293.5.
DR PDB; 6EWC; X-ray; 3.20 A; C/G=400-408.
DR PDBsum; 6EWC; -.
DR AlphaFoldDB; Q8NC44; -.
DR SMR; Q8NC44; -.
DR BioGRID; 122558; 45.
DR DIP; DIP-56781N; -.
DR IntAct; Q8NC44; 31.
DR MINT; Q8NC44; -.
DR STRING; 9606.ENSP00000395249; -.
DR iPTMnet; Q8NC44; -.
DR PhosphoSitePlus; Q8NC44; -.
DR BioMuta; RETREG2; -.
DR DMDM; 296439357; -.
DR EPD; Q8NC44; -.
DR jPOST; Q8NC44; -.
DR MassIVE; Q8NC44; -.
DR MaxQB; Q8NC44; -.
DR PaxDb; Q8NC44; -.
DR PeptideAtlas; Q8NC44; -.
DR PRIDE; Q8NC44; -.
DR ProteomicsDB; 72849; -.
DR Antibodypedia; 2502; 43 antibodies from 16 providers.
DR DNASU; 79137; -.
DR Ensembl; ENST00000430297.7; ENSP00000395249.2; ENSG00000144567.11.
DR GeneID; 79137; -.
DR KEGG; hsa:79137; -.
DR MANE-Select; ENST00000430297.7; ENSP00000395249.2; NM_024293.6; NP_077269.3.
DR UCSC; uc002vjw.5; human.
DR CTD; 79137; -.
DR DisGeNET; 79137; -.
DR GeneCards; RETREG2; -.
DR HGNC; HGNC:28450; RETREG2.
DR HPA; ENSG00000144567; Low tissue specificity.
DR neXtProt; NX_Q8NC44; -.
DR OpenTargets; ENSG00000144567; -.
DR PharmGKB; PA162386165; -.
DR VEuPathDB; HostDB:ENSG00000144567; -.
DR eggNOG; ENOG502QPTN; Eukaryota.
DR GeneTree; ENSGT00940000162511; -.
DR HOGENOM; CLU_036265_2_1_1; -.
DR InParanoid; Q8NC44; -.
DR OMA; TSPLHFV; -.
DR OrthoDB; 901531at2759; -.
DR PhylomeDB; Q8NC44; -.
DR TreeFam; TF329111; -.
DR PathwayCommons; Q8NC44; -.
DR SignaLink; Q8NC44; -.
DR BioGRID-ORCS; 79137; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; FAM134A; human.
DR GenomeRNAi; 79137; -.
DR Pharos; Q8NC44; Tdark.
DR PRO; PR:Q8NC44; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NC44; protein.
DR Bgee; ENSG00000144567; Expressed in sperm and 196 other tissues.
DR ExpressionAtlas; Q8NC44; baseline and differential.
DR Genevisible; Q8NC44; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0061709; P:reticulophagy; IEA:Ensembl.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..543
FT /note="Reticulophagy regulator 2"
FT /id="PRO_0000089346"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 254..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 490..495
FT /note="LIR motif"
FT /evidence="ECO:0000305|PubMed:26040720"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS82"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NS82"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 374
FT /note="R -> H (in dbSNP:rs3210652)"
FT /id="VAR_033720"
FT VARIANT 419
FT /note="P -> Q (in dbSNP:rs3731900)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648"
FT /id="VAR_022835"
FT CONFLICT 338
FT /note="E -> G (in Ref. 1; BAC11332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 57830 MW; 03DD659722BA9E5B CRC64;
MASGGGGGNT GAGGGPGMGL SLGLGLGLSL GMSEATSEAE EEAATAEAVG RLATTLWLRL
RGWEAVLAAA QRLLVWEKPL HSLVTAAALN GLFWLLSSSS LRPFFLLSVS LLAYFLLDLW
QPRFLPDVSA SSPEEPHSDS EGAGSGARPH LLSVPELCRY LAESWLTFQI HLQELLQYKR
QNPAQFCVRV CSGCAVLAVL GHYVPGIMIS YIVLLSILLW PLVVYHELIQ RMYTRLEPLL
MQLDYSMKAE ANALHHKHDK RKRQGKNAPP GGDEPLAETE SESEAELAGF SPVVDVKKTA
LALAITDSEL SDEEASILES GGFSVSRATT PQLTDVSEDL DQQSLPSEPE ETLSRDLGEG
EEGELAPPED LLGRPQALSR QALDSEEEEE DVAAKETLLR LSSPLHFVNT HFNGAGSPPD
GVKCSPGGPV ETLSPETVSG GLTALPGTLS PPLCLVGSDP APSPSILPPV PQDSPQPLPA
PEEEEALTTE DFELLDQGEL EQLNAELGLE PETPPKPPDA PPLGPDIHSL VQSDQEAQAV
AEP
