MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10

MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10 » Multiple EGF-like domains protein 10;
Hydrophobic Thickness 37.2 ± 1.8 Å
Tilt Angle 1 ± 0°
ΔGtransfer -61.9 kcal/mol
ΔGfold -32.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC
Topology Out
TM Segments 857-879 (851-884)
Pathways none
PDB none
OPM none
Complexes none
Interactions

T132A, Complex: T132A:MEG10, PubMed

Domains

AA: 113-130, PDBID: 2YGQ, Subunit A, Seq Identity:52%, Human growth factor-like EGF

AA: 152-197, PDBID: 1KLO, Subunit A, Seq Identity:34%, Laminin EGF domain

AA: 197-216, PDBID: 2YGQ, Subunit A, Seq Identity:60%, Human growth factor-like EGF

AA: 240-259, PDBID: 2YGQ, Subunit A, Seq Identity:56%, Human growth factor-like EGF

AA: 281-326, PDBID: 4OVE, Subunit A, Seq Identity:37%, Laminin EGF domain

AA: 364-415, PDBID: 1KLO, Subunit A, Seq Identity:30%, Laminin EGF domain

AA: 415-434, PDBID: 2YGQ, Subunit A, Seq Identity:56%, Human growth factor-like EGF

AA: 501-520, PDBID: 2YGQ, Subunit A, Seq Identity:56%, Human growth factor-like EGF

AA: 587-606, PDBID: 2YGQ, Subunit A, Seq Identity:56%, Human growth factor-like EGF

AA: 718-737, PDBID: 2YGQ, Subunit A, Seq Identity:56%, Human growth factor-like EGF

AA: 759-802, PDBID: 1KLO, Subunit A, Seq Identity:39%, Laminin EGF domain

AA: 798-838, PDBID: 4OVE, Subunit A, Seq Identity:30%, Laminin EGF domain

UniProt annotation for MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10
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.

SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1. Interacts with AP2M1. Does not interact with MEGF11.

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

DISEASE: Myopathy, early-onset, areflexia, respiratory distress, and dysphagia (EMARDD) OMIM: An autosomal recessive congenital myopathy characterized by onset at birth, or early in infancy, of respiratory distress caused by diaphragmatic weakness. Additional features are dysphagia resulting in poor feeding, failure to thrive, poor head control, facial weakness, cleft palate, contractures and scoliosis. Affected individuals become ventilator-dependent, and most require feeding by gastrostomy. The disorder results in severe muscle weakness and most patients never achieve walking. Death from respiratory failure in childhood occurs in about half of patients. Muscle biopsies from affected individuals show myopathic changes, replacement of myofibers with fatty tissue, small and incompletely fused muscle fibers, and variation in fiber size. Short regions of sarcomeric disorganization with few or no mitochondria (minicores) have been observed in some cases. mutations affecting the gene represented in this entry.

UniProt features for MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10
SIGNAL 1 25 Potential.
CHAIN 26 1140 Multiple epidermal growth factor-like domains protein 10.
DOMAIN 30 107 EMI.
DOMAIN 106 136 EGF-like 1.
DOMAIN 144 179 EGF-like 2.
DOMAIN 187 222 EGF-like 3.
DOMAIN 230 265 EGF-like 4.
DOMAIN 278 308 EGF-like 5.
DOMAIN 316 351 EGF-like 6.
DOMAIN 405 440 EGF-like 7.
DOMAIN 453 483 EGF-like 8.
DOMAIN 491 526 EGF-like 9.
DOMAIN 539 569 EGF-like 10.
DOMAIN 577 612 EGF-like 11.
DOMAIN 665 700 EGF-like 12.
DOMAIN 713 743 EGF-like 13.
DOMAIN 751 786 EGF-like 14.
DOMAIN 799 829 EGF-like 15.
REGION 1 857 Necessary for interaction with AP2M1, self-assembly and formation of the irregular, mosaic-like adhesion pattern.
REGION 945 1140 Necessary for formation of large intracellular vacuoles.
DISULFID 34 95 Potential.
DISULFID 60 69 Potential.
DISULFID 94 105 Potential.
DISULFID 109 118 By similarity.
DISULFID 113 124 By similarity.
DISULFID 126 135 By similarity.
DISULFID 148 160 By similarity.
DISULFID 154 167 By similarity.
DISULFID 169 178 By similarity.
DISULFID 191 203 By similarity.
DISULFID 197 210 By similarity.
DISULFID 212 221 By similarity.
DISULFID 234 246 By similarity.
DISULFID 240 253 By similarity.
DISULFID 255 264 By similarity.
DISULFID 281 289 By similarity.
DISULFID 283 296 By similarity.
DISULFID 298 307 By similarity.
DISULFID 320 332 By similarity.
DISULFID 326 339 By similarity.
DISULFID 341 350 By similarity.
DISULFID 409 421 By similarity.
DISULFID 415 428 By similarity.
DISULFID 430 439 By similarity.
DISULFID 456 464 By similarity.
DISULFID 458 471 By similarity.
DISULFID 473 482 By similarity.
DISULFID 495 507 By similarity.
DISULFID 501 514 By similarity.
DISULFID 516 525 By similarity.
DISULFID 542 550 By similarity.
DISULFID 544 557 By similarity.
DISULFID 559 568 By similarity.
DISULFID 581 593 By similarity.
DISULFID 587 600 By similarity.
DISULFID 602 611 By similarity.
DISULFID 669 681 By similarity.
DISULFID 675 688 By similarity.
DISULFID 690 699 By similarity.
DISULFID 716 724 By similarity.
DISULFID 718 731 By similarity.
DISULFID 733 742 By similarity.
DISULFID 755 767 By similarity.
DISULFID 761 774 By similarity.
DISULFID 776 785 By similarity.
DISULFID 802 810 By similarity.
DISULFID 804 817 By similarity.
DISULFID 819 828 By similarity.
Amino Acid Sequence for MEG10_HUMAN » Multiple epidermal growth factor-like domains protein 10
MVISLNSCLS FICLLLCHWI GTASPLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC TDILNWFKCT RHRVSYRTAY RHGEKTMYRR KSQCCPGFYE SGEMCVPHCA DKCVHGRCIA PNTCQCEPGW GGTNCSSACD GDHWGPHCTS RCQCKNGALC NPITGACHCA AGFRGWRCED RCEQGTYGND CHQRCQCQNG ATCDHVTGEC RCPPGYTGAF CEDLCPPGKH GPQCEQRCPC QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP GYTGERCQDE CPVGTYGVLC AETCQCVNGG KCYHVSGACL CEAGFAGERC EARLCPEGLY GIKCDKRCPC HLENTHSCHP MSGECACKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD CDSVTGKCTC APGFKGIDCS TPCPLGTYGI NCSSRCGCKN DAVCSPVDGS CTCKAGWHGV DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGEKCELPCQ DGTYGLNCAE RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC PSGRFGKNCA GICTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF MGRHCEQKCP SGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN SLSRTSTALP ADSYQIGAIA GIIILVLVVL FLLALFIIYR HKQKGKESSM PAVTYTPAMR VVNADYTISG TLPHSNGGNA NSHYFTNPSY HTLTQCATSP HVNNRDRMTV TKSKNNQLFV NLKNVNPGKR GPVGDCTGTL PADWKHGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSSN CSLSSSENPY ATIKDPPVLI PKSSECGYVE MKSPARRDSP YAEINNSTSA NRNVYEVEPT VSVVQGVFSN NGRLSQDPYD LPKNSHIPCH YDLLPVRDSS SSPKQEDSGG SSSNSSSSSE