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Q6DIB5 (MEG10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multiple epidermal growth factor-like domains protein 10

Short name=Multiple EGF-like domains protein 10
Gene names
Name:Megf10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Membrane receptor involved in phagocytosis by macrophages of apoptotic cells. Cooperates with ABCA1 within the process of engulfment. Promotes the formation of large intracellular vacuoles and may be responsible for the uptake of amyloid-beta peptides. 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. May play role in cell adhesion and motility. Is also an essential factor in the regulation of myogenesis. Controls the balance between skeletal muscle satellite cells proliferation and differentiation problably through regulation of the notch signaling pathway. Ref.5 Ref.6 Ref.7

Subunit structure

Homopolymer Probable. Interacts with GULP1 and ABCA1. Interacts with AP2M1. Does not interact with MEGF11 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein. Basolateral cell membrane; Single-pass type I membrane protein By similarity. Cell projectionphagocytic cup By similarity. 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. Ref.4

Tissue specificity

Expressed in cerebellum (at protein level). Expressed in kidney, stellate cells of the cerebellum and macrophage cell lines. Ref.3 Ref.4 Ref.5

Developmental stage

Expressed in embryo at 15 dpc (at protein level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc. Ref.3

Domain

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

Post-translational modification

Phosphorylated on tyrosine residues By similarity.

Ubiquitinated; mono- and polyubiquitinated forms are detected By similarity.

Sequence similarities

Belongs to the MEGF family.

Contains 15 EGF-like domains.

Contains 1 EMI domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 11471122Multiple epidermal growth factor-like domains protein 10
PRO_0000309733

Regions

Topological domain26 – 857832Extracellular Potential
Transmembrane858 – 87821Helical; Potential
Topological domain879 – 1147269Cytoplasmic Potential
Domain30 – 10778EMI
Domain101 – 13636EGF-like 1
Domain144 – 17936EGF-like 2
Domain187 – 22236EGF-like 3
Domain230 – 26536EGF-like 4
Domain278 – 30831EGF-like 5
Domain316 – 35136EGF-like 6
Domain405 – 44036EGF-like 7
Domain453 – 48331EGF-like 8
Domain491 – 52636EGF-like 9
Domain539 – 56931EGF-like 10
Domain577 – 61236EGF-like 11
Domain665 – 70036EGF-like 12
Domain713 – 74331EGF-like 13
Domain751 – 78636EGF-like 14
Domain799 – 82931EGF-like 15
Region1 – 857857Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion pattern By similarity
Region945 – 1147203Necessary for formation of large intracellular vacuoles By similarity
Compositional bias1119 – 114628Ser-rich

Amino acid modifications

Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 95 Potential
Disulfide bond60 ↔ 69 Potential
Disulfide bond94 ↔ 105 Potential
Disulfide bond109 ↔ 124 By similarity
Disulfide bond126 ↔ 135 By similarity
Disulfide bond148 ↔ 160 By similarity
Disulfide bond154 ↔ 167 By similarity
Disulfide bond169 ↔ 178 By similarity
Disulfide bond191 ↔ 203 By similarity
Disulfide bond197 ↔ 210 By similarity
Disulfide bond212 ↔ 221 By similarity
Disulfide bond234 ↔ 246 By similarity
Disulfide bond240 ↔ 253 By similarity
Disulfide bond255 ↔ 264 By similarity
Disulfide bond281 ↔ 289 By similarity
Disulfide bond283 ↔ 296 By similarity
Disulfide bond298 ↔ 307 By similarity
Disulfide bond320 ↔ 332 By similarity
Disulfide bond326 ↔ 339 By similarity
Disulfide bond341 ↔ 350 By similarity
Disulfide bond409 ↔ 421 By similarity
Disulfide bond415 ↔ 428 By similarity
Disulfide bond430 ↔ 439 By similarity
Disulfide bond456 ↔ 464 By similarity
Disulfide bond458 ↔ 471 By similarity
Disulfide bond473 ↔ 482 By similarity
Disulfide bond495 ↔ 507 By similarity
Disulfide bond501 ↔ 514 By similarity
Disulfide bond516 ↔ 525 By similarity
Disulfide bond542 ↔ 550 By similarity
Disulfide bond544 ↔ 557 By similarity
Disulfide bond559 ↔ 568 By similarity
Disulfide bond581 ↔ 593 By similarity
Disulfide bond587 ↔ 600 By similarity
Disulfide bond602 ↔ 611 By similarity
Disulfide bond669 ↔ 681 By similarity
Disulfide bond675 ↔ 688 By similarity
Disulfide bond690 ↔ 699 By similarity
Disulfide bond716 ↔ 724 By similarity
Disulfide bond718 ↔ 731 By similarity
Disulfide bond733 ↔ 742 By similarity
Disulfide bond755 ↔ 767 By similarity
Disulfide bond761 ↔ 774 By similarity
Disulfide bond776 ↔ 785 By similarity
Disulfide bond802 ↔ 810 By similarity
Disulfide bond804 ↔ 817 By similarity
Disulfide bond819 ↔ 828 By similarity

Experimental info

Sequence conflict3231A → T in BAE38699. Ref.1
Sequence conflict10921G → S in BAE38699. Ref.1
Sequence conflict11371N → S in BAE38699. Ref.1
Sequence conflict11401S → T in BAE38699. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6DIB5 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: FBC50896096181CC

FASTA1,147122,972
        10         20         30         40         50         60 
MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC 

        70         80         90        100        110        120 
TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SRDMCVPHCA DKCVHGRCIA 

       130        140        150        160        170        180 
PNTCQCEPGW GGTNCSSACD GDHWGPHCSS RCQCKNRALC NPITGACHCA AGYRGWRCED 

       190        200        210        220        230        240 
RCEQGTYGND CHQRCQCQNG ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC 

       250        260        270        280        290        300 
QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP 

       310        320        330        340        350        360 
GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC EARLCPEGLY 

       370        380        390        400        410        420 
GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD 

       430        440        450        460        470        480 
CDSVTGRCAC APGFKGTDCS TPCPLGRYGI NCSSRCGCKN DAVCSPVDGS CICKAGWHGV 

       490        500        510        520        530        540 
DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE 

       550        560        570        580        590        600 
RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC 

       610        620        630        640        650        660 
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC 

       670        680        690        700        710        720 
PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN 

       730        740        750        760        770        780 
GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF 

       790        800        810        820        830        840 
MGRHCEQKCP AGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN 

       850        860        870        880        890        900 
SLSRTSTALP ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR 

       910        920        930        940        950        960 
VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI AKSKNNQLFV 

       970        980        990       1000       1010       1020 
NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSST 

      1030       1040       1050       1060       1070       1080 
CSLSSSENPY ATIKDPPALL PKSSECGYVE MKSPARRDSP YAEINNSTPA NRNVYEVEPT 

      1090       1100       1110       1120       1130       1140 
VSVVQGVFSN SGHVTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS 


SSSSSSE 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"Cooperation between engulfment receptors: the case of ABCA1 and MEGF10."
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., Zhou Z., Chimini G.
PLoS ONE 1:E120-E120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation."
Suzuki E., Nakayama M.
Exp. Cell Res. 313:3729-3742(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Megf10 regulates the progression of the satellite cell myogenic program."
Holterman C.E., Le Grand F., Kuang S., Seale P., Rudnicki M.A.
J. Cell Biol. 179:911-922(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MYOGENESIS, TISSUE SPECIFICITY.
[6]"MEGF10 functions as a receptor for the uptake of amyloid-beta."
Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W., Kim I.S.
FEBS Lett. 584:3936-3942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ENDOCYTOSIS.
[7]"MEGF10 and MEGF11 mediate homotypic interactions required for mosaic spacing of retinal neurons."
Kay J.N., Chu M.W., Sanes J.R.
Nature 483:465-469(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURONAL MOSAIC SPACING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK147238 mRNA. Translation: BAE27788.1.
AK148084 mRNA. Translation: BAE28336.1.
AK166316 mRNA. Translation: BAE38699.1.
BC075647 mRNA. Translation: AAH75647.1.
RefSeqNP_001001979.1. NM_001001979.2.
UniGeneMm.297863.

3D structure databases

ProteinModelPortalQ6DIB5.
SMRQ6DIB5. Positions 90-833.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6DIB5.

Proteomic databases

PaxDbQ6DIB5.
PRIDEQ6DIB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
ENSMUST00000139892; ENSMUSP00000116814; ENSMUSG00000024593.
GeneID70417.
KEGGmmu:70417.
UCSCuc008eyz.2. mouse.

Organism-specific databases

CTD84466.
MGIMGI:2685177. Megf10.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00730000110380.
HOGENOMHOG000294130.
HOVERGENHBG108333.
InParanoidQ6DIB5.
OMAFGCNLTC.
OrthoDBEOG72C50D.
PhylomeDBQ6DIB5.
TreeFamTF332598.

Gene expression databases

BgeeQ6DIB5.
CleanExMM_MEGF10.
GenevestigatorQ6DIB5.

Family and domain databases

InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
[Graphical view]
PfamPF12661. hEGF. 4 hits.
PF00053. Laminin_EGF. 5 hits.
[Graphical view]
SMARTSM00181. EGF. 12 hits.
SM00180. EGF_Lam. 5 hits.
[Graphical view]
PROSITEPS00022. EGF_1. 17 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 15 hits.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMEGF10. mouse.
NextBio331567.
PROQ6DIB5.
SOURCESearch...

Entry information

Entry nameMEG10_MOUSE
AccessionPrimary (citable) accession number: Q6DIB5
Secondary accession number(s): Q3TLU3, Q3UG73
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot