GenomeNet

Database: UniProt
Entry: Q9QYP0
LinkDB: Q9QYP0
Original site: Q9QYP0 
ID   MEGF8_RAT               Reviewed;        2788 AA.
AC   Q9QYP0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   23-MAY-2018, entry version 113.
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=Egfl4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1915-2788, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; 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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1353, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Acts as a negative regulator of hedgehog signaling.
CC       {ECO:0000250|UniProtKB:P60882}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC       {ECO:0000269|PubMed:9693030}.
DR   EMBL; AABR03001918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03001941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03004237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB011534; BAA88689.1; -; mRNA.
DR   UniGene; Rn.21378; -.
DR   ProteinModelPortal; Q9QYP0; -.
DR   SMR; Q9QYP0; -.
DR   IntAct; Q9QYP0; 1.
DR   STRING; 10116.ENSRNOP00000027831; -.
DR   iPTMnet; Q9QYP0; -.
DR   PhosphoSitePlus; Q9QYP0; -.
DR   PaxDb; Q9QYP0; -.
DR   PRIDE; Q9QYP0; -.
DR   UCSC; RGD:621190; rat.
DR   RGD; 621190; Megf8.
DR   eggNOG; KOG1388; Eukaryota.
DR   eggNOG; ENOG410YF0N; LUCA.
DR   HOGENOM; HOG000113554; -.
DR   HOVERGEN; HBG108128; -.
DR   InParanoid; Q9QYP0; -.
DR   PhylomeDB; Q9QYP0; -.
DR   TreeFam; TF321873; -.
DR   PRO; PR:Q9QYP0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISS:UniProtKB.
DR   GO; GO:0061371; P:determination of heart left/right asymmetry; ISS:UniProtKB.
DR   GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:UniProtKB.
DR   GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
DR   GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProtKB.
DR   GO; GO:0060972; P:left/right pattern formation; ISS:UniProtKB.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.120.10.80; -; 4.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 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; 13.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00180; EGF_Lam; 4.
DR   SMART; SM00423; PSI; 9.
DR   SUPFAM; SSF117281; SSF117281; 2.
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; 5.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
PE   1: Evidence at protein level;
KW   Calcium; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Kelch repeat; Laminin EGF-like domain; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   2788       Multiple epidermal growth factor-like
FT                                domains protein 8.
FT                                /FTId=PRO_0000055631.
FT   TOPO_DOM     28   2590       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2591   2611       Helical. {ECO:0000255}.
FT   TOPO_DOM   2612   2788       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       30    140       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      138    168       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      170    203       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
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.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1163   1210       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1211   1261       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1263   1405       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN     1403   1445       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1522   1570       Kelch 7.
FT   REPEAT     1580   1626       Kelch 8.
FT   REPEAT     1632   1678       Kelch 9.
FT   REPEAT     1684   1734       Kelch 10.
FT   REPEAT     1739   1786       Kelch 11.
FT   REPEAT     1795   1840       Kelch 12.
FT   DOMAIN     1819   1859       PSI 4.
FT   DOMAIN     1867   1922       PSI 5.
FT   DOMAIN     2003   2061       PSI 6.
FT   DOMAIN     2063   2120       PSI 7.
FT   DOMAIN     2121   2159       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     2196   2244       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     2323   2386       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   COMPBIAS   2471   2486       Pro-rich.
FT   COMPBIAS   2682   2776       Gly-rich.
FT   MOD_RES    1353   1353       Phosphothreonine.
FT                                {ECO:0000244|PubMed:16641100}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1048   1048       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1271   1271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2009   2009       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2157   2157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2172   2172       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     30     57       {ECO:0000250}.
FT   DISULFID    142    152       {ECO:0000250}.
FT   DISULFID    146    158       {ECO:0000250}.
FT   DISULFID    174    184       {ECO:0000250}.
FT   DISULFID    178    191       {ECO:0000250}.
FT   DISULFID    193    202       {ECO:0000250}.
FT   DISULFID   1078   1091       {ECO:0000250}.
FT   DISULFID   1085   1100       {ECO:0000250}.
FT   DISULFID   1102   1114       {ECO:0000250}.
FT   DISULFID   1163   1171       {ECO:0000250}.
FT   DISULFID   1165   1179       {ECO:0000250}.
FT   DISULFID   1182   1191       {ECO:0000250}.
FT   DISULFID   1194   1208       {ECO:0000250}.
FT   DISULFID   1211   1224       {ECO:0000250}.
FT   DISULFID   1213   1231       {ECO:0000250}.
FT   DISULFID   1233   1242       {ECO:0000250}.
FT   DISULFID   1245   1259       {ECO:0000250}.
FT   DISULFID   1263   1302       {ECO:0000250}.
FT   DISULFID   1336   1367       {ECO:0000250}.
FT   DISULFID   1407   1421       {ECO:0000250}.
FT   DISULFID   1415   1433       {ECO:0000250}.
FT   DISULFID   1435   1444       {ECO:0000250}.
FT   DISULFID   2125   2138       {ECO:0000250}.
FT   DISULFID   2132   2147       {ECO:0000250}.
FT   DISULFID   2196   2204       {ECO:0000250}.
FT   DISULFID   2198   2213       {ECO:0000250}.
FT   DISULFID   2216   2225       {ECO:0000250}.
FT   DISULFID   2228   2242       {ECO:0000250}.
SQ   SEQUENCE   2788 AA;  297554 MW;  0CFB8141F3E03C10 CRC64;
     MALGGALAAA LALAFAVLGP LSHKVLAGDC KGQRQVLREA PGFVTDGAGN YSVNGNCEWL
     IEAPSPQHRI LLDFLFLDTE CTYDYLFVYD GDSPQGPLLA SLSGSTRPPP IEASSGKMLL
     HLFSDANYNL LGFNASFRFS LCPGGCQNHG QCKSPGVCVC EPGWGGPDCG LQECSAYCGS
     HGTCASTLGP CRCEPGFLGR ACDLHLWENQ GAGWWHSVSA GDPAFSARVG AAGAFLSPPG
     LLAVFGGQDL NKALGDLVLY NFSTNTWESW DLTPAPAARH SHVAVAWAGF LVLMGGELAN
     GLLTNDVWAF SPLGGGHWEL LAPPASSSSG PPGLAGHAAA LVDDIWLYVS GGRTQHDLFS
     SGLFRFRLDH TSRGYWEQVI PAGGRPPAAT GHSMVFHAPS RTLLVHGGHR PSTARFSVRV
     NSTELFHVDR RVWTTLKGRD GLQGPRERAF HTASVLGNYM VVYGGNVHTH YQEEKCYEDG
     IFFYHLGCHQ WVSGAELAPP GTPEGRAAPP SGRYSHVAAV LGGSVLLVAG GYSGRPRGDL
     MAYKVPPFVF QAPALDYHLD YCSMYTDHSV CSRDPECSWC QGACQSAPPP GTPSGACPAA
     SCLGLGRLLS DCQACLAFSS PTAPPRGPGT LGWCVHNESC LPRPEQARCR GEQISGTVGW
     WGPAPVFVTS LEACVTQSFL PGLHLLTFQQ PPNASQPDKV SIVRSTTITL TPSAETDVSL
     VYRGFIYPML PGGPGGPGAE DVAVWARAQR LHVLARMARG PDTENMEEVG RWVAQQEKET
     RRLQRPGSSR LFPLPGRGNK YAVEIRGQLN GSAGPGHSEL TLLWDRTGVP GGSEISFFFL
     EPYRSLACSS YSSCLGCLAD QGCGWCLNSA TCHLRQGRAH CEDDGNGESL LVLVPALCPL
     CEEHRDCHAC TQDPFCEWHQ STNRKGDAAC SRRGRGRGAL KNPEECPPLC SQRLTCEDCL
     ANSSQCAWCQ STHTCFLFAA YLARYPHGGC RGWDDSVHSE PRCRSCHGFL TCHECLQSHE
     CGWCGNEDNP TLGRCLQGDF SGPLGGGNCS LWVGEGLGLP VALPARWAYA RCPDVDECRL
     GLARCHPRAT CLNTPLSYEC HCQRGYQGDG ITHCNRTCLE DCGHGVCSGP PDFTCVCDLG
     WTSDLPPPTP APGPPAPRCS RDCGCNFHSH CRRRGPGYCD ECQDWTWGEH CERCRPGSFG
     NATGSGGCRP CQCNGHGDPR RGHCDNLSGL CFCQDHTEGA HCQICSPGYY GDPRAGGSCF
     RECGGRALLT NVSSVALGSR RFGGLLPPGG GTARAGPGLS YCVWVVSATE ALQPCAPGTL
     CPPLTLTFSP DSSTPCTLSY VLAFDGFPRF LDTGVVQSDR SLIAAFCGQR RDRPLTVQAL
     SGLLVLHWEA NGSSSWGFNA SVGSARCGSG GPGSCPVPQE CVPQDGAAGA GLCRCPQGWA
     GPHCRMALCP ENCNAHTGAG ICNQSLGVCI CAEGFGGPDC ATKLDGGQLV WETLMDSRLS
     ADTASRFLHR LGHTMVEGPD ATLWMFGGLG LPQGLLGNLY RYSVSERRWT QMLAGAEDGG
     PGPSPRSFHA AAYVPAGRGA MYLLGGLTAG GITCDFWVLN LTTLQWRQEK APQSIELPAV
     AGHTLTARRG LSLLLVGGYS PENGFNQQLL EYQLATTWVS GAQSGTPPTG LYGHSAVYHE
     ATDSLYVFGG FRFHVELAAP SPELYSLHCP DRTWSLLAPS QGAKPRPRLF HASALLGDTM
     VVLGGRSDPD EFSSDVLLYQ VNCNTWLLPD LTRPAFVGSP MEESVAHAVA AVGSRLYISG
     GFGGVALGRL LALTLPPDPC RLLPSPEACN QSGACTWCHG ACLSGDQAHR LGCGVPPCSP
     MPRSPEECRR LRTCSECLAR HPRTLQPGDG EASVPRCKWC TNCPEGACIG RNGSCTSEND
     CRINQREVFW AGNCSEAACG AADCEQCTRE GKCMWTRQFK RTGETRRILS VQPTYDWTCF
     SHSLLNVSPM PVESSPPLPC PTPCHLLPNC TSCLASKGAD GGWQHCVWSS SLQQCLSPSY
     LPLRCMAGGC GRLLRGPESC SLGCAQATQC ALCLRRPHCG WCAWGGQDGG GHCMEGGLSG
     PRDGLTCGRP GASWAFLSCP PEDECANGHH DCNETQNCHD QPHGYECSCK TGYTMDNVTG
     VCRPVCAQGC VNGSCVEPDH CRCHFGFVGR NCSTECRCNR HSECAGVGAR DHCLLCRNHT
     KGSHCEQCLP LFVGSALGGG TCRPCHAFCR GNSHVCVSRK ELEMARREPE KYSLDPEEIE
     AWVAEGPSED EAVCVNCQNN SYGDRCESCL HGYFLLDGKC TKCQCNGHAD TCNEQDGTGC
     PCQNNTETGV CQGSSPSDRR DCYKYQCAKC RESFHGSPLG GQQCYRLISV EQECCLDPTS
     QTNCFHEPKR RALGPGRTVL FGVQPKFTNV DIRLTLDVTF GAVDLYVSTS YDTFVVRVAP
     DTGVHTVHIQ PPPPPPPPPP PADGVPRVAS DLGGLGTGSG SGSPVEPRVR EVWPRGLITY
     VTVTEPSAVL VVRSVRDRLV ITYPHEHHAL KSSRFYLLLL GVGDPNGPGA NGSADSQGLL
     FFRQDQAHID LFVFFSVFFS CFFLFLSLCV LLWKAKQALD QRQEQRRHLQ EMTKMASRPF
     AKVTVCFPPD PAGPAPAWKP AGLPPPAFRR SEPFLAPLLL TGAGGPWGPM GGGCCPPALP
     ATTAGLRAGP ITLEPTEDGM AGVATLLLQL PGGPHAPNGA CLGSALVTLR HRLHEYCGGS
     GGAGGSGHGG GGGRKGLLSQ DNLTSMSL
//
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