ID MEG11_MOUSE Reviewed; 1091 AA.
AC Q80T91; Q3TV46; Q8BKK7; Q8BX64;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 11;
DE Short=Multiple EGF-like domains protein 11;
DE Flags: Precursor;
GN Name=Megf11; Synonyms=Kiaa1781;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 634-1091 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION IN NEURONAL MOSAIC SPACING.
RX PubMed=22407321; DOI=10.1038/nature10877;
RA Kay J.N., Chu M.W., Sanes J.R.;
RT "MEGF10 and MEGF11 mediate homotypic interactions required for mosaic
RT spacing of retinal neurons.";
RL Nature 483:465-469(2012).
CC -!- FUNCTION: May regulate the mosaic spacing of specific neuron subtypes
CC in the retina through homotypic retinal neuron repulsion. Mosaics
CC provide a mechanism to distribute each cell type evenly across the
CC retina, ensuring that all parts of the visual field have access to a
CC full set of processing elements. {ECO:0000269|PubMed:22407321}.
CC -!- SUBUNIT: Homomer. Does not interact with MEGF10. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Basolateral cell membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Forms an irregular, mosaic-like adhesion pattern in region of the
CC cell that becomes firmely fixed to the substrate. Localized to
CC protruding lamellipodia. Does not localize with MEGF10 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80T91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80T91-2; Sequence=VSP_029253, VSP_029255, VSP_029257,
CC VSP_029258;
CC Name=3;
CC IsoId=Q80T91-3; Sequence=VSP_029254;
CC Name=4;
CC IsoId=Q80T91-4; Sequence=VSP_029256, VSP_029259;
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65837.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122555; BAC65837.2; ALT_INIT; mRNA.
DR EMBL; AK048840; BAC33471.1; -; mRNA.
DR EMBL; AK051642; BAC34702.1; -; mRNA.
DR EMBL; AK160406; BAE35774.1; -; mRNA.
DR CCDS; CCDS23281.1; -. [Q80T91-2]
DR RefSeq; NP_001127871.1; NM_001134399.1.
DR RefSeq; NP_766110.3; NM_172522.4. [Q80T91-2]
DR RefSeq; XP_006511052.1; XM_006510989.1.
DR AlphaFoldDB; Q80T91; -.
DR SMR; Q80T91; -.
DR STRING; 10090.ENSMUSP00000128672; -.
DR GlyCosmos; Q80T91; 2 sites, No reported glycans.
DR GlyGen; Q80T91; 2 sites.
DR iPTMnet; Q80T91; -.
DR PhosphoSitePlus; Q80T91; -.
DR ProteomicsDB; 292293; -. [Q80T91-1]
DR ProteomicsDB; 292294; -. [Q80T91-2]
DR ProteomicsDB; 292295; -. [Q80T91-3]
DR ProteomicsDB; 292296; -. [Q80T91-4]
DR Antibodypedia; 42885; 77 antibodies from 14 providers.
DR DNASU; 214058; -.
DR Ensembl; ENSMUST00000068967.11; ENSMUSP00000065353.5; ENSMUSG00000036466.18. [Q80T91-1]
DR Ensembl; ENSMUST00000093829.9; ENSMUSP00000091349.3; ENSMUSG00000036466.18. [Q80T91-2]
DR Ensembl; ENSMUST00000118485.8; ENSMUSP00000114035.2; ENSMUSG00000036466.18. [Q80T91-4]
DR GeneID; 214058; -.
DR KEGG; mmu:214058; -.
DR UCSC; uc009qby.2; mouse. [Q80T91-3]
DR UCSC; uc009qbz.2; mouse. [Q80T91-2]
DR UCSC; uc009qca.2; mouse. [Q80T91-1]
DR AGR; MGI:1920951; -.
DR CTD; 84465; -.
DR MGI; MGI:1920951; Megf11.
DR VEuPathDB; HostDB:ENSMUSG00000036466; -.
DR GeneTree; ENSGT00940000155333; -.
DR HOGENOM; CLU_008281_0_0_1; -.
DR InParanoid; Q80T91; -.
DR OMA; PACNINC; -.
DR OrthoDB; 2540323at2759; -.
DR PhylomeDB; Q80T91; -.
DR TreeFam; TF332598; -.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 214058; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Megf11; mouse.
DR PRO; PR:Q80T91; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80T91; Protein.
DR Bgee; ENSMUSG00000036466; Expressed in cerebellum lobe and 138 other cell types or tissues.
DR ExpressionAtlas; Q80T91; baseline and differential.
DR Genevisible; Q80T91; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; IMP:UniProtKB.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 4.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF7; MULTIPLE EGF LIKE DOMAINS 11; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF12661; hEGF; 4.
DR Pfam; PF00053; Laminin_EGF; 8.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 16.
DR PROSITE; PS00022; EGF_1; 17.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1091
FT /note="Multiple epidermal growth factor-like domains
FT protein 11"
FT /id="PRO_0000309736"
FT TOPO_DOM 19..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..1091
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..100
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 94..129
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 142..172
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 180..215
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 223..258
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 266..301
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 314..344
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 398..433
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 441..476
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 484..519
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 570..605
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 613..650
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 658..693
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 706..736
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 749..779
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 787..822
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..88
FT /evidence="ECO:0000255"
FT DISULFID 53..62
FT /evidence="ECO:0000255"
FT DISULFID 87..98
FT /evidence="ECO:0000255"
FT DISULFID 102..117
FT /evidence="ECO:0000250"
FT DISULFID 119..128
FT /evidence="ECO:0000250"
FT DISULFID 145..153
FT /evidence="ECO:0000250"
FT DISULFID 147..160
FT /evidence="ECO:0000250"
FT DISULFID 162..171
FT /evidence="ECO:0000250"
FT DISULFID 184..196
FT /evidence="ECO:0000250"
FT DISULFID 190..203
FT /evidence="ECO:0000250"
FT DISULFID 205..214
FT /evidence="ECO:0000250"
FT DISULFID 227..239
FT /evidence="ECO:0000250"
FT DISULFID 233..246
FT /evidence="ECO:0000250"
FT DISULFID 248..257
FT /evidence="ECO:0000250"
FT DISULFID 270..282
FT /evidence="ECO:0000250"
FT DISULFID 276..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT DISULFID 317..325
FT /evidence="ECO:0000250"
FT DISULFID 319..332
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 402..414
FT /evidence="ECO:0000250"
FT DISULFID 408..421
FT /evidence="ECO:0000250"
FT DISULFID 423..432
FT /evidence="ECO:0000250"
FT DISULFID 445..457
FT /evidence="ECO:0000250"
FT DISULFID 451..464
FT /evidence="ECO:0000250"
FT DISULFID 466..475
FT /evidence="ECO:0000250"
FT DISULFID 488..500
FT /evidence="ECO:0000250"
FT DISULFID 494..507
FT /evidence="ECO:0000250"
FT DISULFID 509..518
FT /evidence="ECO:0000250"
FT DISULFID 574..586
FT /evidence="ECO:0000250"
FT DISULFID 580..593
FT /evidence="ECO:0000250"
FT DISULFID 595..604
FT /evidence="ECO:0000250"
FT DISULFID 617..631
FT /evidence="ECO:0000250"
FT DISULFID 621..638
FT /evidence="ECO:0000250"
FT DISULFID 640..649
FT /evidence="ECO:0000250"
FT DISULFID 662..674
FT /evidence="ECO:0000250"
FT DISULFID 668..681
FT /evidence="ECO:0000250"
FT DISULFID 683..692
FT /evidence="ECO:0000250"
FT DISULFID 709..717
FT /evidence="ECO:0000250"
FT DISULFID 711..724
FT /evidence="ECO:0000250"
FT DISULFID 726..735
FT /evidence="ECO:0000250"
FT DISULFID 752..760
FT /evidence="ECO:0000250"
FT DISULFID 754..767
FT /evidence="ECO:0000250"
FT DISULFID 769..778
FT /evidence="ECO:0000250"
FT DISULFID 791..803
FT /evidence="ECO:0000250"
FT DISULFID 797..810
FT /evidence="ECO:0000250"
FT DISULFID 812..821
FT /evidence="ECO:0000250"
FT VAR_SEQ 100..131
FT /note="PLCTEECMHGRCVSPDTCHCEPGWGGPDCSSG -> R (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029253"
FT VAR_SEQ 300..1091
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029254"
FT VAR_SEQ 695..738
FT /note="ACPSGFWGSACFHTCSCHNGASCSAEDGACHCTPGWTGLFCTQR -> G
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029255"
FT VAR_SEQ 903..998
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029256"
FT VAR_SEQ 1018..1021
FT /note="DYMK -> VAPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029257"
FT VAR_SEQ 1022..1091
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029258"
FT VAR_SEQ 1087..1091
FT /note="GRCLT -> EPTVSVVQEGRGHNSSYIQNPYDLPKNSHIPGHYDLLPVRQSP
FT AHGPFQEKQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029259"
FT CONFLICT 815
FT /note="G -> E (in Ref. 2; BAE35774)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="Y -> C (in Ref. 2; BAE35774)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 116059 MW; EE9D70D73CED0477 CRC64;
MAPSAVGLLV FLLQAALALN PEDPNVCSHW ESYAVTVQES YAHPFDQIYY TRCADILNWF
KCTRHRISYK TAYRRGLRTM YRRRSQCCPG YYENGDFCIP LCTEECMHGR CVSPDTCHCE
PGWGGPDCSS GCDSEHWGPH CSNRCQCQNG ALCNPITGAC VCAPGFRGWR CEELCAPGTH
GKGCQLLCQC HHGASCDPRT GECLCAPGYT GVYCEELCPP GSHGAHCELR CPCQNGGTCH
HITGECACPP GWTGAVCAQP CPPGTFGQNC SQDCPCHHGG QCDHVTGQCH CTAGYMGDRC
QEECPFGTFG FLCSQRCDCH NGGQCSPATG ACECEPGYKG PSCQERLCPE GLHGPGCTLP
CPCDTENTIS CHPVTGACTC QPGWSGHYCN ESCPAGYYGN GCQLPCTCQN GADCHSITGS
CTCAPGFMGE VCAVPCAAGT YGPNCSSVCS CSNGGTCSPV DGSCTCREGW QGLDCSLPCP
SGTWGLNCNE TCICANGAAC SPFDGSCACT PGWLGDSCEL PCPDGTFGLN CSEHCDCSHA
DGCDPVTGHC CCLAGWTGIR CDSTCPPGRW GPNCSVSCSC ENGGSCSPED GSCECAPGFR
GPLCQRICPP GFYGHGCAQP CPLCVHSRGP CHHISGICEC LPGFSGALCN QVCAGGHFGQ
DCAQLCSCAN NGTCSPIDGS CQCFPGWIGK DCSQACPSGF WGSACFHTCS CHNGASCSAE
DGACHCTPGW TGLFCTQRCP SAFFGKDCGH ICQCQNGASC DHITGKCTCR TGFSGRHCEQ
RCAPGTFGYG CQQLCECMNN ATCDHVTGTC YCSPGFKGIR CDQAALMMDE LNPYTKISPA
LGAERHSVGA VTGIVLLLFL VVVLLGLFAW RRRRQKEKGR DLAPRVSYTP AMRMTSTDYS
LSDLSQSSSH AQCFSNASYH TLACGGPATS QASTLDRNSP TKLSNKSLDR DTAGWTPYSY
VNVLDSHFQI SALEARYPPE DFYIELRHLS RHAEPHSPGT CGMDRRQNTY IMDKGFKDYM
KESVCSSSTC SLNSSENPYA TIKDPPILTC KLPESSYVEM KSPVHLGSPY TDVPSLSTSN
KNIYEVGRCL T
//
