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Protein

Multiple epidermal growth factor-like domains protein 10

Gene

Megf10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity5 Publications

GO - Molecular functioni

  • complement component C1q binding Source: MGI
  • Notch binding Source: UniProtKB
  • scavenger receptor activity Source: MGI

GO - Biological processi

  • apoptotic process involved in development Source: MGI
  • engulfment of apoptotic cell Source: MGI
  • homotypic cell-cell adhesion Source: UniProtKB
  • muscle cell development Source: UniProtKB
  • muscle cell proliferation Source: MGI
  • myoblast migration Source: UniProtKB
  • recognition of apoptotic cell Source: MGI
  • regulation of muscle cell differentiation Source: UniProtKB
  • regulation of skeletal muscle tissue development Source: MGI
  • skeletal muscle satellite cell activation Source: UniProtKB
  • skeletal muscle satellite cell differentiation Source: UniProtKB
  • skeletal muscle satellite cell proliferation Source: UniProtKB

Keywordsi

Biological processCell adhesion, Myogenesis, Phagocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple epidermal growth factor-like domains protein 10Imported
Short name:
Multiple EGF-like domains protein 10
Gene namesi
Name:Megf10Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2685177. Megf10.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini26 – 857ExtracellularSequence analysisAdd BLAST832
Transmembranei858 – 878HelicalSequence analysisAdd BLAST21
Topological domaini879 – 1147CytoplasmicSequence analysisAdd BLAST269

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Disruption phenotypei

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 heterozigous 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).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000030973326 – 1147Multiple epidermal growth factor-like domains protein 10Add BLAST1122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi34 ↔ 95Sequence analysis
Disulfide bondi60 ↔ 69Sequence analysis
Disulfide bondi94 ↔ 105Sequence analysis
Disulfide bondi109 ↔ 124By similarity
Disulfide bondi126 ↔ 135By similarity
Glycosylationi134N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi148 ↔ 160By similarity
Disulfide bondi154 ↔ 167By similarity
Disulfide bondi169 ↔ 178By similarity
Disulfide bondi191 ↔ 203By similarity
Disulfide bondi197 ↔ 210By similarity
Disulfide bondi212 ↔ 221By similarity
Disulfide bondi234 ↔ 246By similarity
Disulfide bondi240 ↔ 253By similarity
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi281 ↔ 289By similarity
Disulfide bondi283 ↔ 296By similarity
Disulfide bondi298 ↔ 307By similarity
Disulfide bondi320 ↔ 332By similarity
Disulfide bondi326 ↔ 339By similarity
Disulfide bondi341 ↔ 350By similarity
Disulfide bondi409 ↔ 421By similarity
Disulfide bondi415 ↔ 428By similarity
Disulfide bondi430 ↔ 439By similarity
Disulfide bondi456 ↔ 464By similarity
Disulfide bondi458 ↔ 471By similarity
Disulfide bondi473 ↔ 482By similarity
Disulfide bondi495 ↔ 507By similarity
Glycosylationi496N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi501 ↔ 514By similarity
Disulfide bondi516 ↔ 525By similarity
Disulfide bondi542 ↔ 550By similarity
Disulfide bondi544 ↔ 557By similarity
Disulfide bondi559 ↔ 568By similarity
Disulfide bondi581 ↔ 593By similarity
Disulfide bondi587 ↔ 600By similarity
Disulfide bondi602 ↔ 611By similarity
Disulfide bondi669 ↔ 681By similarity
Disulfide bondi675 ↔ 688By similarity
Disulfide bondi690 ↔ 699By similarity
Disulfide bondi716 ↔ 724By similarity
Disulfide bondi718 ↔ 731By similarity
Disulfide bondi733 ↔ 742By similarity
Disulfide bondi755 ↔ 767By similarity
Disulfide bondi761 ↔ 774By similarity
Disulfide bondi776 ↔ 785By similarity
Disulfide bondi802 ↔ 810By similarity
Disulfide bondi804 ↔ 817By similarity
Disulfide bondi819 ↔ 828By similarity
Modified residuei1030PhosphotyrosineBy similarity1

Post-translational modificationi

Ubiquitinated; mono- and polyubiquitinated forms are detected.By similarity
Phosphorylated on tyrosine residues. Phosphorylation at Tyr-1030 may be important for muscle cell proliferation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6DIB5.
PaxDbiQ6DIB5.
PeptideAtlasiQ6DIB5.
PRIDEiQ6DIB5.

PTM databases

iPTMnetiQ6DIB5.
PhosphoSitePlusiQ6DIB5.

Expressioni

Tissue specificityi

Expressed in cerebellum (at protein level). Expressed in kidney, stellate cells of the cerebellum and macrophage cell lines.3 Publications

Developmental stagei

Expressed in embryo at 15 dpc (at protein level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000024593.
CleanExiMM_MEGF10.
ExpressionAtlasiQ6DIB5. baseline and differential.
GenevisibleiQ6DIB5. MM.

Interactioni

Subunit structurei

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).By similarityCurated1 Publication

GO - Molecular functioni

  • complement component C1q binding Source: MGI
  • Notch binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000075174.

Structurei

3D structure databases

ProteinModelPortaliQ6DIB5.
SMRiQ6DIB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 107EMIAdd BLAST78
Domaini101 – 136EGF-like 1Add BLAST36
Domaini144 – 179EGF-like 2Add BLAST36
Domaini187 – 222EGF-like 3Add BLAST36
Domaini230 – 265EGF-like 4Add BLAST36
Domaini278 – 308EGF-like 5Add BLAST31
Domaini316 – 351EGF-like 6Add BLAST36
Domaini405 – 440EGF-like 7Add BLAST36
Domaini453 – 483EGF-like 8Add BLAST31
Domaini491 – 526EGF-like 9Add BLAST36
Domaini539 – 569EGF-like 10Add BLAST31
Domaini577 – 612EGF-like 11Add BLAST36
Domaini665 – 700EGF-like 12Add BLAST36
Domaini713 – 743EGF-like 13Add BLAST31
Domaini751 – 786EGF-like 14Add BLAST36
Domaini799 – 829EGF-like 15Add BLAST31

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 857Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion patternBy similarityAdd BLAST857
Regioni945 – 1147Necessary for formation of large intracellular vacuolesBy similarityAdd BLAST203

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1119 – 1146Ser-richAdd BLAST28

Domaini

The EMI and EGF-like domains work in concert to promote self-assembly.

Sequence similaritiesi

Belongs to the MEGF family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1218. Eukaryota.
ENOG410XQWV. LUCA.
GeneTreeiENSGT00730000110380.
HOGENOMiHOG000294130.
HOVERGENiHBG108333.
InParanoidiQ6DIB5.
OMAiFGCNLTC.
OrthoDBiEOG091G00XN.
PhylomeDBiQ6DIB5.
TreeFamiTF332598.

Family and domain databases

Gene3Di1.20.5.100. 1 hit.
InterProiView protein in InterPro
IPR021157. Cyt_c1_TM_anchor_C.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR011489. EMI_domain.
IPR002049. Laminin_EGF.
PfamiView protein in Pfam
PF12661. hEGF. 8 hits.
PF00053. Laminin_EGF. 6 hits.
SMARTiView protein in SMART
SM00181. EGF. 17 hits.
SM00180. EGF_Lam. 14 hits.
PROSITEiView protein in PROSITE
PS00022. EGF_1. 17 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 15 hits.
PS51041. EMI. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6DIB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH
60 70 80 90 100
PFDQIYYTSC TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE
110 120 130 140 150
SRDMCVPHCA DKCVHGRCIA PNTCQCEPGW GGTNCSSACD GDHWGPHCSS
160 170 180 190 200
RCQCKNRALC NPITGACHCA AGYRGWRCED RCEQGTYGND CHQRCQCQNG
210 220 230 240 250
ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC QNGGVCHHVT
260 270 280 290 300
GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
310 320 330 340 350
GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC
360 370 380 390 400
EARLCPEGLY GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC
410 420 430 440 450
SPGFYGEACQ QICSCQNGAD CDSVTGRCAC APGFKGTDCS TPCPLGRYGI
460 470 480 490 500
NCSSRCGCKN DAVCSPVDGS CICKAGWHGV DCSIRCPSGT WGFGCNLTCQ
510 520 530 540 550
CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE RCDCSHADGC
560 570 580 590 600
HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
610 620 630 640 650
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG
660 670 680 690 700
FTGALCNEVC PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS
710 720 730 740 750
QPCPPAHWGP NCIHTCNCHN GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF
760 770 780 790 800
YGKDCALICQ CQNGADCDHI SGQCTCRTGF MGRHCEQKCP AGTYGYGCRQ
810 820 830 840 850
ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN SLSRTSTALP
860 870 880 890 900
ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR
910 920 930 940 950
VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI
960 970 980 990 1000
AKSKNNQLFV NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR
1010 1020 1030 1040 1050
SYMGKSLKDL GKNSEYNSST CSLSSSENPY ATIKDPPALL PKSSECGYVE
1060 1070 1080 1090 1100
MKSPARRDSP YAEINNSTPA NRNVYEVEPT VSVVQGVFSN SGHVTQDPYD
1110 1120 1130 1140
LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS SSSSSSE
Length:1,147
Mass (Da):122,972
Last modified:August 16, 2004 - v1
Checksum:iFBC50896096181CC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti323A → T in BAE38699 (PubMed:16141072).Curated1
Sequence conflicti1092G → S in BAE38699 (PubMed:16141072).Curated1
Sequence conflicti1137N → S in BAE38699 (PubMed:16141072).Curated1
Sequence conflicti1140S → T in BAE38699 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147238 mRNA. Translation: BAE27788.1.
AK148084 mRNA. Translation: BAE28336.1.
AK166316 mRNA. Translation: BAE38699.1.
BC075647 mRNA. Translation: AAH75647.1.
CCDSiCCDS29264.1.
RefSeqiNP_001001979.1. NM_001001979.2.
UniGeneiMm.297863.

Genome annotation databases

EnsembliENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
GeneIDi70417.
KEGGimmu:70417.
UCSCiuc008eyz.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiMEG10_MOUSE
AccessioniPrimary (citable) accession number: Q6DIB5
Secondary accession number(s): Q3TLU3, Q3UG73
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 16, 2004
Last modified: October 25, 2017
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families