ID   IBP7_HUMAN              Reviewed;         282 AA.
AC   Q16270; B4E1N2; B7Z9W7; Q07822; Q53YE6; Q9UCA8;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-MAY-2017, entry version 164.
DE   RecName: Full=Insulin-like growth factor-binding protein 7;
DE            Short=IBP-7;
DE            Short=IGF-binding protein 7;
DE            Short=IGFBP-7;
DE   AltName: Full=IGFBP-rP1;
DE   AltName: Full=MAC25 protein;
DE   AltName: Full=PGI2-stimulating factor;
DE   AltName: Full=Prostacyclin-stimulating factor;
DE   AltName: Full=Tumor-derived adhesion factor;
DE            Short=TAF;
DE   Flags: Precursor;
GN   Name=IGFBP7; Synonyms=MAC25, PSF;
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 [MRNA] (ISOFORM 1), VARIANT PHE-11, AND RNA
RP   EDITING OF POSITION 95.
RC   TISSUE=Leptomeninges;
RX   PubMed=7694637;
RA   Murphy M., Pykett M.J., Harnish P., Zang K.D., George D.L.;
RT   "Identification and characterization of genes differentially expressed
RT   in meningiomas.";
RL   Cell Growth Differ. 4:715-722(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=7980422; DOI=10.1042/bj3030591;
RA   Yamauchi T., Umeda F., Masakado M., Isaji M., Mizushima S., Nawata H.;
RT   "Purification and molecular cloning of prostacyclin-stimulating factor
RT   from serum-free conditioned medium of human diploid fibroblast
RT   cells.";
RL   Biochem. J. 303:591-598(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-11.
RG   NIEHS SNPs program;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thalamus, and Trachea;
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   [6]
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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis, 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 27-46, AND FUNCTION.
RC   TISSUE=Urinary bladder carcinoma;
RX   PubMed=8117260; DOI=10.1006/bbrc.1994.1149;
RA   Akaogi K., Okabe Y., Funahashi K., Yoshitake Y., Nishikawa K.,
RA   Yasumitsu H., Umeda M., Miyazaki K.;
RT   "Cell adhesion activity of a 30-kDa major secreted protein from human
RT   bladder carcinoma cells.";
RL   Biochem. Biophys. Res. Commun. 198:1046-1053(1994).
RN   [9]
RP   PROTEIN SEQUENCE OF 27-41.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 27-36, FUNCTION, AND GLYCOSYLATION.
RX   PubMed=8939990; DOI=10.1074/jbc.271.48.30322;
RA   Oh Y., Nagalla S.R., Yamanaka Y., Kim H.-S., Wilson E.,
RA   Rosenfeld R.G.;
RT   "Synthesis and characterization of insulin-like growth factor-binding
RT   protein (IGFBP)-7. Recombinant human mac25 protein specifically binds
RT   IGF-I and -II.";
RL   J. Biol. Chem. 271:30322-30325(1996).
RN   [11]
RP   POSSIBLE INTERACTION WITH CHMP3.
RX   PubMed=11549700; DOI=10.1210/jcem.86.9.7845;
RA   Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.;
RT   "Interaction of IGF-binding protein-related protein 1 with a novel
RT   protein, neuroendocrine differentiation factor, results in
RT   neuroendocrine differentiation of prostate cancer cells.";
RL   J. Clin. Endocrinol. Metab. 86:4504-4511(2001).
RN   [12]
RP   RNA EDITING OF POSITIONS 78 AND 95.
RX   PubMed=18772245; DOI=10.1261/rna.816908;
RA   Gommans W.M., Tatalias N.E., Sie C.P., Dupuis D., Vendetti N.,
RA   Smith L., Kaushal R., Maas S.;
RT   "Screening of human SNP database identifies recoding sites of A-to-I
RT   RNA editing.";
RL   RNA 14:2074-2085(2008).
RN   [13]
RP   INVOLVEMENT IN RAMSVPS.
RX   PubMed=21835307; DOI=10.1016/j.ajhg.2011.07.010;
RA   Abu-Safieh L., Abboud E.B., Alkuraya H., Shamseldin H., Al-Enzi S.,
RA   Al-Abdi L., Hashem M., Colak D., Jarallah A., Ahmad H., Bobis S.,
RA   Nemer G., Bitar F., Alkuraya F.S.;
RT   "Mutation of IGFBP7 causes upregulation of BRAF/MEK/ERK pathway and
RT   familial retinal arterial macroaneurysms.";
RL   Am. J. Hum. Genet. 89:313-319(2011).
RN   [14]
RP   PHOSPHORYLATION AT SER-239.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted
RT   phosphoproteome.";
RL   Cell 161:1619-1632(2015).
CC   -!- FUNCTION: Binds IGF-I and IGF-II with a relatively low affinity.
CC       Stimulates prostacyclin (PGI2) production. Stimulates cell
CC       adhesion. {ECO:0000269|PubMed:8117260,
CC       ECO:0000269|PubMed:8939990}.
CC   -!- SUBUNIT: May interact with VPS24/CHMP3; the relevance of such
CC       interaction however remains unclear.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q16270-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q16270-2; Sequence=VSP_045297;
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:8939990}.
CC   -!- RNA EDITING: Modified_positions=78 {ECO:0000269|PubMed:18772245},
CC       95 {ECO:0000269|PubMed:18772245, ECO:0000269|PubMed:7694637};
CC       Note=Partially edited. In the brain, position 78 is edited at
CC       about 55% and position 95 at about 31%.;
CC   -!- DISEASE: Retinal arterial macroaneurysm with supravalvular
CC       pulmonic stenosis (RAMSVPS) [MIM:614224]: An autosomal recessive
CC       condition characterized by the bilateral appearance of 'beading'
CC       along the major retinal arterial trunks, with the subsequent
CC       formation of macroaneurysms. Affected individuals also have
CC       supravalvular pulmonic stenosis, often requiring surgical
CC       correction. {ECO:0000269|PubMed:21835307}. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/igfbp7/";
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DR   EMBL; L19182; AAA16187.1; -; mRNA.
DR   EMBL; S75725; AAB32370.1; -; mRNA.
DR   EMBL; AY518539; AAR89912.1; -; Genomic_DNA.
DR   EMBL; BT006654; AAP35300.1; -; mRNA.
DR   EMBL; AK303915; BAG64844.1; -; mRNA.
DR   EMBL; AK316082; BAH14453.1; -; mRNA.
DR   EMBL; AC069307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC017201; AAH17201.1; -; mRNA.
DR   EMBL; BC066339; AAH66339.1; -; mRNA.
DR   CCDS; CCDS3512.1; -. [Q16270-1]
DR   CCDS; CCDS58900.1; -. [Q16270-2]
DR   PIR; I52825; I52825.
DR   PIR; PC2030; PC2030.
DR   PIR; S50031; S50031.
DR   RefSeq; NP_001240764.1; NM_001253835.1. [Q16270-2]
DR   RefSeq; NP_001544.1; NM_001553.2. [Q16270-1]
DR   UniGene; Hs.479808; -.
DR   UniGene; Hs.691061; -.
DR   ProteinModelPortal; Q16270; -.
DR   SMR; Q16270; -.
DR   BioGrid; 109711; 9.
DR   IntAct; Q16270; 9.
DR   MINT; MINT-7006618; -.
DR   STRING; 9606.ENSP00000295666; -.
DR   DrugBank; DB00030; Insulin Human.
DR   DrugBank; DB00071; Insulin Pork.
DR   iPTMnet; Q16270; -.
DR   PhosphoSitePlus; Q16270; -.
DR   BioMuta; IGFBP7; -.
DR   DMDM; 23396609; -.
DR   EPD; Q16270; -.
DR   MaxQB; Q16270; -.
DR   PaxDb; Q16270; -.
DR   PeptideAtlas; Q16270; -.
DR   PRIDE; Q16270; -.
DR   DNASU; 3490; -.
DR   Ensembl; ENST00000295666; ENSP00000295666; ENSG00000163453. [Q16270-1]
DR   Ensembl; ENST00000514062; ENSP00000486293; ENSG00000163453. [Q16270-2]
DR   GeneID; 3490; -.
DR   KEGG; hsa:3490; -.
DR   UCSC; uc003hcn.4; human. [Q16270-1]
DR   CTD; 3490; -.
DR   DisGeNET; 3490; -.
DR   GeneCards; IGFBP7; -.
DR   HGNC; HGNC:5476; IGFBP7.
DR   HPA; CAB020668; -.
DR   HPA; HPA002196; -.
DR   MalaCards; IGFBP7; -.
DR   MIM; 602867; gene.
DR   MIM; 614224; phenotype.
DR   neXtProt; NX_Q16270; -.
DR   OpenTargets; ENSG00000163453; -.
DR   Orphanet; 284247; Familial retinal arterial macroaneurysm.
DR   PharmGKB; PA29709; -.
DR   eggNOG; ENOG410IVG7; Eukaryota.
DR   eggNOG; ENOG4111RFI; LUCA.
DR   GeneTree; ENSGT00530000063555; -.
DR   HOGENOM; HOG000261684; -.
DR   HOVERGEN; HBG031621; -.
DR   InParanoid; Q16270; -.
DR   OMA; HCAPGME; -.
DR   OrthoDB; EOG091G0QK5; -.
DR   PhylomeDB; Q16270; -.
DR   TreeFam; TF331645; -.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   ChiTaRS; IGFBP7; human.
DR   GeneWiki; IGFBP7; -.
DR   GenomeRNAi; 3490; -.
DR   PRO; PR:Q16270; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000163453; -.
DR   CleanEx; HS_IGFBP7; -.
DR   Genevisible; Q16270; HS.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051414; P:response to cortisol; IEA:Ensembl.
DR   GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR009030; Growth_fac_rcpt_.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR011390; IGFBP_rP_mac25.
DR   InterPro; IPR002350; Kazal_dom.
DR   PANTHER; PTHR14186; PTHR14186; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   PIRSF; PIRSF018239; IGFBP_rP_mac25; 1.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Growth factor binding; Immunoglobulin domain; Phosphoprotein;
KW   Polymorphism; Reference proteome; RNA editing; Secreted; Signal.
FT   SIGNAL        1     26       {ECO:0000269|PubMed:15340161,
FT                                ECO:0000269|PubMed:8117260,
FT                                ECO:0000269|PubMed:8939990}.
FT   CHAIN        27    282       Insulin-like growth factor-binding
FT                                protein 7.
FT                                /FTId=PRO_0000014392.
FT   DOMAIN       28    106       IGFBP N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00653}.
FT   DOMAIN      105    158       Kazal-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00798}.
FT   DOMAIN      160    264       Ig-like C2-type.
FT   MOD_RES     239    239       Phosphoserine; by FAM20C.
FT                                {ECO:0000269|PubMed:26091039}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000305|PubMed:8939990}.
FT   DISULFID    181    248       {ECO:0000255|PROSITE-ProRule:PRU00114,
FT                                ECO:0000255|PROSITE-ProRule:PRU00798}.
FT   VAR_SEQ     278    282       EGAEL -> TQ (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_045297.
FT   VARIANT      11     11       L -> F (in dbSNP:rs11573021).
FT                                {ECO:0000269|PubMed:7694637,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_018959.
FT   VARIANT      78     78       R -> G (in RNA edited version;
FT                                dbSNP:rs11555284).
FT                                /FTId=VAR_063638.
FT   VARIANT      95     95       K -> R (in RNA edited version;
FT                                dbSNP:rs1133243).
FT                                /FTId=VAR_063639.
FT   CONFLICT      4      4       P -> A (in Ref. 1; AAA16187).
FT                                {ECO:0000305}.
FT   CONFLICT     13     13       A -> P (in Ref. 1; AAA16187).
FT                                {ECO:0000305}.
FT   CONFLICT     69     69       E -> G (in Ref. 5; BAH14453).
FT                                {ECO:0000305}.
FT   CONFLICT    273    282       PVKKGEGAEL -> ASEKR (in Ref. 1;
FT                                AAA16187). {ECO:0000305}.
SQ   SEQUENCE   282 AA;  29130 MW;  75F96EBC3B444D37 CRC64;
     MERPSLRALL LGAAGLLLLL LPLSSSSSSD TCGPCEPASC PPLPPLGCLL GETRDACGCC
     PMCARGEGEP CGGGGAGRGY CAPGMECVKS RKRRKGKAGA AAGGPGVSGV CVCKSRYPVC
     GSDGTTYPSG CQLRAASQRA ESRGEKAITQ VSKGTCEQGP SIVTPPKDIW NVTGAQVYLS
     CEVIGIPTPV LIWNKVKRGH YGVQRTELLP GDRDNLAIQT RGGPEKHEVT GWVLVSPLSK
     EDAGEYECHA SNSQGQASAS AKITVVDALH EIPVKKGEGA EL
//