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Multiple epidermal growth factor-like domains protein 11 (Multiple EGF-like domains protein 11)

 MEG11_HUMAN             Reviewed;        1044 AA.
A6BM72; Q17R86; Q6UXS5; Q8ND91; Q96KG6;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 3.
05-DEC-2018, entry version 101.
RecName: Full=Multiple epidermal growth factor-like domains protein 11;
Short=Multiple EGF-like domains protein 11;
Flags: Precursor;
Name=MEGF11; Synonyms=KIAA1781; ORFNames=UNQ1949/PRO4432;
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] (ISOFORMS 1 AND 2), AND
VARIANTS ARG-317 AND PHE-861.
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 4).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ASN-95 AND ARG-317.
TISSUE=Brain;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1044 (ISOFORM 3), AND
VARIANT ARG-317.
TISSUE=Testis;
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).
[6]
SUBCELLULAR LOCATION.
TISSUE=Brain;
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).
-!- FUNCTION: May regulate 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 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homopolymer (Probable). Does not interact with MEGF10.
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17498693};
Single-pass type I membrane protein {ECO:0000269|PubMed:17498693}.
Basolateral cell membrane {ECO:0000269|PubMed:17498693}; Single-
pass type I membrane protein {ECO:0000269|PubMed:17498693}.
Note=Forms an irregular, mosaic-like adhesion pattern in region of
the cell that becomes firmely fixed to the substrate. Localized to
protruding lamellipodia. Does not localize with MEGF10.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=A6BM72-1; Sequence=Displayed;
Name=2;
IsoId=A6BM72-2; Sequence=VSP_029247, VSP_029248;
Name=3;
IsoId=A6BM72-3; Sequence=VSP_029249, VSP_029250;
Name=4;
IsoId=A6BM72-4; Sequence=VSP_029246, VSP_029251, VSP_029252;
-!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB47410.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAD38994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB058677; BAB47410.2; ALT_INIT; mRNA.
EMBL; AB300051; BAF64841.1; -; mRNA.
EMBL; AY358226; AAQ88593.1; -; mRNA.
EMBL; AC011847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC084854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC117419; AAI17420.1; -; mRNA.
EMBL; BC126313; AAI26314.1; -; mRNA.
EMBL; AL834326; CAD38994.1; ALT_INIT; mRNA.
CCDS; CCDS10213.2; -. [A6BM72-1]
RefSeq; NP_115821.2; NM_032445.2. [A6BM72-1]
RefSeq; XP_016878161.1; XM_017022672.1. [A6BM72-1]
UniGene; Hs.712886; -.
ProteinModelPortal; A6BM72; -.
SMR; A6BM72; -.
BioGrid; 124098; 2.
IntAct; A6BM72; 2.
STRING; 9606.ENSP00000386908; -.
iPTMnet; A6BM72; -.
PhosphoSitePlus; A6BM72; -.
BioMuta; MEGF11; -.
PaxDb; A6BM72; -.
PRIDE; A6BM72; -.
ProteomicsDB; 769; -.
ProteomicsDB; 770; -. [A6BM72-2]
ProteomicsDB; 771; -. [A6BM72-3]
ProteomicsDB; 772; -. [A6BM72-4]
TopDownProteomics; A6BM72-3; -. [A6BM72-3]
Ensembl; ENST00000288745; ENSP00000288745; ENSG00000157890. [A6BM72-2]
Ensembl; ENST00000409699; ENSP00000386908; ENSG00000157890. [A6BM72-1]
Ensembl; ENST00000422354; ENSP00000414475; ENSG00000157890. [A6BM72-1]
GeneID; 84465; -.
KEGG; hsa:84465; -.
UCSC; uc002apl.2; human. [A6BM72-1]
CTD; 84465; -.
DisGeNET; 84465; -.
EuPathDB; HostDB:ENSG00000157890.17; -.
GeneCards; MEGF11; -.
H-InvDB; HIX0018384; -.
HGNC; HGNC:29635; MEGF11.
HPA; HPA017982; -.
MIM; 612454; gene.
neXtProt; NX_A6BM72; -.
OpenTargets; ENSG00000157890; -.
PharmGKB; PA144596411; -.
eggNOG; KOG1218; Eukaryota.
eggNOG; ENOG410XQWV; LUCA.
GeneTree; ENSGT00940000155333; -.
HOGENOM; HOG000294130; -.
HOVERGEN; HBG108333; -.
InParanoid; A6BM72; -.
PhylomeDB; A6BM72; -.
TreeFam; TF332598; -.
ChiTaRS; MEGF11; human.
GenomeRNAi; 84465; -.
PRO; PR:A6BM72; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000157890; Expressed in 121 organ(s), highest expression level in cerebellum.
CleanEx; HS_MEGF11; -.
ExpressionAtlas; A6BM72; baseline and differential.
Genevisible; A6BM72; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR011489; EMI_domain.
InterPro; IPR002049; Laminin_EGF.
Pfam; PF12661; hEGF; 3.
Pfam; PF00053; Laminin_EGF; 8.
SMART; SM00181; EGF; 17.
SMART; SM00180; EGF_Lam; 16.
PROSITE; PS00022; EGF_1; 17.
PROSITE; PS01186; EGF_2; 17.
PROSITE; PS50026; EGF_3; 14.
PROSITE; PS51041; EMI; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1044 Multiple epidermal growth factor-like
domains protein 11.
/FTId=PRO_0000309735.
TOPO_DOM 20 848 Extracellular. {ECO:0000255}.
TRANSMEM 849 869 Helical. {ECO:0000255}.
TOPO_DOM 870 1044 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 101 EMI. {ECO:0000255|PROSITE-
ProRule:PRU00384}.
DOMAIN 95 130 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 143 173 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 181 216 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 224 259 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 267 302 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 310 345 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 399 434 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 442 477 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 490 520 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 571 606 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 659 694 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 707 737 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 750 780 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 788 823 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 531 531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 89 {ECO:0000255}.
DISULFID 54 63 {ECO:0000255}.
DISULFID 88 99 {ECO:0000255}.
DISULFID 103 118 {ECO:0000250}.
DISULFID 120 129 {ECO:0000250}.
DISULFID 146 154 {ECO:0000250}.
DISULFID 148 161 {ECO:0000250}.
DISULFID 163 172 {ECO:0000250}.
DISULFID 185 197 {ECO:0000250}.
DISULFID 191 204 {ECO:0000250}.
DISULFID 206 215 {ECO:0000250}.
DISULFID 228 240 {ECO:0000250}.
DISULFID 234 247 {ECO:0000250}.
DISULFID 249 258 {ECO:0000250}.
DISULFID 271 283 {ECO:0000250}.
DISULFID 277 290 {ECO:0000250}.
DISULFID 292 301 {ECO:0000250}.
DISULFID 314 326 {ECO:0000250}.
DISULFID 320 333 {ECO:0000250}.
DISULFID 335 344 {ECO:0000250}.
DISULFID 403 415 {ECO:0000250}.
DISULFID 409 422 {ECO:0000250}.
DISULFID 424 433 {ECO:0000250}.
DISULFID 446 458 {ECO:0000250}.
DISULFID 452 465 {ECO:0000250}.
DISULFID 467 476 {ECO:0000250}.
DISULFID 493 501 {ECO:0000250}.
DISULFID 495 508 {ECO:0000250}.
DISULFID 510 519 {ECO:0000250}.
DISULFID 575 587 {ECO:0000250}.
DISULFID 581 594 {ECO:0000250}.
DISULFID 596 605 {ECO:0000250}.
DISULFID 663 675 {ECO:0000250}.
DISULFID 669 682 {ECO:0000250}.
DISULFID 684 693 {ECO:0000250}.
DISULFID 710 718 {ECO:0000250}.
DISULFID 712 725 {ECO:0000250}.
DISULFID 727 736 {ECO:0000250}.
DISULFID 753 761 {ECO:0000250}.
DISULFID 755 768 {ECO:0000250}.
DISULFID 770 779 {ECO:0000250}.
DISULFID 792 804 {ECO:0000250}.
DISULFID 798 811 {ECO:0000250}.
DISULFID 813 822 {ECO:0000250}.
VAR_SEQ 1 827 Missing (in isoform 4).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_029246.
VAR_SEQ 1 75 Missing (in isoform 2).
{ECO:0000303|PubMed:11347906}.
/FTId=VSP_029247.
VAR_SEQ 76 101 RGLRTMYRRRSQCCPGYYESGDFCIP -> MHTPSIRSITH
DAQTSSTGSSAPGTA (in isoform 2).
{ECO:0000303|PubMed:11347906}.
/FTId=VSP_029248.
VAR_SEQ 740 875 CPAAFFGKDCGRVCQCQNGASCDHISGKCTCRTGFTGQHCE
QRCAPGTFGYGCQQLCECMNNSTCDHVTGTCYCSPGFKGIR
CDQAALMMEELNPYTKISPALGAERHSVGAVTGIMLLLFLI
VVLLGLFAWHRRR -> KPHLLASQPLRIPCCGLLATVGIV
QTSREGGMQAAPGLVVPDSCPTRTEELCRGSSRPDWIQGID
KPKVLEGQGCKAAQQHFLGRTVGAYASVRMAPAVTTSVASA
PAAQASPGNTVSRDVPQEPLAMGVSSYVSA (in
isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_029249.
VAR_SEQ 876 1044 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_029250.
VAR_SEQ 904 964 GACGMDRRQNTYIMDKGFKDYMKESVCSSSTCSLNSSENPY
ATIKDPPILTCKLPESSYVE -> ASTTPWWPVMEHLARPF
SQRPRTQLSNKSLDRDTAGWTPYSYVNVLDQCPGGQVPARG
LLH (in isoform 4).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_029251.
VAR_SEQ 965 1044 Missing (in isoform 4).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_029252.
VARIANT 95 95 S -> N (in dbSNP:rs16949528).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_059261.
VARIANT 242 242 H -> R (in dbSNP:rs333550).
/FTId=VAR_036990.
VARIANT 317 317 H -> R (in dbSNP:rs333550).
{ECO:0000269|PubMed:11347906,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005}.
/FTId=VAR_059262.
VARIANT 474 474 L -> P (in dbSNP:rs35309197).
/FTId=VAR_059263.
VARIANT 861 861 L -> F (in dbSNP:rs3803414).
{ECO:0000269|PubMed:11347906}.
/FTId=VAR_059264.
VARIANT 988 988 I -> T (in dbSNP:rs2303374).
/FTId=VAR_059265.
SEQUENCE 1044 AA; 110844 MW; 8F4CF00B8B1DFCA2 CRC64;
MVLSLTGLIA FSFLQATLAL NPEDPNVCSH WESYAVTVQE SYAHPFDQIY YTRCTDILNW
FKCTRHRISY KTAYRRGLRT MYRRRSQCCP GYYESGDFCI PLCTEECVHG RCVSPDTCHC
EPGWGGPDCS SGCDSDHWGP HCSNRCQCQN GALCNPITGA CVCAAGFRGW RCEELCAPGT
HGKGCQLPCQ CRHGASCDPR AGECLCAPGY TGVYCEELCP PGSHGAHCEL RCPCQNGGTC
HHITGECACP PGWTGAVCAQ PCPPGTFGQN CSQDCPCHHG GQCDHVTGQC HCTAGYMGDR
CQEECPFGSF GFQCSQHCDC HNGGQCSPTT GACECEPGYK GPRCQERLCP EGLHGPGCTL
PCPCDADNTI SCHPVTGACT CQPGWSGHHC NESCPVGYYG DGCQLPCTCQ NGADCHSITG
GCTCAPGFMG EVCAVSCAAG TYGPNCSSIC SCNNGGTCSP VDGSCTCKEG WQGLDCTLPC
PSGTWGLNCN ESCTCANGAA CSPIDGSCSC TPGWLGDTCE LPCPDGTFGL NCSEHCDCSH
ADGCDPVTGH CCCLAGWTGI RCDSTCPPGR WGPNCSVSCS CENGGSCSPE DGSCECAPGF
RGPLCQRICP PGFYGHGCAQ PCPLCVHSSR PCHHISGICE CLPGFSGALC NQVCAGGYFG
QDCAQLCSCA NNGTCSPIDG SCQCFPGWIG KDCSQACPPG FWGPACFHAC SCHNGASCSA
EDGACHCTPG WTGLFCTQRC PAAFFGKDCG RVCQCQNGAS CDHISGKCTC RTGFTGQHCE
QRCAPGTFGY GCQQLCECMN NSTCDHVTGT CYCSPGFKGI RCDQAALMME ELNPYTKISP
ALGAERHSVG AVTGIMLLLF LIVVLLGLFA WHRRRQKEKG RDLAPRVSYT PAMRMTSTDY
SLSGACGMDR RQNTYIMDKG FKDYMKESVC SSSTCSLNSS ENPYATIKDP PILTCKLPES
SYVEMKSPVH MGSPYTDVPS LSTSNKNIYE VEPTVSVVQE GCGHNSSYIQ NAYDLPRNSH
IPGHYDLLPV RQSPANGPSQ DKQS


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