MDGA1_RAT
ID MDGA1_RAT Reviewed; 956 AA.
AC P85171;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 1;
DE AltName: Full=Ig6M;
DE Flags: Precursor;
GN Name=Mdga1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pons {ECO:0000269|PubMed:15019943};
RX PubMed=15019943; DOI=10.1016/j.mcn.2003.10.016;
RA Litwack E.D., Babey R., Buser R., Gesemann M., O'Leary D.D.M.;
RT "Identification and characterization of two novel brain-derived
RT immunoglobulin superfamily members with a unique structural organization.";
RL Mol. Cell. Neurosci. 25:263-274(2004).
RN [2]
RP FUNCTION, AND INTERACTION WITH NLGN2.
RX PubMed=23358245; DOI=10.1083/jcb.201206028;
RA Pettem K.L., Yokomaku D., Takahashi H., Ge Y., Craig A.M.;
RT "Interaction between autism-linked MDGAs and neuroligins suppresses
RT inhibitory synapse development.";
RL J. Cell Biol. 200:321-336(2013).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 (By similarity). Plays a role in the
CC formation or maintenance of inhibitory synapses. May function by
CC inhibiting the activity of NLGN2. {ECO:0000250,
CC ECO:0000269|PubMed:23248271, ECO:0000269|PubMed:23358245}.
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 (By similarity). Interacts (through
CC the Ig-like domains) with NLGN2. {ECO:0000250,
CC ECO:0000269|PubMed:23358245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15019943};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15019943}. Note=Associated
CC with lipid rafts. {ECO:0000250|UniProtKB:Q8NFP4,
CC ECO:0000269|PubMed:15019943}.
CC -!- TISSUE SPECIFICITY: High levels detected in developing central and
CC peripheral nervous systems with little expression elsewhere. In brain,
CC highest levels in cerebral cortex and hindbrain at E15. At postnatal
CC day 1, highest levels in basilar pons and superficial layers of the
CC neocortex. In the developing spinal cord, restricted to a subpopulation
CC of neurons in the dorsal and spinal ventral cord, probably D1
CC interneurons. Expressed in brain. {ECO:0000269|PubMed:15019943,
CC ECO:0000269|PubMed:23248271}.
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DR RefSeq; XP_006256269.1; XM_006256207.3.
DR AlphaFoldDB; P85171; -.
DR SMR; P85171; -.
DR STRING; 10116.ENSRNOP00000040424; -.
DR GlyGen; P85171; 4 sites.
DR PaxDb; P85171; -.
DR PRIDE; P85171; -.
DR GeneID; 309659; -.
DR UCSC; RGD:1307031; rat.
DR CTD; 266727; -.
DR RGD; 1307031; Mdga1.
DR eggNOG; ENOG502QUWH; Eukaryota.
DR HOGENOM; CLU_014908_0_0_1; -.
DR InParanoid; P85171; -.
DR OrthoDB; 118847at2759; -.
DR PhylomeDB; P85171; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:P85171; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P85171; RN.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:HGNC-UCL.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; ISO:RGD.
DR GO; GO:0051964; P:negative regulation of synapse assembly; IDA:RGD.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IEP:HGNC-UCL.
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 1: Evidence at protein 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_0000292928"
FT PROPEP 934..956
FT /note="Removed in mature form"
FT /id="PRO_0000292929"
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..534
FT /note="Ig-like 5"
FT /evidence="ECO:0000255"
FT DOMAIN 539..632
FT /note="Ig-like 6"
FT /evidence="ECO:0000255"
FT DOMAIN 644..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 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 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"
SQ SEQUENCE 956 AA; 105976 MW; C67A9F1CDA71C575 CRC64;
MEVTCLLLLA LIPFHCRGQG VYAPAQAQIV HAGQACVVKE DNISERVYTI RESDTLVLQC
LVTGHPRPQV RWTKTAGSAS DKFQETSVFN ETLRIERIAR TQGGRYYCKA ENGVGVPAIK
SIRVDVQYLD EPVLTVHQTV SDVRGNFYQE KTVFLRCTVS SNPPARFIWK RGSDTLSHSQ
DNGVDIYEPL YTQGETKVLK LKNLRPQDYA SYTCQVSVRN VCGIPDKSIT FQLTNTTAPP
TLKLSVNETL VVNPGENVTV QCLLTGGDPL PQLHWSHGPG PLPLGALAQG GTLSIPSVQA
RDSGYYNCTA TNNVGNPAKK TVNLLVRSLK NATFQITPDM IKESENIQLG QDLKLSCHVD
AVPQEKVNYQ WFKNGKPART SKRLLVTRND PELPAVTSSL ELIDLHFSDY GTYLCVASFP
GSPVPDLSVE VNISSETVPP TISVPKGRAV VTVREGSPAE LQCEVRGKPR PPVLWSRVDK
EAALLPSGLA LEETPDGKLR VERVSREMSG TYRCQTARYN GFNVRAREAQ VQLTVHFPPE
VEPSSQDVRQ ALGRPVLLRC SLLRGSPQRI ASAVWRFKGQ LLPPPPVLPA AAAEGPDHAE
LRLDALTRDS SGNYECSVSN DVGSATCLFQ VSAKAYSPEF YFDTPNPTRS HKLSKNYSYV
LQWTQREPDA VDPVLNYRLS IRQLNQHNAM VKAIPVRRVE KGQLLEYTLT DLRVPHSYEI
HLTPYTTFGA GDMASRVIHY TEPINSPSLS DNTCHFEDEK ICGYTQDLTD NFDWTRQNAL
TQNPKRSPNT GPPTDISGTP EGYYMFIETS RPRELGDRAR LVSPLYNASA KFYCVSFFYH
MYGKHIGSLN LLVRSRNKGT LDTHAWSLSG NKGNVWQQAH VPINPSGPFQ IIFEGVRGSG
YLGDIAIDDV TLKKGECPRR QMDPNKVVVM PGSGAPRLSS LQLWGSMTIF LLALQR
