MDGA1_MOUSE
ID MDGA1_MOUSE Reviewed; 956 AA.
AC Q0PMG2; E9PY95; E9QP80;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 1;
DE Flags: Precursor;
GN Name=Mdga1 {ECO:0000312|EMBL:ABG78614.1, ECO:0000312|MGI:MGI:1922012};
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] {ECO:0000305, ECO:0000312|EMBL:ABG78614.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:ABG78614.1};
RC TISSUE=Brain {ECO:0000312|EMBL:ABG78614.1};
RX PubMed=16641224; DOI=10.1523/jneurosci.4935-05.2006;
RA Takeuchi A., O'Leary D.D.M.;
RT "Radial migration of superficial layer cortical neurons controlled by novel
RT Ig cell adhesion molecule MDGA1.";
RL J. Neurosci. 26:4460-4464(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 562-818.
RG The MGC Project Team;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16959869; DOI=10.1093/cercor/bhl064;
RA Takeuchi A., Hamasaki T., Litwack E.D., O'leary D.D.;
RT "Novel IgCAM, MDGA1, expressed in unique cortical area- and layer-specific
RT patterns and transiently by distinct forebrain populations of Cajal-Retzius
RT neurons.";
RL Cereb. Cortex 17:1531-1541(2007).
RN [5]
RP FUNCTION.
RX PubMed=23248271; DOI=10.1073/pnas.1219987110;
RA Lee K., Kim Y., Lee S.-J., Qiang Y., Lee D., Lee H.W., Kim H., Je H.S.,
RA Suedhof T.C., Ko J.;
RT "MDGAs interact selectively with neuroligin-2 but not other neuroligins to
RT regulate inhibitory synapse development.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:336-341(2013).
CC -!- FUNCTION: Required for radial migration of cortical neurons in the
CC superficial layer of the neocortex. Plays a role in the formation or
CC maintenance of inhibitory synapses. May function by inhibiting the
CC activity of NLGN2. {ECO:0000269|PubMed:16641224,
CC ECO:0000269|PubMed:23248271}.
CC -!- SUBUNIT: Interacts heterophilically through its MAM domain with
CC proteins in axon-rich regions and through its Ig-like domains with
CC proteins in differentiating muscle. Interacts (through the Ig-like
CC domains) with NLGN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Note=Associated with lipid rafts.
CC {ECO:0000250|UniProtKB:Q8NFP4}.
CC -!- TISSUE SPECIFICITY: Expressed by neurons in layers 2 and 3 of the
CC cortex during their migration and settling in the cortical plate. Also
CC found in layers 4 and 6a. From 9.5 dpc-13.5 dpc, detected in the
CC marginal zone of the developing cortex. At 16.5 dpc, modest expression
CC is found in the intermediate zone. At postnatal day 1, evident in the
CC superficial cortical plate. By postnatal day 7, expression is limited
CC to layers 2 and 3 throughout most of the cortex.
CC {ECO:0000269|PubMed:16641224, ECO:0000269|PubMed:16959869}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo and soon after
CC birth but not detected in adults. {ECO:0000269|PubMed:16641224}.
CC -!- DISRUPTION PHENOTYPE: Mice display impaired migration of superficial
CC layer cortical neurons with neurons found deep in the cortical plate or
CC beneath it. {ECO:0000269|PubMed:16641224}.
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DR EMBL; DQ788983; ABG78614.1; -; mRNA.
DR EMBL; AC151294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CD352497; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS89052.1; -.
DR RefSeq; XP_006525103.1; XM_006525040.3.
DR AlphaFoldDB; Q0PMG2; -.
DR SMR; Q0PMG2; -.
DR STRING; 10090.ENSMUSP00000126529; -.
DR GlyConnect; 2500; 5 N-Linked glycans (3 sites).
DR GlyGen; Q0PMG2; 8 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q0PMG2; -.
DR PhosphoSitePlus; Q0PMG2; -.
DR SwissPalm; Q0PMG2; -.
DR MaxQB; Q0PMG2; -.
DR PaxDb; Q0PMG2; -.
DR PRIDE; Q0PMG2; -.
DR ProteomicsDB; 292203; -.
DR ProteomicsDB; 355368; -.
DR Antibodypedia; 29838; 30 antibodies from 13 providers.
DR Ensembl; ENSMUST00000171691; ENSMUSP00000126529; ENSMUSG00000043557.
DR MGI; MGI:1922012; Mdga1.
DR VEuPathDB; HostDB:ENSMUSG00000043557; -.
DR eggNOG; ENOG502QUWH; Eukaryota.
DR GeneTree; ENSGT00940000159201; -.
DR InParanoid; Q0PMG2; -.
DR OrthoDB; 118847at2759; -.
DR TreeFam; TF330345; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 74762; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Mdga1; mouse.
DR PRO; PR:Q0PMG2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q0PMG2; protein.
DR Bgee; ENSMUSG00000043557; Expressed in neural tube mantle layer and 105 other tissues.
DR ExpressionAtlas; Q0PMG2; baseline and differential.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0051964; P:negative regulation of synapse assembly; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IDA:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:MGI.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00137; MAM; 1.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS50060; MAM_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Neurogenesis; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..933
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292926"
FT PROPEP 934..956
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292927"
FT DOMAIN 24..123
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 132..230
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 240..323
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 338..432
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 440..532
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 539..650
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 627..744
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 752..919
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 780..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 933
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 262..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 357..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 463..514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 560..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 23
FT /note="A -> T (in Ref. 1; ABG78614)"
FT /evidence="ECO:0000305"
FT CONFLICT 633..649
FT /note="AKAYSPEFYFDTPNPTR -> V (in Ref. 1; ABG78614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 106047 MW; 1CE4AC3195936ECD CRC64;
MEVTCLLLLA LIPFHCRGQG VYAPAQAQIV HAGQACVVKE DNISERVYTI RESDTLVLQC
LVTGHPRPQV RWTKTAGSAS DKFQETSVFN ETLRIERIAR TQGGRYYCKA ENGVGVPAIK
SIRVDVQYLD EPVLTVHQTV SDVRGNFYQE KTVFLRCTVS SNPPARFIWK RGSDTLSHSQ
DNGVDIYEPL YTQGETKVLK LKNLRPQDYA SYTCQVSVRN VCGIPDKAIT FQLTNTTAPP
ALKLSVNETL VVNPGENVTV QCLLTGGDPL PQLHWSHGPG PLPLGALAQG GTLSIPSVQA
RDSGYYNCTA TNNVGNPAKK TVNLLVRSLK NATFQITPDM IKESENIQLG QDLKLSCHVD
AVPQEKVNYQ WFKNGKPART SKRLLVTRND PELPAVTSSL ELIDLHFSDY GTYLCMASFP
GSPVPDLSIE VNISSETVPP TISVPKGRAV VTVREGSPAE LQCEVRGKPR PPVLWSRVDK
EAALLPSGLA LEETPDGKLR LESVSRDMSG TYRCQTARYN GFNVRPREAQ VQLTVHFPPE
VEPSSQDVRQ ALGRPVLLRC SLLRGSPQRI ASAVWRFKGQ LLPPPPVLPA AAVETPDHAE
LRLDALTRDS SGNYECSVSN DVGSATCLFQ VSAKAYSPEF YFDTPNPTRS HKLSKNYSYV
LQWTQREPDA VDPVLNYRLS IRQLNQHNAM VKAIPVRRVE KGQLLEYILT DLRVPHSYEI
RLTPYTTFGA GDMASRIIHY TEPINLPSLS DNTCHFEDEK ICGYTQDLTD NFDWTRQNAL
TQNPKRSPNT GPPTDISGTP EGYYMFIETS RPRELGDRAR LVSPLYNASA KFYCVSFFYH
MYGKHIGSLN LLVRSRNKGT LDTHAWSLSG NKGNVWQQAH VPINPSGPFQ IIFEGVRGSG
YLGDIAIDDV TLKKGECPRR QMDPNKVVVM PGSGAPRLSS LQLWGSMAIF LLALQR
