GenomeNet

Database: UniProt
Entry: Q7Z7M0
LinkDB: Q7Z7M0
Original site: Q7Z7M0 
ID   MEGF8_HUMAN             Reviewed;        2845 AA.
AC   Q7Z7M0; A8KAY0; O75097;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   09-JUL-2014, entry version 116.
DE   RecName: Full=Multiple epidermal growth factor-like domains protein 8;
DE            Short=Multiple EGF-like domains protein 8;
DE   AltName: Full=Epidermal growth factor-like protein 4;
DE            Short=EGF-like protein 4;
DE   Flags: Precursor;
GN   Name=MEGF8; Synonyms=C19orf49, EGFL4, KIAA0817;
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 2).
RC   TISSUE=Brain;
RX   PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA   Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT   "Identification of high-molecular-weight proteins with multiple EGF-
RT   like motifs by motif-trap screening.";
RL   Genomics 51:27-34(1998).
RN   [2]
RP   SEQUENCE REVISION.
RA   Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 416-2845 (ISOFORM 1).
RA   Shan Y.X., Yu L.;
RT   "Cloning, characterization and location of a novel human gene
RT   containing an EGF domain.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1271.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA   Moore R.J., Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [7]
RP   VARIANTS CRPT2 ARG-199; HIS-1566 AND GLY-2434.
RX   PubMed=23063620; DOI=10.1016/j.ajhg.2012.08.027;
RA   Twigg S.R., Lloyd D., Jenkins D., Elcioglu N.E., Cooper C.D.,
RA   Al-Sannaa N., Annagur A., Gillessen-Kaesbach G., Huning I.,
RA   Knight S.J., Goodship J.A., Keavney B.D., Beales P.L., Gileadi O.,
RA   McGowan S.J., Wilkie A.O.;
RT   "Mutations in multidomain protein MEGF8 identify a Carpenter syndrome
RT   subtype associated with defective lateralization.";
RL   Am. J. Hum. Genet. 91:897-905(2012).
CC   -!- INTERACTION:
CC       O15265:ATXN7; NbExp=2; IntAct=EBI-947617, EBI-708350;
CC       O00555:CACNA1A; NbExp=2; IntAct=EBI-947617, EBI-766279;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z7M0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z7M0-2; Sequence=VSP_036067;
CC   -!- DISEASE: Carpenter syndrome 2 (CRPT2) [MIM:614976]: An autosomal
CC       recessive multiple congenital malformation disorder characterized
CC       by multisuture craniosynostosis and polysyndactyly of the hands
CC       and feet, in association with abnormal left-right patterning and
CC       other features, most commonly obesity, umbilical hernia,
CC       cryptorchidism, and congenital heart disease. Note=The disease is
CC       caused by mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Contains 2 CUB domains.
CC   -!- SIMILARITY: Contains 5 EGF-like domains.
CC   -!- SIMILARITY: Contains 12 Kelch repeats.
CC   -!- SIMILARITY: Contains 4 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 7 PSI domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP35084.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAA32469.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AB011541; BAA32469.2; ALT_INIT; mRNA.
DR   EMBL; AC011497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC153880; AAI53881.1; -; mRNA.
DR   EMBL; AY280362; AAP35084.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12604.2; -. [Q7Z7M0-2]
DR   CCDS; CCDS62693.1; -. [Q7Z7M0-1]
DR   PIR; T00209; T00209.
DR   RefSeq; NP_001258867.1; NM_001271938.1. [Q7Z7M0-1]
DR   RefSeq; NP_001401.2; NM_001410.2. [Q7Z7M0-2]
DR   UniGene; Hs.132483; -.
DR   ProteinModelPortal; Q7Z7M0; -.
DR   SMR; Q7Z7M0; 39-203, 211-343, 1084-1259, 1430-1483, 2201-2373.
DR   BioGrid; 108274; 6.
DR   IntAct; Q7Z7M0; 8.
DR   MINT; MINT-2808456; -.
DR   STRING; 9606.ENSP00000334219; -.
DR   PhosphoSite; Q7Z7M0; -.
DR   DMDM; 218511690; -.
DR   PaxDb; Q7Z7M0; -.
DR   PRIDE; Q7Z7M0; -.
DR   Ensembl; ENST00000251268; ENSP00000251268; ENSG00000105429. [Q7Z7M0-1]
DR   Ensembl; ENST00000334370; ENSP00000334219; ENSG00000105429. [Q7Z7M0-2]
DR   GeneID; 1954; -.
DR   KEGG; hsa:1954; -.
DR   UCSC; uc002otl.4; human. [Q7Z7M0-2]
DR   UCSC; uc002otm.5; human. [Q7Z7M0-1]
DR   CTD; 1954; -.
DR   GeneCards; GC19P042829; -.
DR   HGNC; HGNC:3233; MEGF8.
DR   HPA; HPA049248; -.
DR   MIM; 604267; gene.
DR   MIM; 614976; phenotype.
DR   neXtProt; NX_Q7Z7M0; -.
DR   Orphanet; 65759; Carpenter syndrome.
DR   PharmGKB; PA27666; -.
DR   eggNOG; NOG304142; -.
DR   HOGENOM; HOG000113554; -.
DR   HOVERGEN; HBG108128; -.
DR   OMA; GHSMVFH; -.
DR   OrthoDB; EOG7J9VRK; -.
DR   PhylomeDB; Q7Z7M0; -.
DR   TreeFam; TF321873; -.
DR   SignaLink; Q7Z7M0; -.
DR   ChiTaRS; MEGF8; human.
DR   GenomeRNAi; 1954; -.
DR   NextBio; 7919; -.
DR   PRO; PR:Q7Z7M0; -.
DR   ArrayExpress; Q7Z7M0; -.
DR   Bgee; Q7Z7M0; -.
DR   CleanEx; HS_MEGF8; -.
DR   Genevestigator; Q7Z7M0; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProt.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProt.
DR   GO; GO:0097094; P:craniofacial suture morphogenesis; IMP:UniProt.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISS:UniProt.
DR   GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:UniProt.
DR   GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:UniProt.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProt.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProt.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProt.
DR   GO; GO:0055113; P:epiboly involved in gastrulation with mouth forming second; IMP:UniProt.
DR   GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProt.
DR   GO; GO:0060972; P:left/right pattern formation; IMP:UniProt.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:UniProt.
DR   GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:UniProt.
DR   GO; GO:0010468; P:regulation of gene expression; ISS:UniProt.
DR   Gene3D; 2.120.10.80; -; 3.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00423; PSI; 9.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Complete proteome; Craniosynostosis;
KW   Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Kelch repeat; Laminin EGF-like domain; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   2845       Multiple epidermal growth factor-like
FT                                domains protein 8.
FT                                /FTId=PRO_0000055629.
FT   TOPO_DOM     28   2647       Extracellular (Potential).
FT   TRANSMEM   2648   2668       Helical; (Potential).
FT   TOPO_DOM   2669   2845       Cytoplasmic (Potential).
FT   DOMAIN       30    140       CUB 1.
FT   DOMAIN      138    168       EGF-like 1.
FT   DOMAIN      170    203       EGF-like 2.
FT   REPEAT      241    287       Kelch 1.
FT   REPEAT      290    338       Kelch 2.
FT   REPEAT      346    399       Kelch 3.
FT   REPEAT      402    453       Kelch 4.
FT   REPEAT      459    511       Kelch 5.
FT   REPEAT      525    575       Kelch 6.
FT   DOMAIN      561    613       PSI 1.
FT   DOMAIN      847    899       PSI 2.
FT   DOMAIN      900    947       PSI 3.
FT   DOMAIN     1074   1115       EGF-like 3; calcium-binding (Potential).
FT   DOMAIN     1163   1210       Laminin EGF-like 1.
FT   DOMAIN     1211   1261       Laminin EGF-like 2.
FT   DOMAIN     1263   1405       CUB 2.
FT   DOMAIN     1403   1445       EGF-like 4.
FT   REPEAT     1522   1570       Kelch 7.
FT   REPEAT     1580   1626       Kelch 8.
FT   REPEAT     1632   1679       Kelch 9.
FT   REPEAT     1685   1735       Kelch 10.
FT   REPEAT     1796   1843       Kelch 11.
FT   REPEAT     1852   1898       Kelch 12.
FT   DOMAIN     1876   1916       PSI 4.
FT   DOMAIN     1924   1979       PSI 5.
FT   DOMAIN     2060   2118       PSI 6.
FT   DOMAIN     2120   2177       PSI 7.
FT   DOMAIN     2178   2216       EGF-like 5.
FT   DOMAIN     2253   2301       Laminin EGF-like 3.
FT   DOMAIN     2380   2443       Laminin EGF-like 4.
FT   COMPBIAS   2528   2564       Pro-rich.
FT   COMPBIAS   2739   2833       Gly-rich.
FT   MOD_RES    1353   1353       Phosphothreonine (By similarity).
FT   CARBOHYD     50     50       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    217    217       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1048   1048       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1271   1271       N-linked (GlcNAc...).
FT   CARBOHYD   2066   2066       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2229   2229       N-linked (GlcNAc...) (Potential).
FT   DISULFID     30     57       By similarity.
FT   DISULFID    142    152       By similarity.
FT   DISULFID    146    158       By similarity.
FT   DISULFID    174    184       By similarity.
FT   DISULFID    178    191       By similarity.
FT   DISULFID    193    202       By similarity.
FT   DISULFID   1078   1091       By similarity.
FT   DISULFID   1085   1100       By similarity.
FT   DISULFID   1102   1114       By similarity.
FT   DISULFID   1163   1171       By similarity.
FT   DISULFID   1165   1179       By similarity.
FT   DISULFID   1182   1191       By similarity.
FT   DISULFID   1194   1208       By similarity.
FT   DISULFID   1211   1224       By similarity.
FT   DISULFID   1213   1231       By similarity.
FT   DISULFID   1233   1242       By similarity.
FT   DISULFID   1245   1259       By similarity.
FT   DISULFID   1263   1302       By similarity.
FT   DISULFID   1336   1367       By similarity.
FT   DISULFID   1407   1421       By similarity.
FT   DISULFID   1415   1433       By similarity.
FT   DISULFID   1435   1444       By similarity.
FT   DISULFID   2182   2195       By similarity.
FT   DISULFID   2189   2204       By similarity.
FT   DISULFID   2253   2261       By similarity.
FT   DISULFID   2255   2270       By similarity.
FT   DISULFID   2273   2282       By similarity.
FT   DISULFID   2285   2299       By similarity.
FT   DISULFID   2380   2389       By similarity.
FT   DISULFID   2382   2397       By similarity.
FT   DISULFID   2399   2424       By similarity.
FT   DISULFID   2427   2441       By similarity.
FT   VAR_SEQ     700    766       Missing (in isoform 2).
FT                                /FTId=VSP_036067.
FT   VARIANT     199    199       G -> R (in CRPT2).
FT                                /FTId=VAR_069305.
FT   VARIANT    1566   1566       R -> H (in CRPT2).
FT                                /FTId=VAR_069306.
FT   VARIANT    2434   2434       S -> G (in CRPT2).
FT                                /FTId=VAR_069307.
SQ   SEQUENCE   2845 AA;  303100 MW;  DDBF0EE07511587D CRC64;
     MALGKVLAMA LVLALAVLGS LSPGARAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
     IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPRGPLLA SLSGSTRPPP IEASSGKMLL
     HLFSDANYNL LGFNASFRFS LCPGGCQSHG QCQPPGVCAC EPGWGGPDCG LQECSAYCGS
     HGTCASPLGP CRCEPGFLGR ACDLHLWENQ GAGWWHNVSA RDPAFSARIG AAGAFLSPPG
     LLAVFGGQDL NNALGDLVLY NFSANTWESW DLSPAPAARH SHVAVAWAGS LVLMGGELAD
     GSLTNDVWAF SPLGRGHWEL LAPPASSSSG PPGLAGHAAA LVDDVWLYVS GGRTPHDLFS
     SGLFRFRLDS TSGGYWEQVI PAGGRPPAAT GHSMVFHAPS RALLVHGGHR PSTARFSVRV
     NSTELFHVDR HVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
     IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
     MAYKVPPFVF QAPAPDYHLD YCSMYTDHSV CSRDPECSWC QGACQAAPPP GTPLGACPAA
     SCLGLGRLLG DCQACLAFSS PTAPPRGPGT LGWCVHNESC LPRPEQARCR GEQISGTVGW
     WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNTSQPDKV SIVRSTTITL TPSAETDVSL
     VYRGFIYPML PGGPGGPGAE DVAVWTRAQR LHVLARMARG PDTENMEEVG RWVAHQEKET
     RRLQRPGSAR LFPLPGRDHK YAVEIQGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
     EPYRSSSCTS YSSCLGCLAD QGCGWCLTSA TCHLRQGGAH CGDDGAGGSL LVLVPTLCPL
     CEEHRDCHAC TQDPFCEWHQ STSRKGDAAC SRRGRGRGAL KSPEECPPLC SQRLTCEDCL
     ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCDGFL TCHECLQSHE
     CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
     GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ISHCNRTCLE DCGHGVCSGP PDFTCVCDLG
     WTSDLPPPTP APGPPAPRCS RDCGCSFHSH CRKRGPGFCD ECQDWTWGEH CERCRPGSFG
     NATGSRGCRP CQCNGHGDPR RGHCDNLSGL CFCQDHTEGA HCQLCSPGYY GDPRAGGSCF
     RECGGRALLT NVSSVALGSR RVGGLLPPGG GAARAGPGLS YCVWVVSATE ELQPCAPGTL
     CPPLTLTFSP DSSTPCTLSY VLAFDGFPRF LDTGVVQSDR SLIAAFCGQR RDRPLTVQAL
     SGLLVLHWEA NGSSSWGFNA SVGSARCGSG GPGSCPVPQE CVPQDGAAGA GLCRCPQGWA
     GPHCRMALCP ENCNAHTGAG TCNQSLGVCI CAEGFGGPDC ATKLDGGQLV WETLMDSRLS
     ADTASRFLHR LGHTMVDGPD ATLWMFGGLG LPQGLLGNLY RYSVSERRWT QMLAGAEDGG
     PGPSPRSFHA AAYVPAGRGA MYLLGGLTAG GVTRDFWVLN LTTLQWRQEK APQTVELPAV
     AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATGTWV SGAQSGTPPT GLYGHSAVYH
     EATDSLYVFG GFRFHVELAA PSPELYSLHC PDRTWSLLAP SQGAKRDRMR NVRGSSRGLG
     QVPGEQPGSW GFREVRKKMA LWAALAGTGG FLEEISPHLK EPRPRLFHAS ALLGDTMVVL
     GGRSDPDEFS SDVLLYQVNC NAWLLPDLTR SASVGPPMEE SVAHAVAAVG SRLYISGGFG
     GVALGRLLAL TLPPDPCRLL SSPEACNQSG ACTWCHGACL SGDQAHRLGC GGSPCSPMPR
     SPEECRRLRT CSECLARHPR TLQPGDGEAS TPRCKWCTNC PEGACIGRNG SCTSENDCRI
     NQREVFWAGN CSEAACGAAD CEQCTREGKC MWTRQFKRTG ETRRILSVQP TYDWTCFSHS
     LLNVSPMPVE SSPPLPCPTP CHLLPNCTSC LDSKGADGGW QHCVWSSSLQ QCLSPSYLPL
     RCMAGGCGRL LRGPESCSLG CAQATQCALC LRRPHCGWCA WGGQDGGGRC MEGGLSGPRD
     GLTCGRPGAS WAFLSCPPED ECANGHHDCN ETQNCHDQPH GYECSCKTGY TMDNMTGLCR
     PVCAQGCVNG SCVEPDHCRC HFGFVGRNCS TECRCNRHSE CAGVGARDHC LLCRNHTKGS
     HCEQCLPLFV GSAVGGGTCR PCHAFCRGNS HICISRKELQ MSKGEPKKYS LDPEEIENWV
     TEGPSEDEAV CVNCQNNSYG EKCESCLQGY FLLDGKCTKC QCNGHADTCN EQDGTGCPCQ
     NNTETGTCQG SSPSDRRDCY KYQCAKCRES FHGSPLGGQQ CYRLISVEQE CCLDPTSQTN
     CFHEPKRRAL GPGRTVLFGV QPKFTNVDIR LTLDVTFGAV DLYVSTSYDT FVVRVAPDTG
     VHTVHIQPPP APPPPPPPAD GGPRGAGDPG GAGASSGPGA PAEPRVREVW PRGLITYVTV
     TEPSAVLVVR GVRDRLVITY PHEHHALKSS RFYLLLLGVG DPSGPGANGS ADSQGLLFFR
     QDQAHIDLFV FFSVFFSCFF LFLSLCVLLW KAKQALDQRQ EQRRHLQEMT KMASRPFAKV
     TVCFPPDPTA PASAWKPAGL PPPAFRRSEP FLAPLLLTGA GGPWGPMGGG CCPPAIPATT
     AGLRAGPITL EPTEDGMAGV ATLLLQLPGG PHAPNGACLG SALVTLRHRL HEYCGGGGGA
     GGSGHGTGAG RKGLLSQDNL TSMSL
//
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