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Multiple epidermal growth factor-like domains protein 10 (Multiple EGF-like domains protein 10)

 MEG10_MOUSE             Reviewed;        1147 AA.
Q6DIB5; Q3TLU3; Q3UG73;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
13-FEB-2019, entry version 129.
RecName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000312|MGI:MGI:2685177};
Short=Multiple EGF-like domains protein 10;
Flags: Precursor;
Name=Megf10 {ECO:0000312|MGI:MGI:2685177};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and
MEGF10.";
PLoS ONE 1:E120-E120(2006).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
Suzuki E., Nakayama M.;
"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
assembly protein complex 2 medium chain and induces large vacuole
formation.";
Exp. Cell Res. 313:3729-3742(2007).
[5]
FUNCTION IN MYOGENESIS, AND TISSUE SPECIFICITY.
PubMed=18056409; DOI=10.1083/jcb.200709083;
Holterman C.E., Le Grand F., Kuang S., Seale P., Rudnicki M.A.;
"Megf10 regulates the progression of the satellite cell myogenic
program.";
J. Cell Biol. 179:911-922(2007).
[6]
FUNCTION IN ENDOCYTOSIS.
PubMed=20828568; DOI=10.1016/j.febslet.2010.08.050;
Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W.,
Kim I.S.;
"MEGF10 functions as a receptor for the uptake of amyloid-beta.";
FEBS Lett. 584:3936-3942(2010).
[7]
FUNCTION IN NEURONAL MOSAIC SPACING.
PubMed=22407321; DOI=10.1038/nature10877;
Kay J.N., Chu M.W., Sanes J.R.;
"MEGF10 and MEGF11 mediate homotypic interactions required for mosaic
spacing of retinal neurons.";
Nature 483:465-469(2012).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27170117; DOI=10.1523/JNEUROSCI.3850-15.2016;
Iram T., Ramirez-Ortiz Z., Byrne M.H., Coleman U.A., Kingery N.D.,
Means T.K., Frenkel D., El Khoury J.;
"Megf10 Is a Receptor for C1Q That Mediates Clearance of Apoptotic
Cells by Astrocytes.";
J. Neurosci. 36:5185-5192(2016).
[9]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION
WITH NOTCH1.
PubMed=28498977; DOI=10.1093/hmg/ddx189;
Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
Cho K.A., Pacak C.A., Draper I., Kang P.B.;
"Consequences of MEGF10 deficiency on myoblast function and Notch1
interactions.";
Hum. Mol. Genet. 26:2984-3000(2017).
-!- FUNCTION: Membrane receptor involved in phagocytosis by
macrophages and astrocytes of apoptotic cells. Receptor for C1q,
an eat-me signal, that binds phosphatidylserine expressed on the
surface of apoptotic cells (PubMed:27170117). Cooperates with
ABCA1 within the process of engulfment (By similarity). Promotes
the formation of large intracellular vacuoles and may be
responsible for the uptake of amyloid-beta peptides
(PubMed:20828568). Necessary for astrocyte-dependent apoptotic
neuron clearance in the developing cerebellum (PubMed:27170117).
Plays role in muscle cell proliferation, adhesion and motility. Is
also an essential factor in the regulation of myogenesis. Controls
the balance between skeletal muscle satellite cells proliferation
and differentiation through regulation of the notch signaling
pathway (PubMed:28498977). May also function in the mosaic spacing
of specific neuron subtypes in the retina through homotypic
retinal neuron repulsion. Mosaics provide a mechanism to
distribute each cell type evenly across the retina, ensuring that
all parts of the visual field have access to a full set of
processing elements (PubMed:22407321).
{ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:18056409,
ECO:0000269|PubMed:20828568, ECO:0000269|PubMed:22407321,
ECO:0000269|PubMed:27170117, ECO:0000269|PubMed:28498977}.
-!- SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1.
Interacts with AP2M1. Does not interact with MEGF11 (By
similarity). Binds with high affinity to complement C1q (By
similarity). Interacts (via the cytoplasmic domain) with NOTCH1
(via NICD domain) (PubMed:28498977).
{ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:28498977,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17643423,
ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17643423}. Cell projection, phagocytic cup
{ECO:0000250|UniProtKB:Q96KG7}. Note=Forms an irregular, mosaic-
like adhesion pattern in region of the cell surface that becomes
firmely fixed to the substrate. Expressed at the cell surface in
clusters around cell corpses during engulfment. During the
engulfment of apoptotic thymocytes, recruited at the bottom of the
forming phagocytic cup. Colocalizes with ABCA1 in absence of any
phagocytic challenge. Does not localize within lamellipodia. Does
not localize with MEGF11 (By similarity). Enriched at the sites of
contact with apoptotic thymocyte cells.
{ECO:0000250|UniProtKB:Q96KG7}.
-!- TISSUE SPECIFICITY: Expressed in cerebellum (at protein level).
Expressed in kidney, stellate cells of the cerebellum and
macrophage cell lines. {ECO:0000269|PubMed:17205124,
ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:18056409}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc (at protein
level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.
{ECO:0000269|PubMed:17205124}.
-!- DOMAIN: The EMI and EGF-like domains work in concert to promote
self-assembly.
-!- PTM: Ubiquitinated; mono- and polyubiquitinated forms are
detected. {ECO:0000250|UniProtKB:Q96KG7}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-
1030 may be important for muscle cell proliferation.
{ECO:0000250|UniProtKB:Q96KG7}.
-!- DISRUPTION PHENOTYPE: Mutants show at postnatal day 7 an increased
amount of apoptotic cells in the developing cerebellum. However,
adult brains do not show higher numbers of apoptotic cells in the
cerebellum compared to wild-type. Astrocytes from knockout mice as
well as heterozygous mice have a significant impairment in
engulfment of apoptotic cells (PubMed:27170117). Mutants have
normal mobility and their skeletal muscles show mildly increased
endomysial connective tissue. They display reduced motor activity
after exercise and show slower muscle regeneration
(PubMed:28498977). MEGF10 and DMD double knockout animals have
pronounced fiber size variability and intracellular inclusions in
the quadriceps femoris with extensive endomysial connective tissue
infiltration. Mice develop muscle weakness, kyphosis and a
waddling gait. At 2 months of age, they have reduced contractile
force compared to wild-type mice. They display reduced motor
activity after exercise and they walk shorter distances than wild-
type. They have a delayed regeneration after muscle injury and an
aberrant muscle fber typing and cross-sectional areas
(PubMed:28498977). {ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
-!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK147238; BAE27788.1; -; mRNA.
EMBL; AK148084; BAE28336.1; -; mRNA.
EMBL; AK166316; BAE38699.1; -; mRNA.
EMBL; BC075647; AAH75647.1; -; mRNA.
CCDS; CCDS29264.1; -.
RefSeq; NP_001001979.1; NM_001001979.2.
UniGene; Mm.297863; -.
ProteinModelPortal; Q6DIB5; -.
SMR; Q6DIB5; -.
STRING; 10090.ENSMUSP00000075174; -.
iPTMnet; Q6DIB5; -.
PhosphoSitePlus; Q6DIB5; -.
MaxQB; Q6DIB5; -.
PaxDb; Q6DIB5; -.
PeptideAtlas; Q6DIB5; -.
PRIDE; Q6DIB5; -.
Ensembl; ENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
GeneID; 70417; -.
KEGG; mmu:70417; -.
UCSC; uc008eyz.2; mouse.
CTD; 84466; -.
MGI; MGI:2685177; Megf10.
eggNOG; KOG1218; Eukaryota.
eggNOG; ENOG410XQWV; LUCA.
GeneTree; ENSGT00940000157703; -.
HOGENOM; HOG000294130; -.
HOVERGEN; HBG108333; -.
InParanoid; Q6DIB5; -.
OrthoDB; 561378at2759; -.
PhylomeDB; Q6DIB5; -.
TreeFam; TF332598; -.
ChiTaRS; Megf10; mouse.
PRO; PR:Q6DIB5; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024593; Expressed in 162 organ(s), highest expression level in utricle of membranous labyrinth.
ExpressionAtlas; Q6DIB5; baseline and differential.
Genevisible; Q6DIB5; MM.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0001891; C:phagocytic cup; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; ISO:MGI.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
GO; GO:1902742; P:apoptotic process involved in development; IMP:MGI.
GO; GO:0043652; P:engulfment of apoptotic cell; IMP:MGI.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0055001; P:muscle cell development; ISS:UniProtKB.
GO; GO:0033002; P:muscle cell proliferation; ISO:MGI.
GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI.
GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
GO; GO:0048641; P:regulation of skeletal muscle tissue development; ISO:MGI.
GO; GO:0014719; P:skeletal muscle satellite cell activation; IMP:UniProtKB.
GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:UniProtKB.
GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IDA:UniProtKB.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR011489; EMI_domain.
InterPro; IPR002049; Laminin_EGF.
Pfam; PF12661; hEGF; 7.
Pfam; PF00053; Laminin_EGF; 6.
SMART; SM00181; EGF; 17.
SMART; SM00180; EGF_Lam; 14.
PROSITE; PS00022; EGF_1; 17.
PROSITE; PS01186; EGF_2; 17.
PROSITE; PS50026; EGF_3; 15.
PROSITE; PS51041; EMI; 1.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Cell projection; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Myogenesis;
Phagocytosis; Phosphoprotein; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1147 Multiple epidermal growth factor-like
domains protein 10.
/FTId=PRO_0000309733.
TOPO_DOM 26 857 Extracellular. {ECO:0000255}.
TRANSMEM 858 878 Helical. {ECO:0000255}.
TOPO_DOM 879 1147 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 107 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 101 136 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 144 179 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 187 222 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 230 265 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 278 308 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 316 351 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 405 440 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 453 483 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 491 526 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 539 569 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 577 612 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 665 700 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 713 743 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 751 786 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 799 829 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 1 857 Necessary for interaction with AP2M1,
self-assembly and formation of the
irregular, mosaic-like adhesion pattern.
{ECO:0000250|UniProtKB:Q96KG7}.
REGION 945 1147 Necessary for formation of large
intracellular vacuoles.
{ECO:0000250|UniProtKB:Q96KG7}.
COMPBIAS 1119 1146 Ser-rich.
MOD_RES 1030 1030 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q96KG7}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 95 {ECO:0000255}.
DISULFID 60 69 {ECO:0000255}.
DISULFID 94 105 {ECO:0000255}.
DISULFID 109 124 {ECO:0000250}.
DISULFID 126 135 {ECO:0000250}.
DISULFID 148 160 {ECO:0000250}.
DISULFID 154 167 {ECO:0000250}.
DISULFID 169 178 {ECO:0000250}.
DISULFID 191 203 {ECO:0000250}.
DISULFID 197 210 {ECO:0000250}.
DISULFID 212 221 {ECO:0000250}.
DISULFID 234 246 {ECO:0000250}.
DISULFID 240 253 {ECO:0000250}.
DISULFID 255 264 {ECO:0000250}.
DISULFID 281 289 {ECO:0000250}.
DISULFID 283 296 {ECO:0000250}.
DISULFID 298 307 {ECO:0000250}.
DISULFID 320 332 {ECO:0000250}.
DISULFID 326 339 {ECO:0000250}.
DISULFID 341 350 {ECO:0000250}.
DISULFID 409 421 {ECO:0000250}.
DISULFID 415 428 {ECO:0000250}.
DISULFID 430 439 {ECO:0000250}.
DISULFID 456 464 {ECO:0000250}.
DISULFID 458 471 {ECO:0000250}.
DISULFID 473 482 {ECO:0000250}.
DISULFID 495 507 {ECO:0000250}.
DISULFID 501 514 {ECO:0000250}.
DISULFID 516 525 {ECO:0000250}.
DISULFID 542 550 {ECO:0000250}.
DISULFID 544 557 {ECO:0000250}.
DISULFID 559 568 {ECO:0000250}.
DISULFID 581 593 {ECO:0000250}.
DISULFID 587 600 {ECO:0000250}.
DISULFID 602 611 {ECO:0000250}.
DISULFID 669 681 {ECO:0000250}.
DISULFID 675 688 {ECO:0000250}.
DISULFID 690 699 {ECO:0000250}.
DISULFID 716 724 {ECO:0000250}.
DISULFID 718 731 {ECO:0000250}.
DISULFID 733 742 {ECO:0000250}.
DISULFID 755 767 {ECO:0000250}.
DISULFID 761 774 {ECO:0000250}.
DISULFID 776 785 {ECO:0000250}.
DISULFID 802 810 {ECO:0000250}.
DISULFID 804 817 {ECO:0000250}.
DISULFID 819 828 {ECO:0000250}.
CONFLICT 323 323 A -> T (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1092 1092 G -> S (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1137 1137 N -> S (in Ref. 1; BAE38699).
{ECO:0000305}.
CONFLICT 1140 1140 S -> T (in Ref. 1; BAE38699).
{ECO:0000305}.
SEQUENCE 1147 AA; 122972 MW; FBC50896096181CC CRC64;
MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC
TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SRDMCVPHCA DKCVHGRCIA
PNTCQCEPGW GGTNCSSACD GDHWGPHCSS RCQCKNRALC NPITGACHCA AGYRGWRCED
RCEQGTYGND CHQRCQCQNG ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC
QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC EARLCPEGLY
GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD
CDSVTGRCAC APGFKGTDCS TPCPLGRYGI NCSSRCGCKN DAVCSPVDGS CICKAGWHGV
DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE
RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC
PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN
GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF
MGRHCEQKCP AGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN
SLSRTSTALP ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR
VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI AKSKNNQLFV
NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSST
CSLSSSENPY ATIKDPPALL PKSSECGYVE MKSPARRDSP YAEINNSTPA NRNVYEVEPT
VSVVQGVFSN SGHVTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS
SSSSSSE


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EIAAB12604 Cbl20,Egfl7,EGF-like protein 7,Epidermal growth factor-like protein 7,Megf7,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,Rat,Rattus norvegicus
EIAAB12603 Egfl7,EGF-like protein 7,Epidermal growth factor-like protein 7,Megf7,Mouse,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,Mus musculus,NOTCH4-like protein
EIAAB14452 Cadherin family member 8,CDHF8,FAT2,hFat2,Homo sapiens,Human,KIAA0811,MEGF1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 2
EIAAB38673 Homo sapiens,Human,KIAA0814,MEGF5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,SLIL2,Slit homolog 3 protein,SLIT3,Slit-3,UNQ691_PRO1336
EIAAB38670 Homo sapiens,Human,KIAA0813,MEGF4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,SLIL1,Slit homolog 1 protein,SLIT1,Slit-1
EIAAB38674 Megf5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,Rat,Rattus norvegicus,Slit homolog 3 protein,Slit3,Slit-3
EIAAB38671 Megf4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,Rat,Rattus norvegicus,Slit homolog 1 protein,Slit1,Slit-1
25-807 INADL is a protein with multiple PDZ domains. PDZ domains mediate protein-protein interactions, and proteins with multiple PDZ domains often organize multimeric complexes at the plasma membrane. This 0.05 mg
TRM2A_MOUSE Rat ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
E0590Ge Rat ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
E15038h Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 10 96T
CSB-EL013680RA Rat Multiple epidermal growth factor-like domains protein 6(MEGF6) ELISA kit 96T
MEGF8_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 8 96T
CSB-EL013681RA Rat Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T
TRI25_HUMAN Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
TRPC7_MOUSE Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 96T
E0589h Human ELISA Kit FOR Multiple epidermal growth factor-like domains protein 6 96T
E0589Rb Mouse ELISA Kit FOR Multiple epidermal growth factor-like domains protein 11 96T
CSB-EL013681MO Mouse Multiple epidermal growth factor-like domains protein 8(MEGF8) ELISA kit 96T

Kits Elisa; taq POLYMERASE

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Pathways :
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1049: G Protein Signaling Pathways
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1165: G Protein Signaling Pathways
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[MEGF10 KIAA1780] Multiple epidermal growth factor-like domains protein 10 (Multiple EGF-like domains protein 10)
[FAT2 CDHF8 KIAA0811 MEGF1] Protocadherin Fat 2 (hFat2) (Cadherin family member 8) (Multiple epidermal growth factor-like domains protein 1) (Multiple EGF-like domains protein 1)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[EGF] Pro-epidermal growth factor (EGF) [Cleaved into: Epidermal growth factor (Urogastrone)]
[MEGF9 EGFL5 KIAA0818 UNQ671/PRO1305] Multiple epidermal growth factor-like domains protein 9 (Multiple EGF-like domains protein 9) (Epidermal growth factor-like protein 5) (EGF-like protein 5)
[Egfr] Epidermal growth factor receptor (EC 2.7.10.1)
[EGFR] Epidermal growth factor receptor (EC 2.7.10.1)
[HBEGF DTR DTS HEGFL] Proheparin-binding EGF-like growth factor [Cleaved into: Heparin-binding EGF-like growth factor (HB-EGF) (HBEGF) (Diphtheria toxin receptor) (DT-R)]
[Egfr c-erbB DER top CG10079] Epidermal growth factor receptor (Egfr) (EC 2.7.10.1) (Drosophila relative of ERBB) (Gurken receptor) (Protein torpedo)
[Tek Hyk Tie-2 Tie2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)
[TEK TIE2 VMCM VMCM1] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (hTIE2) (p140 TEK) (CD antigen CD202b)
[FGFR3 JTK4] Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (CD antigen CD333)
[GRB2 ASH] Growth factor receptor-bound protein 2 (Adapter protein GRB2) (Protein Ash) (SH2/SH3 adapter GRB2)
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[EGFR] Epidermal growth factor receptor (CER) (EC 2.7.10.1) (Fragment)
[FGFR1 BFGFR CEK FGFBR FLG FLT2 HBGFR] Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)
[PDGFRB PDGFR PDGFR1] Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)
[GRB7] Growth factor receptor-bound protein 7 (B47) (Epidermal growth factor receptor GRB-7) (GRB7 adapter protein)
[Erbb2 Neu] Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Epidermal growth factor receptor-related protein) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (p185erbB2) (p185neu) (CD antigen CD340)
[ERBB4 HER4] Receptor tyrosine-protein kinase erbB-4 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-4) (Tyrosine kinase-type cell surface receptor HER4) (p180erbB4) [Cleaved into: ERBB4 intracellular domain (4ICD) (E4ICD) (s80HER4)]
[EPS15 AF1P] Epidermal growth factor receptor substrate 15 (Protein Eps15) (Protein AF-1p)
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)
[TMEFF2 HPP1 TENB2 TPEF UNQ178/PRO204] Tomoregulin-2 (TR-2) (Hyperplastic polyposis protein 1) (Transmembrane protein with EGF-like and two follistatin-like domains)
[PTEN MMAC1 TEP1] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)
[SHANK3 KIAA1650 PROSAP2 PSAP2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2)
[SH3PXD2A FISH KIAA0418 SH3MD1 TKS5] SH3 and PX domain-containing protein 2A (Adapter protein TKS5) (Five SH3 domain-containing protein) (SH3 multiple domains protein 1) (Tyrosine kinase substrate with five SH3 domains)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[Shank3 Kiaa1650 Prosap2] SH3 and multiple ankyrin repeat domains protein 3 (Shank3) (Proline-rich synapse-associated protein 2) (ProSAP2) (SPANK-2)
[Fgfr1 Flg] Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)

Bibliography :
[27460346] Japanese multiple epidermal growth factor 10 (MEGF10) myopathy with novel mutations: A phenotype-genotype correlation.
[16142919] Identification of common and specific growth factor binding sites in heparan sulfate proteoglycans.
[12593722] Evidence that the complement control protein-epidermal growth factor-like domain of thyroid peroxidase lies on the fringe of the immunodominant region recognized by autoantibodies.
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