MEG10_DANRE
ID MEG10_DANRE Reviewed; 1119 AA.
AC E9QJQ6; A0A0B5JFJ1;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000303|PubMed:22371254};
DE Short=Multiple EGF-like domains protein 10 {ECO:0000305};
DE Flags: Precursor;
GN Name=megf10 {ECO:0000303|PubMed:22371254};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AJG06078.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-849.
RX PubMed=26190107; DOI=10.1016/j.celrep.2015.06.047;
RA Gao X., Metzger U., Panza P., Mahalwar P., Alsheimer S., Geiger H.,
RA Maischein H.M., Levesque M.P., Templin M., Sollner C.;
RT "A Floor-Plate Extracellular Protein-Protein Interaction Screen Identifies
RT Draxin as a Secreted Netrin-1 Antagonist.";
RL Cell Rep. 12:694-708(2015).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22371254; DOI=10.1007/s10048-012-0315-z;
RA Boyden S.E., Mahoney L.J., Kawahara G., Myers J.A., Mitsuhashi S.,
RA Estrella E.A., Duncan A.R., Dey F., Dechene E.T., Blasko-Goehringer J.M.,
RA Bonnemann C.G., Darras B.T., Mendell J.R., Lidov H.G., Nishino I.,
RA Beggs A.H., Kunkel L.M., Kang P.B.;
RT "Mutations in the satellite cell gene MEGF10 cause a recessive congenital
RT myopathy with minicores.";
RL Neurogenetics 13:115-124(2012).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 110-CYS--LYS-1119.
RX DOI=10.1093/hmg/ddz064;
RA Saha M., Rizzo S.A., Ramanathan M., Hightower R.M., Santostefano K.E.,
RA Terada N., Finkel R.S., Berg J.S., Chahin N., Pacak C.A., Wagner R.E.,
RA Alexander M.S., Draper I., Kang P.B.;
RT "Selective serotonin reuptake inhibitors ameliorate MEGF10 myopathy.";
RL Hum. Mol. Genet. 2019:0-0(2019).
CC -!- FUNCTION: Membrane receptor involved in phagocytosis by macrophages and
CC astrocytes of apoptotic cells (By similarity). Essential factor in the
CC regulation of muscle development including myogenesis (PubMed:22371254,
CC Ref.4). Likely plays a key role in muscle cell proliferation, adhesion
CC and motility (PubMed:22371254, Ref.4). May control the balance between
CC skeletal muscle satellite cells proliferation and differentiation
CC through regulation of the notch signaling pathway (Ref.4).
CC {ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:22371254,
CC ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96KG7};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown causes widespread disruption
CC of myofibril organization and decreased muscle striation resulting in
CC curled or bent tails, impaired swimming, and reduced motility in
CC response to touch. Severely bent tails result from subtle abnormalities
CC in somite boundaries and abundant gaps between myofibers.
CC {ECO:0000269|PubMed:22371254}.
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
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DR EMBL; CR396586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KM655732; AJG06078.1; -; mRNA.
DR AlphaFoldDB; E9QJQ6; -.
DR STRING; 7955.ENSDARP00000129223; -.
DR PaxDb; E9QJQ6; -.
DR Ensembl; ENSDART00000043936; ENSDARP00000043935; ENSDARG00000017229.
DR ZFIN; ZDB-GENE-080506-1; megf10.
DR GeneTree; ENSGT00940000157703; -.
DR InParanoid; E9QJQ6; -.
DR OMA; SSHCGCK; -.
DR PhylomeDB; E9QJQ6; -.
DR TreeFam; TF332598; -.
DR PRO; PR:E9QJQ6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000017229; Expressed in retina and 10 other tissues.
DR ExpressionAtlas; E9QJQ6; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043277; P:apoptotic cell clearance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0030239; P:myofibril assembly; IMP:ZFIN.
DR GO; GO:1901863; P:positive regulation of muscle tissue development; IMP:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF00053; Laminin_EGF; 6.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 14.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Laminin EGF-like domain; Membrane; Myogenesis; Phagocytosis;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1119
FT /note="Multiple epidermal growth factor-like domains
FT protein 10"
FT /evidence="ECO:0000255"
FT /id="PRO_5003244777"
FT TOPO_DOM 23..851
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 873..1119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..104
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 98..133
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 141..176
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 184..219
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 227..261
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 274..304
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 312..347
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 401..436
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 444..479
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 487..522
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 573..608
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 616..653
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 666..696
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 709..739
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 747..782
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 795..825
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 57..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 91..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DISULFID 102..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 106..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 123..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 145..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 151..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 188..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 194..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 231..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 237..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 252..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 277..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 279..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 294..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 316..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 322..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 337..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 405..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 411..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 426..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 448..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 454..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 469..478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 491..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 497..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 512..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 577..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 583..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 598..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 620..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 669..677
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 671..684
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 686..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 712..720
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 714..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 729..738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 751..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 757..770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 772..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 798..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..813
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 815..824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 110..1119
FT /note="Missing: Decreased survival. 4 days post-
FT fertilization (dpf) displays significant tail bending due
FT to severe defects in dorsal muscle integrity. Also shows a
FT slight delay in somite formation which is restored by 3
FT dpf."
FT /evidence="ECO:0000269|Ref.4"
SQ SEQUENCE 1119 AA; 120038 MW; 7F8805CE3E407E1C CRC64;
MMSSCGPLLL AVSCCLVALT SSLNLDDPNV CSHWESYSVT VQETYAHPFD QIYYTSCTDI
LNWFKCTQHR VSYRTAYRRG EKTMHRRKSQ CCPGFYESGD ICVPHCAEKC VHGRCVAPNT
CQCEPGWGGA DCSSACDRDH WGPHCSSRCQ CKNEALCNPI TGACICAPGY HGWRCEDLCD
HSTYGNNCQQ KCLCQNNATC HHITGECVCS PGYTGAFCED LCPPGKHGQQ CEERCPCQNG
GVCHHVTGEC SCPAGWGMVC GQPCPTGRFG KNCSQECQCH NGGICSPSTG QCVCSSGYTG
ERCQDQCQVG TYGIGCSQAC RCVNGAQCYH VSGACLCEQG YTGESCEERI CPDGQYGLKC
DRKCPCNTNN TRSCHPMSGE CSCQSGWSGL YCNETCAPGF YGEACQEVCR CQNGADCHSV
SGECICAPGY KGSDCAIACP PGTYGINCTS LCSCKNGAIC SPIDGSCSCQ AGWHGVDCSI
NCPSGTWGLG CNLSCVCGNG GACNALDGKC TCTPGWRGDR CDQHCQDGTY GLDCRERCDC
SHADGCHPST GHCRCLAGWT GIHCDSVCAE GRWGPNCSLS CNCKNSASCS PDEGACECAP
GFRGTTCQHI CSPGVFGHRC SQACPHCVHS NGPCHHVTGQ CECLPGFKGA LCNEVCPSGK
FGKNCGGSCT CTNNGTCSPM DGSCQCYPGW IGSDCSQPCP PGQWGPNCIH TCNCHNGAFC
SAYDGECKCT AGWTGLYCTQ RCPLGFYGKD CVQACQCENG ADCNHISGQC TCRTGFMGRH
CETKCPAGSY GYGCRQVCDC LNNSTCDHMT GTCYCNPGWK GTRCDQAGGN IAESPNSLTS
AALPMDSYQI GAITGIIILV LLVLILLLLF IIYRKKQKGK ESSMPSVTYT PTMRANTDYA
IAESLPQTEV LPNSNYFSNP SYHTLTQCSS PPHINNIPYG KMNNNQLFVN LKNTEPRKRL
SLLDHTGTLP ADWKQGGSFS ELGAYGVDRR YMGKSLRDLV KSLPYHASSC SLNSSENPYA
TIKDPPLLLT KSTECGYVEM KSPAHRDSPY AEIHSSSPAN KNVYEVEPTI SSVQALTNNN
CNGPFCQDPY DLPKNSHIPC HYDLLPTRDS SPSPTEDSK
