Entry euk:CHP2_HUMAN

ID   CHP2_HUMAN              Reviewed;         196 AA.
AC   O43745; A8K2I8;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   10-MAY-2017, entry version 141.
DE   RecName: Full=Calcineurin B homologous protein 2;
DE   AltName: Full=Hepatocellular carcinoma-associated antigen 520;
GN   Name=CHP2; Synonyms=HCA520;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Hepatoma;
RX   PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA   Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA   Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA   Chen W.-F.;
RT   "Large scale identification of human hepatocellular carcinoma-
RT   associated antigens by autoantibodies.";
RL   J. Immunol. 169:1102-1109(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Caudate nucleus, and Colon;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SLC9A1.
RX   PubMed=12226101; DOI=10.1074/jbc.M208313200;
RA   Pang T., Wakabayashi S., Shigekawa M.;
RT   "Expression of calcineurin B homologous protein 2 protects serum
RT   deprivation-induced cell death by serum-independent activation of
RT   Na+/H+ exchanger.";
RL   J. Biol. Chem. 277:43771-43777(2002).
RN   [6]
RP   FUNCTION AS A CALCINEURIN ACTIVATOR, AND INTERACTION WITH PPP3CA.
RX   PubMed=18815128; DOI=10.1074/jbc.M806684200;
RA   Li G.D., Zhang X., Li R., Wang Y.D., Wang Y.L., Han K.J., Qian X.P.,
RA   Yang C.G., Liu P., Wei Q., Chen W.F., Zhang J., Zhang Y.;
RT   "CHP2 activates the calcineurin/nuclear factor of activated T cells
RT   signaling pathway and enhances the oncogenic potential of HEK293
RT   cells.";
RL   J. Biol. Chem. 283:32660-32668(2008).
RN   [7]
RP   INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   ASP-50; GLY-82; GLU-135; 137-LEU--VAL-148 AND GLU-176.
RX   PubMed=21392185; DOI=10.1111/j.1365-2443.2011.01497.x;
RA   Li Q.H., Wang L.H., Lin Y.N., Chang G.Q., Li H.W., Jin W.N., Hu R.H.,
RA   Pang T.X.;
RT   "Nuclear accumulation of calcineurin B homologous protein 2 (CHP2)
RT   results in enhanced proliferation of tumor cells.";
RL   Genes Cells 16:416-426(2011).
RN   [8]
RP   PRELIMINARY X-RAY CRYSTALLOGRAPHY OF 1-195 IN COMPLEX WITH SLC9A1.
RX   PubMed=16511206; DOI=10.1107/S1744309105030836;
RA   Ben Ammar Y., Takeda S., Sugawara M., Miyano M., Mori H.,
RA   Wakabayashi S.;
RT   "Crystallization and preliminary crystallographic analysis of the
RT   human calcineurin homologous protein CHP2 bound to the cytoplasmic
RT   region of the Na+/H+ exchanger NHE1.";
RL   Acta Crystallogr. F 61:956-958(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-195 IN COMPLEX WITH SLC9A1.
RX   PubMed=16710297; DOI=10.1038/sj.emboj.7601145;
RA   Ammar Y.B., Takeda S., Hisamitsu T., Mori H., Wakabayashi S.;
RT   "Crystal structure of CHP2 complexed with NHE1-cytosolic region and an
RT   implication for pH regulation.";
RL   EMBO J. 25:2315-2325(2006).
CC   -!- FUNCTION: Functions as an integral cofactor in cell pH regulation
CC       by controlling plasma membrane-type Na(+)/H(+) exchange activity.
CC       Binds to and activates SLC9A1/NHE1 in a serum-independent manner,
CC       thus increasing pH and protecting cells from serum deprivation-
CC       induced death. Also plays a role in the regulation of cell
CC       proliferation and tumor growth by increasing the phosphatase
CC       activity of PPP3CA in a calcium-dependent manner. Activator of the
CC       calcineurin/NFAT signaling pathway. Involved in the cytoplasmic
CC       translocation of the transcription factor NFATC3 to the nucleus.
CC       {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:18815128}.
CC   -!- SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1; the
CC       interaction occurs in a calcium-dependent manner.
CC       {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:16710297,
CC       ECO:0000269|PubMed:18815128, ECO:0000269|PubMed:21392185}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21392185}.
CC       Cytoplasm {ECO:0000269|PubMed:21392185}. Cell membrane
CC       {ECO:0000269|PubMed:21392185}. Note=Predominantly localized in a
CC       juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear
CC       region and at the plasma membrane (By similarity). Exported from
CC       the nucleus to the cytoplasm through a nuclear export signal (NES)
CC       pathway. May shuttle between nucleus and cytoplasm. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in malignantly transformed cells but
CC       not detected in normal tissues. {ECO:0000269|PubMed:12097419,
CC       ECO:0000269|PubMed:12226101}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       CHP subfamily. {ECO:0000305}.
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DR   EMBL; AF146019; AAG14945.1; -; mRNA.
DR   EMBL; AK290253; BAF82942.1; -; mRNA.
DR   EMBL; AK313062; BAG35891.1; -; mRNA.
DR   EMBL; AC130454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471145; EAW55801.1; -; Genomic_DNA.
DR   CCDS; CCDS10617.1; -.
DR   RefSeq; NP_071380.1; NM_022097.3.
DR   UniGene; Hs.178589; -.
DR   PDB; 2BEC; X-ray; 2.70 A; A=1-196.
DR   PDBsum; 2BEC; -.
DR   ProteinModelPortal; O43745; -.
DR   SMR; O43745; -.
DR   BioGrid; 121996; 5.
DR   IntAct; O43745; 2.
DR   MINT; MINT-2729920; -.
DR   STRING; 9606.ENSP00000300113; -.
DR   iPTMnet; O43745; -.
DR   PhosphoSitePlus; O43745; -.
DR   EPD; O43745; -.
DR   PaxDb; O43745; -.
DR   PeptideAtlas; O43745; -.
DR   PRIDE; O43745; -.
DR   DNASU; 63928; -.
DR   Ensembl; ENST00000300113; ENSP00000300113; ENSG00000166869.
DR   GeneID; 63928; -.
DR   KEGG; hsa:63928; -.
DR   UCSC; uc002dmb.2; human.
DR   CTD; 63928; -.
DR   DisGeNET; 63928; -.
DR   GeneCards; CHP2; -.
DR   HGNC; HGNC:24927; CHP2.
DR   HPA; CAB072806; -.
DR   neXtProt; NX_O43745; -.
DR   OpenTargets; ENSG00000166869; -.
DR   eggNOG; KOG0034; Eukaryota.
DR   eggNOG; COG5126; LUCA.
DR   GeneTree; ENSGT00860000133729; -.
DR   HOGENOM; HOG000233019; -.
DR   HOVERGEN; HBG105307; -.
DR   InParanoid; O43745; -.
DR   KO; K17611; -.
DR   OMA; HFRPVDE; -.
DR   OrthoDB; EOG091G0LZ1; -.
DR   PhylomeDB; O43745; -.
DR   TreeFam; TF354284; -.
DR   EvolutionaryTrace; O43745; -.
DR   GenomeRNAi; 63928; -.
DR   PRO; PR:O43745; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   Bgee; ENSG00000166869; -.
DR   Genevisible; O43745; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
KW   Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus;
KW   Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000255}.
FT   CHAIN         2    196       Calcineurin B homologous protein 2.
FT                                /FTId=PRO_0000073848.
FT   DOMAIN       26     61       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN       71    106       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      111    146       EF-hand 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      152    187       EF-hand 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     124    135       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     165    176       2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   MOTIF       137    148       Nuclear export signal.
FT   MOD_RES      27     27       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q810D1}.
FT   LIPID         2      2       N-myristoyl glycine. {ECO:0000255}.
FT   VARIANT     127    127       R -> P (in dbSNP:rs35641939).
FT                                /FTId=VAR_048664.
FT   MUTAGEN      50     50       D->A: Does not reduce calcium-binding.
FT                                {ECO:0000269|PubMed:21392185}.
FT   MUTAGEN      82     82       G->A: Does not reduce calcium-binding.
FT                                {ECO:0000269|PubMed:21392185}.
FT   MUTAGEN     135    135       E->A: Reduces calcium-binding. Inhibits
FT                                calcium-binding and cell membrane
FT                                localization; when associated with A-176.
FT                                {ECO:0000269|PubMed:21392185}.
FT   MUTAGEN     137    148       LQVLRLMVGVQV->AQVARAMAGAQA: Localizes in
FT                                the nucleus and increases cell
FT                                proliferation.
FT                                {ECO:0000269|PubMed:21392185}.
FT   MUTAGEN     176    176       E->A: Reduces calcium-binding. Inhibits
FT                                calcium-binding and cell membrane
FT                                localization; when associated with A-135.
FT                                {ECO:0000269|PubMed:21392185}.
FT   TURN         14     16       {ECO:0000244|PDB:2BEC}.
FT   HELIX        17     21       {ECO:0000244|PDB:2BEC}.
FT   HELIX        25     38       {ECO:0000244|PDB:2BEC}.
FT   HELIX        48     52       {ECO:0000244|PDB:2BEC}.
FT   HELIX        55     59       {ECO:0000244|PDB:2BEC}.
FT   HELIX        63     68       {ECO:0000244|PDB:2BEC}.
FT   HELIX        80     87       {ECO:0000244|PDB:2BEC}.
FT   HELIX        88     90       {ECO:0000244|PDB:2BEC}.
FT   HELIX        95     98       {ECO:0000244|PDB:2BEC}.
FT   HELIX       112    123       {ECO:0000244|PDB:2BEC}.
FT   STRAND      128    131       {ECO:0000244|PDB:2BEC}.
FT   HELIX       133    142       {ECO:0000244|PDB:2BEC}.
FT   HELIX       150    164       {ECO:0000244|PDB:2BEC}.
FT   STRAND      169    173       {ECO:0000244|PDB:2BEC}.
FT   HELIX       174    179       {ECO:0000244|PDB:2BEC}.
FT   TURN        180    183       {ECO:0000244|PDB:2BEC}.
FT   HELIX       186    189       {ECO:0000244|PDB:2BEC}.
FT   TURN        193    195       {ECO:0000244|PDB:2BEC}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       115    143       ismart:EFh [T]
FT   MYHIT        30     58       ismart:EFh [T]
FT   MYHIT       111    146       iprf:EF_HAND_2 [T]
FT   MYHIT        26     61       iprf:EF_HAND_2 [T]
FT   MYHIT       114    179       ipfam:EF-hand_7 [T]
FT   MYHIT       124    136       ipat:EF_HAND_1 [T]
FT   MYHIT       165    177       ipat:EF_HAND_1 [T]
FT   MYHIT        35     53       ipfam:EF-hand_5 [T]
FT   MYHIT       156    184       ismart:EFh [T]
FT   MYHIT       152    187       iprf:EF_HAND_2 [T]
SQ   SEQUENCE   196 AA;  22452 MW;  F5113D558AFA27DE CRC64;
     MGSRSSHAAV IPDGDSIRRE TGFSQASLLR LHHRFRALDR NKKGYLSRMD LQQIGALAVN
     PLGDRIIESF FPDGSQRVDF PGFVRVLAHF RPVEDEDTET QDPKKPEPLN SRRNKLHYAF
     QLYDLDRDGK ISRHEMLQVL RLMVGVQVTE EQLENIADRT VQEADEDGDG AVSFVEFTKS
     LEKMDVEQKM SIRILK
//