REEP5_HUMAN
ID REEP5_HUMAN Reviewed; 189 AA.
AC Q00765; B7Z681; D3DT04; Q04198; Q5QGT0; Q9BWH9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Receptor expression-enhancing protein 5;
DE AltName: Full=Polyposis locus protein 1;
DE AltName: Full=Protein TB2;
GN Name=REEP5; Synonyms=C5orf18, DP1, TB2;
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).
RX PubMed=1678319; DOI=10.1016/0092-8674(81)90022-2;
RA Joslyn G., Carlson M., Thliveris A., Albertsen H., Gelbert L., Samowitz W.,
RA Groden J., Stevens J., Spirio L., Robertson M., Sargeant L., Krapcho K.,
RA Wolff E., Burt R., Hughes J.P., Warrington J., McPherson J.D.,
RA Wasmuth J.J., le Paslier D., Abderrahim H., Cohen D., Leppert M., White R.;
RT "Identification of deletion mutations and three new genes at the familial
RT polyposis locus.";
RL Cell 66:601-613(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1651562; DOI=10.1126/science.1651562;
RA Kinzler K.W., Nilbert M.C., Su L.-K., Vogelstein B., Bryan T.M., Levy D.B.,
RA Smith K.J., Preisinger A.C., Hedge P., McKechnie D., Finniear R.,
RA Markham A., Groffen J., Boguski M.S., Altschul S.F., Horii A.K., Ando H.,
RA Miyoshi Y., Miki Y., Nishisho I., Nakamura Y.;
RT "Identification of FAP locus genes from chromosome 5q21.";
RL Science 253:661-665(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT "RTP family members induce functional expression of mammalian odorant
RT receptors.";
RL Cell 119:679-691(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and 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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=16720576; DOI=10.1074/jbc.m513637200;
RA Behrens M., Bartelt J., Reichling C., Winnig M., Kuhn C., Meyerhof W.;
RT "Members of RTP and REEP gene families influence functional bitter taste
RT receptor expression.";
RL J. Biol. Chem. 281:20650-20659(2006).
RN [9]
RP INTERACTION WITH ATL2.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 IDENTIFICATION BY 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 [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE27.
RX PubMed=23969831; DOI=10.1073/pnas.1307391110;
RA Chang J., Lee S., Blackstone C.;
RT "Protrudin binds atlastins and endoplasmic reticulum-shaping proteins and
RT regulates network formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:14954-14959(2013).
RN [14]
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP SUBUNIT, INTERACTION WITH ATL3; CKAP4 AND RTN4, TISSUE SPECIFICITY, AND
RP TOPOLOGY.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
CC -!- FUNCTION: Plays an essential role in heart function and development by
CC regulating the organization and function of the sarcoplasmic reticulum
CC in cardiomyocytes. {ECO:0000250|UniProtKB:Q60870}.
CC -!- SUBUNIT: Monomer (PubMed:32075961). Homodimer; maybe disulfide-linked
CC (PubMed:32075961). Homotrimer (By similarity). Interacts with ATL1 (By
CC similarity). Interacts with ATL2 (PubMed:19665976). Interacts with ATL3
CC (PubMed:32075961). Interacts with CKAP4 (PubMed:32075961). Interacts
CC with RTN4 (isoforms A and B) (PubMed:32075961). Interacts with ZFYVE27
CC (PubMed:23969831). {ECO:0000250|UniProtKB:Q60870,
CC ECO:0000269|PubMed:19665976, ECO:0000269|PubMed:23969831,
CC ECO:0000269|PubMed:32075961}.
CC -!- INTERACTION:
CC Q00765; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-1549827, EBI-7131019;
CC Q00765; P53365: ARFIP2; NbExp=3; IntAct=EBI-1549827, EBI-638194;
CC Q00765; Q6P1Q0: LETMD1; NbExp=3; IntAct=EBI-1549827, EBI-1549822;
CC Q00765; Q96AL5: PBX3; NbExp=3; IntAct=EBI-1549827, EBI-741171;
CC Q00765; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-1549827, EBI-14223623;
CC Q00765; Q13596: SNX1; NbExp=3; IntAct=EBI-1549827, EBI-2822329;
CC Q00765; Q5T4F4: ZFYVE27; NbExp=4; IntAct=EBI-1549827, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23969831}; Multi-pass membrane protein
CC {ECO:0000255}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q60870}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network
CC (PubMed:23969831). In cardiomyocytes, localizes to the junctional
CC sarcoplasmic reticulum membrane which is closely tethered to the cell
CC membrane and contractile machinery (By similarity).
CC {ECO:0000250|UniProtKB:Q60870, ECO:0000269|PubMed:23969831}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q00765-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q00765-2; Sequence=VSP_056633;
CC -!- TISSUE SPECIFICITY: Expressed in heart (at protein level)
CC (PubMed:32075961). Expressed in circumvallate papillae and testis
CC (PubMed:16720576). {ECO:0000269|PubMed:16720576,
CC ECO:0000269|PubMed:32075961}.
CC -!- DOMAIN: The short lumenal loops between transmembrane domains 1 and 2
CC and between transmembrane domains 3 and 4 may impart a wedge-like
CC configuration, thus deforming membranes. {ECO:0000305|PubMed:32075961}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA66351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH65926.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M73547; AAA60136.1; ALT_INIT; mRNA.
DR EMBL; M74090; AAA66351.1; ALT_INIT; mRNA.
DR EMBL; AY562243; AAT70688.1; -; mRNA.
DR EMBL; AK299902; BAH13167.1; -; mRNA.
DR EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48994.1; -; Genomic_DNA.
DR EMBL; CH471086; EAW48995.1; -; Genomic_DNA.
DR EMBL; BC000232; AAH00232.2; -; mRNA.
DR EMBL; BC065926; AAH65926.1; ALT_INIT; mRNA.
DR CCDS; CCDS4109.2; -. [Q00765-1]
DR PIR; A39658; A39658.
DR RefSeq; NP_005660.4; NM_005669.4. [Q00765-1]
DR AlphaFoldDB; Q00765; -.
DR BioGRID; 113637; 356.
DR CORUM; Q00765; -.
DR IntAct; Q00765; 91.
DR MINT; Q00765; -.
DR STRING; 9606.ENSP00000368959; -.
DR ChEMBL; CHEMBL4295797; -.
DR GlyGen; Q00765; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q00765; -.
DR PhosphoSitePlus; Q00765; -.
DR SwissPalm; Q00765; -.
DR BioMuta; REEP5; -.
DR DMDM; 82654932; -.
DR EPD; Q00765; -.
DR jPOST; Q00765; -.
DR MassIVE; Q00765; -.
DR MaxQB; Q00765; -.
DR PaxDb; Q00765; -.
DR PeptideAtlas; Q00765; -.
DR PRIDE; Q00765; -.
DR ProteomicsDB; 57872; -. [Q00765-1]
DR ProteomicsDB; 6755; -.
DR TopDownProteomics; Q00765-1; -. [Q00765-1]
DR Antibodypedia; 25369; 294 antibodies from 30 providers.
DR DNASU; 7905; -.
DR Ensembl; ENST00000379638.9; ENSP00000368959.4; ENSG00000129625.13. [Q00765-1]
DR GeneID; 7905; -.
DR KEGG; hsa:7905; -.
DR MANE-Select; ENST00000379638.9; ENSP00000368959.4; NM_005669.5; NP_005660.4.
DR UCSC; uc003kqe.2; human. [Q00765-1]
DR CTD; 7905; -.
DR DisGeNET; 7905; -.
DR GeneCards; REEP5; -.
DR HGNC; HGNC:30077; REEP5.
DR HPA; ENSG00000129625; Low tissue specificity.
DR MIM; 125265; gene.
DR neXtProt; NX_Q00765; -.
DR OpenTargets; ENSG00000129625; -.
DR PharmGKB; PA134882361; -.
DR VEuPathDB; HostDB:ENSG00000129625; -.
DR eggNOG; KOG1725; Eukaryota.
DR GeneTree; ENSGT00940000157873; -.
DR InParanoid; Q00765; -.
DR OMA; FILVLWM; -.
DR OrthoDB; 1473891at2759; -.
DR PhylomeDB; Q00765; -.
DR TreeFam; TF314913; -.
DR PathwayCommons; Q00765; -.
DR SignaLink; Q00765; -.
DR SIGNOR; Q00765; -.
DR BioGRID-ORCS; 7905; 14 hits in 1084 CRISPR screens.
DR ChiTaRS; REEP5; human.
DR GeneWiki; REEP5; -.
DR GenomeRNAi; 7905; -.
DR Pharos; Q00765; Tbio.
DR PRO; PR:Q00765; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q00765; protein.
DR Bgee; ENSG00000129625; Expressed in middle temporal gyrus and 212 other tissues.
DR ExpressionAtlas; Q00765; baseline and differential.
DR Genevisible; Q00765; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:FlyBase.
DR GO; GO:0032386; P:regulation of intracellular transport; ISS:FlyBase.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT CHAIN 1..189
FT /note="Receptor expression-enhancing protein 5"
FT /id="PRO_0000101815"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32075961"
FT TRANSMEM 35..51
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TOPO_DOM 52..53
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TOPO_DOM 75..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TOPO_DOM 104..105
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:32075961"
FT TOPO_DOM 124..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:32075961"
FT REGION 114..185
FT /note="Required for dimerization and maintaining
FT endoplasmic reticulum morphology"
FT /evidence="ECO:0000269|PubMed:32075961"
FT VAR_SEQ 118..189
FT /note="CGFLLWCMAPSPSNGAELLYKRIIRPFFLKHESQMDSVVKDLKDKAKETADA
FT ITKEAKKATVNLLGEEKKST -> VWSGLGFLLPRCLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056633"
FT CONFLICT 115
FT /note="M -> I (in Ref. 2; AAA66351)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> S (in Ref. 1; AAA60136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21493 MW; F4E57E500CB7C831 CRC64;
MSAAMRERFD RFLHEKNCMT DLLAKLEAKT GVNRSFIALG VIGLVALYLV FGYGASLLCN
LIGFGYPAYI SIKAIESPNK EDDTQWLTYW VVYGVFSIAE FFSDIFLSWF PFYYMLKCGF
LLWCMAPSPS NGAELLYKRI IRPFFLKHES QMDSVVKDLK DKAKETADAI TKEAKKATVN
LLGEEKKST
