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Multiple epidermal growth factor-like domains protein 10 (Multiple EGF-like domains protein 10)

 MEG10_HUMAN             Reviewed;        1140 AA.
Q96KG7; Q68DE5; Q8WUL3;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 127.
RecName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000312|HGNC:HGNC:29634};
Short=Multiple EGF-like domains protein 10 {ECO:0000305};
Flags: Precursor;
Name=MEGF10 {ECO:0000312|HGNC:HGNC:29634}; Synonyms=KIAA1780;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH GULP1 AND ABCA1, MUTAGENESIS OF ASN-927 AND TYR-930,
AND SUBCELLULAR LOCATION.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and
MEGF10.";
PLoS ONE 1:E120-E120(2006).
[6]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17498693; DOI=10.1016/j.yexcr.2007.03.041;
Suzuki E., Nakayama M.;
"The mammalian Ced-1 ortholog MEGF10/KIAA1780 displays a novel
adhesion pattern.";
Exp. Cell Res. 313:2451-2464(2007).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AP2M1
AND GULP1, PHOSPHORYLATION, AND UBIQUITINATION.
PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
Suzuki E., Nakayama M.;
"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
assembly protein complex 2 medium chain and induces large vacuole
formation.";
Exp. Cell Res. 313:3729-3742(2007).
[8]
FUNCTION IN ENDOCYTOSIS.
PubMed=20828568; DOI=10.1016/j.febslet.2010.08.050;
Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W.,
Kim I.S.;
"MEGF10 functions as a receptor for the uptake of amyloid-beta.";
FEBS Lett. 584:3936-3942(2010).
[9]
FUNCTION IN MYOGENESIS, AND VARIANT EMARDD ARG-774.
PubMed=22101682; DOI=10.1038/ng.995;
Logan C.V., Lucke B., Pottinger C., Abdelhamed Z.A., Parry D.A.,
Szymanska K., Diggle C.P., Riesen A., Morgan J.E., Markham G.,
Ellis I., Manzur A.Y., Markham A.F., Shires M., Helliwell T.,
Scoto M., Hubner C., Bonthron D.T., Taylor G.R., Sheridan E.,
Muntoni F., Carr I.M., Schuelke M., Johnson C.A.;
"Mutations in MEGF10, a regulator of satellite cell myogenesis, cause
early onset myopathy, areflexia, respiratory distress and dysphagia
(EMARDD).";
Nat. Genet. 43:1189-1192(2011).
[10]
VARIANTS EMARDD TRP-71; ARG-326 AND ARG-774.
PubMed=22371254; DOI=10.1007/s10048-012-0315-z;
Boyden S.E., Mahoney L.J., Kawahara G., Myers J.A., Mitsuhashi S.,
Estrella E.A., Duncan A.R., Dey F., Dechene E.T.,
Blasko-Goehringer J.M., Bonnemann C.G., Darras B.T., Mendell J.R.,
Lidov H.G., Nishino I., Beggs A.H., Kunkel L.M., Kang P.B.;
"Mutations in the satellite cell gene MEGF10 cause a recessive
congenital myopathy with minicores.";
Neurogenetics 13:115-124(2012).
[11]
CHARACTERIZATION OF VARIANTS EMARDD ARG-326 AND ARG-774, MUTAGENESIS
OF TYR-1030, AND PHOSPHORYLATION AT TYR-1030.
PubMed=23954233; DOI=10.1016/j.febslet.2013.08.002;
Mitsuhashi S., Mitsuhashi H., Alexander M.S., Sugimoto H., Kang P.B.;
"Cysteine mutations cause defective tyrosine phosphorylation in MEGF10
myopathy.";
FEBS Lett. 587:2952-2957(2013).
[12]
CHARACTERIZATION OF VARIANTS EMARDD ARG-326 AND ARG-774, FUNCTION,
INTERACTION WITH COMPLEMENT C1Q, AND SUBCELLULAR LOCATION.
PubMed=27170117; DOI=10.1523/JNEUROSCI.3850-15.2016;
Iram T., Ramirez-Ortiz Z., Byrne M.H., Coleman U.A., Kingery N.D.,
Means T.K., Frenkel D., El Khoury J.;
"Megf10 Is a Receptor for C1Q That Mediates Clearance of Apoptotic
Cells by Astrocytes.";
J. Neurosci. 36:5185-5192(2016).
[13]
CHARACTERIZATION OF VARIANTS EMARDD ARG-326 AND ARG-774, FUNCTION, AND
INTERACTION WITH NOTCH1.
PubMed=28498977; DOI=10.1093/hmg/ddx189;
Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
Cho K.A., Pacak C.A., Draper I., Kang P.B.;
"Consequences of MEGF10 deficiency on myoblast function and Notch1
interactions.";
Hum. Mol. Genet. 26:2984-3000(2017).
-!- FUNCTION: 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. Promotes the formation of
large intracellular vacuoles and may be responsible for the uptake
of amyloid-beta peptides (PubMed:20828568, PubMed:17643423).
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:17498693, PubMed:17643423, PubMed:20828568,
PubMed:22101682, PubMed:27170117, PubMed:28498977).
{ECO:0000269|PubMed:17205124, ECO:0000269|PubMed:17498693,
ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:20828568,
ECO:0000269|PubMed:22101682, ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
-!- SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1.
Interacts with AP2M1 (PubMed:17643423). Does not interact with
MEGF11 (PubMed:17498693). Binds with high affinity to complement
C1q (PubMed:27170117). Interacts (via the cytoplasmic domain) with
NOTCH1 (via NICD domain) (PubMed:28498977).
{ECO:0000269|PubMed:17205124, ECO:0000269|PubMed:17498693,
ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27170117};
Single-pass type I membrane protein. Cell projection, phagocytic
cup {ECO:0000269|PubMed:17205124}. Note=Enriched at the sites of
contact with apoptotic thymocyte cells (PubMed:17205124). 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
(PubMed:17498693). Colocalizes with ABCA1 in absence of any
phagocytic challenge (PubMed:17205124). Does not localize within
lamellipodia (PubMed:17498693). Does not localize with MEGF11
(PubMed:17498693). {ECO:0000269|PubMed:17205124,
ECO:0000269|PubMed:17498693}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96KG7-1; Sequence=Displayed;
Name=2;
IsoId=Q96KG7-2; Sequence=VSP_029244, VSP_029245;
Note=No experimental confirmation available.;
-!- DOMAIN: The EMI and EGF-like domains work in concert to promote
self-assembly.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-
1030 may be important for muscle cell proliferation.
{ECO:0000269|PubMed:17643423, ECO:0000269|PubMed:23954233}.
-!- PTM: Ubiquitinated; mono- and polyubiquitinated forms are
detected. {ECO:0000269|PubMed:17643423}.
-!- DISEASE: Myopathy, early-onset, areflexia, respiratory distress,
and dysphagia (EMARDD) [MIM:614399]: 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. {ECO:0000269|PubMed:22101682,
ECO:0000269|PubMed:22371254, ECO:0000269|PubMed:23954233,
ECO:0000269|PubMed:27170117, ECO:0000269|PubMed:28498977}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB47409.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB058676; BAB47409.2; ALT_INIT; mRNA.
EMBL; CR749437; CAH18275.1; -; mRNA.
EMBL; CH471062; EAW62406.1; -; Genomic_DNA.
EMBL; BC020198; AAH20198.1; -; mRNA.
EMBL; BC152478; AAI52479.1; -; mRNA.
CCDS; CCDS4142.1; -. [Q96KG7-1]
CCDS; CCDS78055.1; -. [Q96KG7-2]
RefSeq; NP_001243474.1; NM_001256545.1. [Q96KG7-1]
RefSeq; NP_001295048.1; NM_001308119.1. [Q96KG7-2]
RefSeq; NP_001295050.1; NM_001308121.1. [Q96KG7-2]
RefSeq; NP_115822.1; NM_032446.2. [Q96KG7-1]
RefSeq; XP_011541996.1; XM_011543694.1. [Q96KG7-1]
UniGene; Hs.438709; -.
ProteinModelPortal; Q96KG7; -.
SMR; Q96KG7; -.
BioGrid; 124099; 6.
IntAct; Q96KG7; 24.
STRING; 9606.ENSP00000274473; -.
iPTMnet; Q96KG7; -.
PhosphoSitePlus; Q96KG7; -.
BioMuta; MEGF10; -.
DMDM; 74716908; -.
EPD; Q96KG7; -.
PaxDb; Q96KG7; -.
PeptideAtlas; Q96KG7; -.
PRIDE; Q96KG7; -.
Ensembl; ENST00000274473; ENSP00000274473; ENSG00000145794. [Q96KG7-1]
Ensembl; ENST00000418761; ENSP00000416284; ENSG00000145794. [Q96KG7-2]
Ensembl; ENST00000503335; ENSP00000423354; ENSG00000145794. [Q96KG7-1]
Ensembl; ENST00000508365; ENSP00000423195; ENSG00000145794. [Q96KG7-2]
GeneID; 84466; -.
KEGG; hsa:84466; -.
UCSC; uc003kuh.5; human. [Q96KG7-1]
CTD; 84466; -.
DisGeNET; 84466; -.
EuPathDB; HostDB:ENSG00000145794.16; -.
GeneCards; MEGF10; -.
HGNC; HGNC:29634; MEGF10.
MalaCards; MEGF10; -.
MIM; 612453; gene.
MIM; 614399; phenotype.
neXtProt; NX_Q96KG7; -.
OpenTargets; ENSG00000145794; -.
Orphanet; 98920; Spinal muscular atrophy with respiratory distress type 1.
PharmGKB; PA144596410; -.
eggNOG; KOG1218; Eukaryota.
eggNOG; ENOG410XQWV; LUCA.
GeneTree; ENSGT00730000110380; -.
HOGENOM; HOG000294130; -.
HOVERGEN; HBG108333; -.
InParanoid; Q96KG7; -.
OMA; FGCNLTC; -.
OrthoDB; EOG091G00XN; -.
PhylomeDB; Q96KG7; -.
TreeFam; TF332598; -.
GeneWiki; MEGF10; -.
GenomeRNAi; 84466; -.
PRO; PR:Q96KG7; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145794; -.
CleanEx; HS_MEGF10; -.
Genevisible; Q96KG7; HS.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001849; F:complement component C1q binding; IDA:MGI.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; IDA:MGI.
GO; GO:1902742; P:apoptotic process involved in development; ISS:UniProtKB.
GO; GO:0043652; P:engulfment of apoptotic cell; ISS:UniProtKB.
GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
GO; GO:0055001; P:muscle cell development; IMP:UniProtKB.
GO; GO:0033002; P:muscle cell proliferation; IMP:UniProtKB.
GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
GO; GO:0051147; P:regulation of muscle cell differentiation; IMP:UniProtKB.
GO; GO:0048641; P:regulation of skeletal muscle tissue development; IMP:UniProtKB.
GO; GO:0014719; P:skeletal muscle satellite cell activation; ISS:UniProtKB.
GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:UniProtKB.
GO; GO:0014841; P:skeletal muscle satellite cell proliferation; ISS:UniProtKB.
Gene3D; 1.20.5.100; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR011489; EMI_domain.
InterPro; IPR002049; Laminin_EGF.
Pfam; PF12661; hEGF; 7.
Pfam; PF00053; Laminin_EGF; 5.
SMART; SM00181; EGF; 17.
SMART; SM00180; EGF_Lam; 14.
PROSITE; PS00022; EGF_1; 17.
PROSITE; PS01186; EGF_2; 17.
PROSITE; PS50026; EGF_3; 15.
PROSITE; PS51041; EMI; 1.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
Complete proteome; Disease mutation; Disulfide bond; EGF-like domain;
Glycoprotein; Membrane; Myogenesis; Phagocytosis; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 1140 Multiple epidermal growth factor-like
domains protein 10.
/FTId=PRO_0000309732.
TOPO_DOM 26 857 Extracellular. {ECO:0000255}.
TRANSMEM 858 878 Helical. {ECO:0000255}.
TOPO_DOM 879 1140 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 107 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 106 136 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 144 179 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 187 222 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 230 265 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 278 308 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 316 351 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 405 440 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 453 483 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 491 526 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 539 569 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 577 612 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 665 700 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 713 743 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 751 786 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 799 829 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 1 857 Necessary for interaction with AP2M1,
self-assembly and formation of the
irregular, mosaic-like adhesion pattern.
{ECO:0000269|PubMed:17643423}.
REGION 945 1140 Necessary for formation of large
intracellular vacuoles.
COMPBIAS 1119 1139 Ser-rich.
MOD_RES 1030 1030 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:23954233}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 95 {ECO:0000255}.
DISULFID 60 69 {ECO:0000255}.
DISULFID 94 105 {ECO:0000255}.
DISULFID 109 118 {ECO:0000250}.
DISULFID 113 124 {ECO:0000250}.
DISULFID 126 135 {ECO:0000250}.
DISULFID 148 160 {ECO:0000250}.
DISULFID 154 167 {ECO:0000250}.
DISULFID 169 178 {ECO:0000250}.
DISULFID 191 203 {ECO:0000250}.
DISULFID 197 210 {ECO:0000250}.
DISULFID 212 221 {ECO:0000250}.
DISULFID 234 246 {ECO:0000250}.
DISULFID 240 253 {ECO:0000250}.
DISULFID 255 264 {ECO:0000250}.
DISULFID 281 289 {ECO:0000250}.
DISULFID 283 296 {ECO:0000250}.
DISULFID 298 307 {ECO:0000250}.
DISULFID 320 332 {ECO:0000250}.
DISULFID 326 339 {ECO:0000250}.
DISULFID 341 350 {ECO:0000250}.
DISULFID 409 421 {ECO:0000250}.
DISULFID 415 428 {ECO:0000250}.
DISULFID 430 439 {ECO:0000250}.
DISULFID 456 464 {ECO:0000250}.
DISULFID 458 471 {ECO:0000250}.
DISULFID 473 482 {ECO:0000250}.
DISULFID 495 507 {ECO:0000250}.
DISULFID 501 514 {ECO:0000250}.
DISULFID 516 525 {ECO:0000250}.
DISULFID 542 550 {ECO:0000250}.
DISULFID 544 557 {ECO:0000250}.
DISULFID 559 568 {ECO:0000250}.
DISULFID 581 593 {ECO:0000250}.
DISULFID 587 600 {ECO:0000250}.
DISULFID 602 611 {ECO:0000250}.
DISULFID 669 681 {ECO:0000250}.
DISULFID 675 688 {ECO:0000250}.
DISULFID 690 699 {ECO:0000250}.
DISULFID 716 724 {ECO:0000250}.
DISULFID 718 731 {ECO:0000250}.
DISULFID 733 742 {ECO:0000250}.
DISULFID 755 767 {ECO:0000250}.
DISULFID 761 774 {ECO:0000250}.
DISULFID 776 785 {ECO:0000250}.
DISULFID 802 810 {ECO:0000250}.
DISULFID 804 817 {ECO:0000250}.
DISULFID 819 828 {ECO:0000250}.
VAR_SEQ 566 567 VH -> LF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029244.
VAR_SEQ 568 1140 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_029245.
VARIANT 71 71 R -> W (in EMARDD; unknown pathological
significance; dbSNP:rs387907074).
{ECO:0000269|PubMed:22371254}.
/FTId=VAR_067469.
VARIANT 206 206 V -> I (in dbSNP:rs3812054).
/FTId=VAR_036988.
VARIANT 326 326 C -> R (in EMARDD; slightly decreased
tyrosine phosphorylation; slightly
reduced apoptotic cell engulfement by
astrocytes; no effect on cell membrane
location; no effect on binding to C1q; no
effect on myoblasts migration and
proliferation; no effect on interaction
with NOTCH1; dbSNP:rs387907073).
{ECO:0000269|PubMed:22371254,
ECO:0000269|PubMed:23954233,
ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
/FTId=VAR_067470.
VARIANT 774 774 C -> R (in EMARDD; impairs tyrosine
phosphorylation; no effect on cell
membrane location; impairs binding to
C1q; reduced apoptotic cell engulfement
by astrocytes by 50%; reduced myoblast
migration and proliferation; decreased
interaction with NOTCH1; no effect on
NOTCH1 nuclear location;
dbSNP:rs387907072).
{ECO:0000269|PubMed:22101682,
ECO:0000269|PubMed:22371254,
ECO:0000269|PubMed:23954233,
ECO:0000269|PubMed:27170117,
ECO:0000269|PubMed:28498977}.
/FTId=VAR_067471.
VARIANT 897 897 P -> L (in dbSNP:rs13183625).
/FTId=VAR_046377.
VARIANT 1072 1072 R -> K (in dbSNP:rs17164935).
/FTId=VAR_036989.
MUTAGEN 927 927 N->A: Does not interact with GULP1; when
associated with A-930.
{ECO:0000269|PubMed:17205124}.
MUTAGEN 930 930 Y->A: Does not interact with GULP1; when
associated with A-927.
{ECO:0000269|PubMed:17205124}.
MUTAGEN 1030 1030 Y->D: Enhances cell proliferation.
{ECO:0000269|PubMed:23954233}.
MUTAGEN 1030 1030 Y->F: Abolishes tyrosine phosphorylation.
Unable to enhance cell proliferation.
{ECO:0000269|PubMed:23954233}.
CONFLICT 543 543 D -> G (in Ref. 2; CAH18275).
{ECO:0000305}.
SEQUENCE 1140 AA; 122205 MW; 45B2FA239423895A CRC64;
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


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