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Multiple epidermal growth factor-like domains protein 8 (Multiple EGF-like domains protein 8) (Epidermal growth factor-like protein 4) (EGF-like protein 4)

 MEGF8_RAT               Reviewed;        2788 AA.
Q9QYP0;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
23-MAY-2018, entry version 113.
RecName: Full=Multiple epidermal growth factor-like domains protein 8;
Short=Multiple EGF-like domains protein 8;
AltName: Full=Epidermal growth factor-like protein 4;
Short=EGF-like protein 4;
Flags: Precursor;
Name=Megf8; Synonyms=Egfl4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1915-2788, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1353, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
-!- FUNCTION: Acts as a negative regulator of hedgehog signaling.
{ECO:0000250|UniProtKB:P60882}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in brain.
{ECO:0000269|PubMed:9693030}.
-----------------------------------------------------------------------
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EMBL; AABR03001918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03001941; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03004237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB011534; BAA88689.1; -; mRNA.
UniGene; Rn.21378; -.
ProteinModelPortal; Q9QYP0; -.
SMR; Q9QYP0; -.
IntAct; Q9QYP0; 1.
STRING; 10116.ENSRNOP00000027831; -.
iPTMnet; Q9QYP0; -.
PhosphoSitePlus; Q9QYP0; -.
PaxDb; Q9QYP0; -.
PRIDE; Q9QYP0; -.
UCSC; RGD:621190; rat.
RGD; 621190; Megf8.
eggNOG; KOG1388; Eukaryota.
eggNOG; ENOG410YF0N; LUCA.
HOGENOM; HOG000113554; -.
HOVERGEN; HBG108128; -.
InParanoid; Q9QYP0; -.
PhylomeDB; Q9QYP0; -.
TreeFam; TF321873; -.
PRO; PR:Q9QYP0; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0071907; P:determination of digestive tract left/right asymmetry; ISS:UniProtKB.
GO; GO:0061371; P:determination of heart left/right asymmetry; ISS:UniProtKB.
GO; GO:0060971; P:embryonic heart tube left/right pattern formation; ISS:UniProtKB.
GO; GO:0003143; P:embryonic heart tube morphogenesis; ISS:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
GO; GO:0097155; P:fasciculation of sensory neuron axon; ISS:UniProtKB.
GO; GO:0060972; P:left/right pattern formation; ISS:UniProtKB.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:UniProtKB.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
CDD; cd00041; CUB; 1.
Gene3D; 2.120.10.80; -; 4.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024731; EGF_dom.
InterPro; IPR015915; Kelch-typ_b-propeller.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR002165; Plexin_repeat.
InterPro; IPR016201; PSI.
InterPro; IPR035914; Sperma_CUB_dom_sf.
Pfam; PF00431; CUB; 1.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00053; Laminin_EGF; 3.
Pfam; PF01437; PSI; 1.
SMART; SM00042; CUB; 1.
SMART; SM00181; EGF; 13.
SMART; SM00179; EGF_CA; 2.
SMART; SM00180; EGF_Lam; 4.
SMART; SM00423; PSI; 9.
SUPFAM; SSF117281; SSF117281; 2.
SUPFAM; SSF49854; SSF49854; 1.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01180; CUB; 2.
PROSITE; PS00022; EGF_1; 6.
PROSITE; PS01186; EGF_2; 7.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS01248; EGF_LAM_1; 4.
PROSITE; PS50027; EGF_LAM_2; 3.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; EGF-like domain;
Glycoprotein; Kelch repeat; Laminin EGF-like domain; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 2788 Multiple epidermal growth factor-like
domains protein 8.
/FTId=PRO_0000055631.
TOPO_DOM 28 2590 Extracellular. {ECO:0000255}.
TRANSMEM 2591 2611 Helical. {ECO:0000255}.
TOPO_DOM 2612 2788 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 140 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 138 168 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 170 203 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 241 287 Kelch 1.
REPEAT 290 338 Kelch 2.
REPEAT 346 399 Kelch 3.
REPEAT 402 453 Kelch 4.
REPEAT 459 511 Kelch 5.
REPEAT 525 575 Kelch 6.
DOMAIN 561 613 PSI 1.
DOMAIN 847 899 PSI 2.
DOMAIN 900 947 PSI 3.
DOMAIN 1074 1115 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1163 1210 Laminin EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1211 1261 Laminin EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 1263 1405 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1403 1445 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1522 1570 Kelch 7.
REPEAT 1580 1626 Kelch 8.
REPEAT 1632 1678 Kelch 9.
REPEAT 1684 1734 Kelch 10.
REPEAT 1739 1786 Kelch 11.
REPEAT 1795 1840 Kelch 12.
DOMAIN 1819 1859 PSI 4.
DOMAIN 1867 1922 PSI 5.
DOMAIN 2003 2061 PSI 6.
DOMAIN 2063 2120 PSI 7.
DOMAIN 2121 2159 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2196 2244 Laminin EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 2323 2386 Laminin EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
COMPBIAS 2471 2486 Pro-rich.
COMPBIAS 2682 2776 Gly-rich.
MOD_RES 1353 1353 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1048 1048 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1271 1271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2009 2009 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2157 2157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2172 2172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 57 {ECO:0000250}.
DISULFID 142 152 {ECO:0000250}.
DISULFID 146 158 {ECO:0000250}.
DISULFID 174 184 {ECO:0000250}.
DISULFID 178 191 {ECO:0000250}.
DISULFID 193 202 {ECO:0000250}.
DISULFID 1078 1091 {ECO:0000250}.
DISULFID 1085 1100 {ECO:0000250}.
DISULFID 1102 1114 {ECO:0000250}.
DISULFID 1163 1171 {ECO:0000250}.
DISULFID 1165 1179 {ECO:0000250}.
DISULFID 1182 1191 {ECO:0000250}.
DISULFID 1194 1208 {ECO:0000250}.
DISULFID 1211 1224 {ECO:0000250}.
DISULFID 1213 1231 {ECO:0000250}.
DISULFID 1233 1242 {ECO:0000250}.
DISULFID 1245 1259 {ECO:0000250}.
DISULFID 1263 1302 {ECO:0000250}.
DISULFID 1336 1367 {ECO:0000250}.
DISULFID 1407 1421 {ECO:0000250}.
DISULFID 1415 1433 {ECO:0000250}.
DISULFID 1435 1444 {ECO:0000250}.
DISULFID 2125 2138 {ECO:0000250}.
DISULFID 2132 2147 {ECO:0000250}.
DISULFID 2196 2204 {ECO:0000250}.
DISULFID 2198 2213 {ECO:0000250}.
DISULFID 2216 2225 {ECO:0000250}.
DISULFID 2228 2242 {ECO:0000250}.
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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Genprice Inc, Invoices and accounting
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