ID   EGFL6_HUMAN             Reviewed;         553 AA.
AC   Q8IUX8; B2RCB1; Q6UXJ1; Q8NBV0; Q8WYG3; Q9NY67; Q9NZL7; Q9UFK6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 157.
DE   RecName: Full=Epidermal growth factor-like protein 6;
DE            Short=EGF-like protein 6;
DE   AltName: Full=MAM and EGF domains-containing gene protein;
DE   Flags: Precursor;
GN   Name=EGFL6; Synonyms=MAEG; ORFNames=PP648, UNQ281/PRO320;
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 DEVELOPMENTAL STAGE.
RC   TISSUE=Fetal liver;
RX   PubMed=10610727; DOI=10.1006/geno.1999.6011;
RA   Yeung G., Mulero J.J., Berntsen R.P., Loeb D.B., Drmanac R., Ford J.E.;
RT   "Cloning of a novel epidermal growth factor repeat containing gene EGFL6:
RT   expressed in tumor and fetal tissues.";
RL   Genomics 62:304-307(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=10777661; DOI=10.1006/geno.2000.6146;
RA   Buchner G., Orfanelli U., Quaderi N., Bassi M.T., Andolfi G.;
RT   "Identification of a new EGF-repeat-containing gene from human Xp22: a
RT   candidate for developmental disorders.";
RL   Genomics 65:16-23(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] PHE-508.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May bind integrin alpha-8/beta-1 and play a role in hair
CC       follicle morphogenesis. Promotes matrix assembly (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8IUX8; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-715208, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IUX8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IUX8-2; Sequence=VSP_027089;
CC   -!- DEVELOPMENTAL STAGE: Only detected in fetal tissues.
CC       {ECO:0000269|PubMed:10610727, ECO:0000269|PubMed:10777661}.
CC   -!- SIMILARITY: Belongs to the nephronectin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG22483.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAQ88699.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF186084; AAF27812.1; -; mRNA.
DR   EMBL; AJ245671; CAB92132.1; -; mRNA.
DR   EMBL; AF193055; AAG22483.1; ALT_FRAME; mRNA.
DR   EMBL; AY358333; AAQ88699.1; ALT_FRAME; mRNA.
DR   EMBL; AK075214; BAC11477.1; -; mRNA.
DR   EMBL; AK315018; BAG37508.1; -; mRNA.
DR   EMBL; AL117610; CAB56014.2; -; mRNA.
DR   EMBL; CH471074; EAW98822.1; -; Genomic_DNA.
DR   EMBL; BC038587; AAH38587.1; -; mRNA.
DR   CCDS; CCDS14155.1; -. [Q8IUX8-1]
DR   CCDS; CCDS55370.1; -. [Q8IUX8-2]
DR   PIR; T17324; T17324.
DR   RefSeq; NP_001161362.1; NM_001167890.1. [Q8IUX8-2]
DR   RefSeq; NP_056322.2; NM_015507.3. [Q8IUX8-1]
DR   AlphaFoldDB; Q8IUX8; -.
DR   SMR; Q8IUX8; -.
DR   BioGRID; 117459; 19.
DR   IntAct; Q8IUX8; 18.
DR   MINT; Q8IUX8; -.
DR   STRING; 9606.ENSP00000369976; -.
DR   GlyCosmos; Q8IUX8; 1 site, No reported glycans.
DR   GlyGen; Q8IUX8; 4 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q8IUX8; -.
DR   PhosphoSitePlus; Q8IUX8; -.
DR   BioMuta; EGFL6; -.
DR   DMDM; 74728003; -.
DR   MassIVE; Q8IUX8; -.
DR   PaxDb; 9606-ENSP00000369976; -.
DR   PeptideAtlas; Q8IUX8; -.
DR   ProteomicsDB; 70628; -. [Q8IUX8-1]
DR   ProteomicsDB; 70629; -. [Q8IUX8-2]
DR   Antibodypedia; 641; 132 antibodies from 17 providers.
DR   DNASU; 25975; -.
DR   Ensembl; ENST00000361306.6; ENSP00000355126.1; ENSG00000198759.12. [Q8IUX8-1]
DR   Ensembl; ENST00000380602.3; ENSP00000369976.3; ENSG00000198759.12. [Q8IUX8-2]
DR   GeneID; 25975; -.
DR   KEGG; hsa:25975; -.
DR   MANE-Select; ENST00000361306.6; ENSP00000355126.1; NM_015507.4; NP_056322.2.
DR   UCSC; uc004cvi.4; human. [Q8IUX8-1]
DR   AGR; HGNC:3235; -.
DR   CTD; 25975; -.
DR   DisGeNET; 25975; -.
DR   GeneCards; EGFL6; -.
DR   HGNC; HGNC:3235; EGFL6.
DR   HPA; ENSG00000198759; Tissue enriched (placenta).
DR   MIM; 300239; gene.
DR   neXtProt; NX_Q8IUX8; -.
DR   OpenTargets; ENSG00000198759; -.
DR   PharmGKB; PA27668; -.
DR   VEuPathDB; HostDB:ENSG00000198759; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00930000150973; -.
DR   HOGENOM; CLU_036867_0_0_1; -.
DR   InParanoid; Q8IUX8; -.
DR   OMA; NGRACID; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q8IUX8; -.
DR   TreeFam; TF330819; -.
DR   PathwayCommons; Q8IUX8; -.
DR   SignaLink; Q8IUX8; -.
DR   BioGRID-ORCS; 25975; 10 hits in 779 CRISPR screens.
DR   ChiTaRS; EGFL6; human.
DR   GenomeRNAi; 25975; -.
DR   Pharos; Q8IUX8; Tbio.
DR   PRO; PR:Q8IUX8; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q8IUX8; Protein.
DR   Bgee; ENSG00000198759; Expressed in visceral pleura and 131 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005178; F:integrin binding; TAS:ProtInc.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   PANTHER; PTHR24050:SF24; EPIDERMAL GROWTH FACTOR-LIKE PROTEIN 6; 1.
DR   PANTHER; PTHR24050; PA14 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF00629; MAM; 1.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS50060; MAM_2; 1.
DR   Genevisible; Q8IUX8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW   Coiled coil; Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..553
FT                   /note="Epidermal growth factor-like protein 6"
FT                   /id="PRO_0000295811"
FT   DOMAIN          65..91
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          94..133
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          137..173
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          174..212
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          219..259
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          400..546
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   REGION          291..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          331..363
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        330..350
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        98..109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        105..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        120..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        178..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        185..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        223..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        230..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        247..258
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         394
FT                   /note="K -> KA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10777661"
FT                   /id="VSP_027089"
FT   VARIANT         66
FT                   /note="E -> K (in dbSNP:rs16979010)"
FT                   /id="VAR_033366"
FT   VARIANT         164
FT                   /note="R -> C (in dbSNP:rs34613284)"
FT                   /id="VAR_033367"
FT   VARIANT         508
FT                   /note="L -> F (in dbSNP:rs34550481)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_033368"
FT   VARIANT         535
FT                   /note="D -> N (in dbSNP:rs16979033)"
FT                   /id="VAR_033369"
FT   CONFLICT        22
FT                   /note="N -> D (in Ref. 5; BAC11477)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83
FT                   /note="F -> L (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="N -> Y (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="C -> S (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="E -> G (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="L -> S (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        521
FT                   /note="E -> V (in Ref. 6; CAB56014)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   553 AA;  61317 MW;  3AE93A0362E861E0 CRC64;
     MPLPWSLALP LLLSWVAGGF GNAASARHHG LLASARQPGV CHYGTKLACC YGWRRNSKGV
     CEATCEPGCK FGECVGPNKC RCFPGYTGKT CSQDVNECGM KPRPCQHRCV NTHGSYKCFC
     LSGHMLMPDA TCVNSRTCAM INCQYSCEDT EEGPQCLCPS SGLRLAPNGR DCLDIDECAS
     GKVICPYNRR CVNTFGSYYC KCHIGFELQY ISGRYDCIDI NECTMDSHTC SHHANCFNTQ
     GSFKCKCKQG YKGNGLRCSA IPENSVKEVL RAPGTIKDRI KKLLAHKNSM KKKAKIKNVT
     PEPTRTPTPK VNLQPFNYEE IVSRGGNSHG GKKGNEEKMK EGLEDEKREE KALKNDIEER
     SLRGDVFFPK VNEAGEFGLI LVQRKALTSK LEHKDLNISV DCSFNHGICD WKQDREDDFD
     WNPADRDNAI GFYMAVPALA GHKKDIGRLK LLLPDLQPQS NFCLLFDYRL AGDKVGKLRV
     FVKNSNNALA WEKTTSEDEK WKTGKIQLYQ GTDATKSIIF EAERGKGKTG EIAVDGVLLV
     SGLCPDSLLS VDD
//