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Q6DIB5

- MEG10_MOUSE

UniProt

Q6DIB5 - MEG10_MOUSE

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Protein

Multiple epidermal growth factor-like domains protein 10

Gene

Megf10

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

Functioni

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.3 Publications

GO - Biological processi

  1. homotypic cell-cell adhesion Source: UniProtKB
  2. muscle cell development Source: UniProtKB
  3. recognition of apoptotic cell Source: MGI
  4. regulation of muscle cell differentiation Source: UniProtKB
  5. regulation of skeletal muscle tissue development Source: Ensembl
  6. skeletal muscle satellite cell activation Source: UniProtKB
  7. skeletal muscle satellite cell differentiation Source: UniProtKB
  8. skeletal muscle satellite cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Myogenesis, Phagocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple epidermal growth factor-like domains protein 10
Short name:
Multiple EGF-like domains protein 10
Gene namesi
Name:Megf10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:2685177. Megf10.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Basolateral cell membrane By similarity; 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.By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. phagocytic cup Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 11471122Multiple epidermal growth factor-like domains protein 10PRO_0000309733Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 95Sequence Analysis
Disulfide bondi60 ↔ 69Sequence Analysis
Disulfide bondi94 ↔ 105Sequence Analysis
Disulfide bondi109 ↔ 124By similarity
Disulfide bondi126 ↔ 135By similarity
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis
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

Post-translational modificationi

Phosphorylated on tyrosine residues.By similarity
Ubiquitinated; mono- and polyubiquitinated forms are detected.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ6DIB5.
PaxDbiQ6DIB5.
PRIDEiQ6DIB5.

PTM databases

PhosphoSiteiQ6DIB5.

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

BgeeiQ6DIB5.
CleanExiMM_MEGF10.
ExpressionAtlasiQ6DIB5. baseline and differential.
GenevestigatoriQ6DIB5.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ6DIB5.
SMRiQ6DIB5. Positions 91-833.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 857832ExtracellularSequence AnalysisAdd
BLAST
Topological domaini879 – 1147269CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei858 – 87821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10778EMIPROSITE-ProRule annotationAdd
BLAST
Domaini101 – 13636EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 17936EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 22236EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini230 – 26536EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini278 – 30831EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini316 – 35136EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 44036EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini453 – 48331EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 52636EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini539 – 56931EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini577 – 61236EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini665 – 70036EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini713 – 74331EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini751 – 78636EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini799 – 82931EGF-like 15PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 857857Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion patternBy similarityAdd
BLAST
Regioni945 – 1147203Necessary for formation of large intracellular vacuolesBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1119 – 114628Ser-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the MEGF family.Curated
Contains 15 EGF-like domains.PROSITE-ProRule annotation
Contains 1 EMI domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000110380.
HOGENOMiHOG000294130.
HOVERGENiHBG108333.
InParanoidiQ6DIB5.
OMAiFGCNLTC.
OrthoDBiEOG72C50D.
PhylomeDBiQ6DIB5.
TreeFamiTF332598.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
[Graphical view]
PfamiPF12661. hEGF. 4 hits.
PF00053. Laminin_EGF. 5 hits.
[Graphical view]
SMARTiSM00181. EGF. 12 hits.
SM00180. EGF_Lam. 5 hits.
[Graphical view]
PROSITEiPS00022. EGF_1. 17 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 15 hits.
PS51041. EMI. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti323 – 3231A → T in BAE38699. (PubMed:16141072)Curated
Sequence conflicti1092 – 10921G → S in BAE38699. (PubMed:16141072)Curated
Sequence conflicti1137 – 11371N → S in BAE38699. (PubMed:16141072)Curated
Sequence conflicti1140 – 11401S → T in BAE38699. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENSMUST00000139892; ENSMUSP00000116814; ENSMUSG00000024593.
GeneIDi70417.
KEGGimmu:70417.
UCSCiuc008eyz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK147238 mRNA. Translation: BAE27788.1 .
AK148084 mRNA. Translation: BAE28336.1 .
AK166316 mRNA. Translation: BAE38699.1 .
BC075647 mRNA. Translation: AAH75647.1 .
CCDSi CCDS29264.1.
RefSeqi NP_001001979.1. NM_001001979.2.
UniGenei Mm.297863.

3D structure databases

ProteinModelPortali Q6DIB5.
SMRi Q6DIB5. Positions 91-833.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q6DIB5.

Proteomic databases

MaxQBi Q6DIB5.
PaxDbi Q6DIB5.
PRIDEi Q6DIB5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075770 ; ENSMUSP00000075174 ; ENSMUSG00000024593 .
ENSMUST00000139892 ; ENSMUSP00000116814 ; ENSMUSG00000024593 .
GeneIDi 70417.
KEGGi mmu:70417.
UCSCi uc008eyz.2. mouse.

Organism-specific databases

CTDi 84466.
MGIi MGI:2685177. Megf10.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110380.
HOGENOMi HOG000294130.
HOVERGENi HBG108333.
InParanoidi Q6DIB5.
OMAi FGCNLTC.
OrthoDBi EOG72C50D.
PhylomeDBi Q6DIB5.
TreeFami TF332598.

Miscellaneous databases

ChiTaRSi MEGF10. mouse.
NextBioi 331567.
PROi Q6DIB5.
SOURCEi Search...

Gene expression databases

Bgeei Q6DIB5.
CleanExi MM_MEGF10.
ExpressionAtlasi Q6DIB5. baseline and differential.
Genevestigatori Q6DIB5.

Family and domain databases

InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR011489. EMI_domain.
[Graphical view ]
Pfami PF12661. hEGF. 4 hits.
PF00053. Laminin_EGF. 5 hits.
[Graphical view ]
SMARTi SM00181. EGF. 12 hits.
SM00180. EGF_Lam. 5 hits.
[Graphical view ]
PROSITEi PS00022. EGF_1. 17 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 15 hits.
PS51041. EMI. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMEG10_MOUSE
AccessioniPrimary (citable) accession number: Q6DIB5
Secondary accession number(s): Q3TLU3, Q3UG73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: August 16, 2004
Last modified: October 29, 2014
This is version 103 of the entry and version 1 of the sequence. [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

External Data

Dasty 3