MDGA2_MOUSE
ID MDGA2_MOUSE Reviewed; 949 AA.
AC P60755;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 2;
DE AltName: Full=MAM domain-containing protein 1;
DE Flags: Precursor;
GN Name=Mdga2; Synonyms=Mamdc1;
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 [MRNA].
RC STRAIN=CD-1;
RA Huang C.Q., Wu S.L., Liu S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP 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 [4]
RP INTERACTION WITH NLGN2.
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: May be involved in cell-cell interactions. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (through the Ig-like domains) with NLGN2.
CC {ECO:0000269|PubMed:23248271, ECO:0000269|PubMed:23358245}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
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DR EMBL; AY371925; AAQ75751.1; -; mRNA.
DR CCDS; CCDS25945.1; -.
DR RefSeq; NP_996893.3; NM_207010.2.
DR AlphaFoldDB; P60755; -.
DR SMR; P60755; -.
DR STRING; 10090.ENSMUSP00000137608; -.
DR GlyConnect; 2501; 4 N-Linked glycans (3 sites).
DR GlyGen; P60755; 8 sites, 4 N-linked glycans (3 sites).
DR iPTMnet; P60755; -.
DR PhosphoSitePlus; P60755; -.
DR SwissPalm; P60755; -.
DR MaxQB; P60755; -.
DR PaxDb; P60755; -.
DR PRIDE; P60755; -.
DR ProteomicsDB; 293446; -.
DR Antibodypedia; 162; 94 antibodies from 17 providers.
DR DNASU; 320772; -.
DR Ensembl; ENSMUST00000223141; ENSMUSP00000152613; ENSMUSG00000034912.
DR GeneID; 320772; -.
DR KEGG; mmu:320772; -.
DR UCSC; uc007nrl.3; mouse.
DR CTD; 161357; -.
DR MGI; MGI:2444706; Mdga2.
DR VEuPathDB; HostDB:ENSMUSG00000034912; -.
DR eggNOG; ENOG502QSMD; Eukaryota.
DR GeneTree; ENSGT00940000155369; -.
DR HOGENOM; CLU_014908_0_0_1; -.
DR InParanoid; P60755; -.
DR OMA; HKDETEY; -.
DR PhylomeDB; P60755; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 320772; 1 hit in 67 CRISPR screens.
DR ChiTaRS; Mdga2; mouse.
DR PRO; PR:P60755; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P60755; protein.
DR Bgee; ENSMUSG00000034912; Expressed in lateral septal nucleus and 96 other tissues.
DR ExpressionAtlas; P60755; baseline and differential.
DR Genevisible; P60755; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IDA:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF07679; I-set; 1.
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; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..924
FT /note="MAM domain-containing glycosylphosphatidylinositol
FT anchor protein 2"
FT /id="PRO_0000014860"
FT PROPEP 925..949
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000292044"
FT DOMAIN 27..127
FT /note="Ig-like 1"
FT DOMAIN 134..232
FT /note="Ig-like 2"
FT DOMAIN 242..328
FT /note="Ig-like 3"
FT DOMAIN 340..436
FT /note="Ig-like 4"
FT DOMAIN 442..533
FT /note="Ig-like 5"
FT DOMAIN 540..627
FT /note="Ig-like 6"
FT DOMAIN 638..738
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 739..914
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT LIPID 924
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 159..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 264..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 359..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 465..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 561..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 949 AA; 106689 MW; 10205A40D4DB379A CRC64;
MDLVYGLVWL LTVLLEGISG QGVYAPPTVR IVHSGLACNI EEERYSERVY TIREGETLEL
TCLVTGHPRP QIRWTKTAGS ASDRFQDSSV FNETLRITNI QRHQGGRYYC KAENGLGSPA
IKSIRVDVYY LDDPVVTVHQ SIGEAKEQFY YERTVFLRCV ANSNPPVRYS WRRGQEVLLQ
GSDKGVEIYE PFFTQGETKI LKLKNLRPQD YANYSCIASV RNVCNIPDKM VSFRLSNKTA
SPSIKLLVDD PIVVNPGEAI TLVCVTTGGE PTPSLTWVRS FGTLPEKIVL NGGTLTIPAI
TSDDAGTYSC IANNNVGNPA KKSTNIIVRA LKKGRFWITP DPYHKDDNIQ IGREVKISCQ
VEAVPSEELT FSWFKNGRPL RSSERMVITQ TDPDVSPGTT NLDIIDLKFT DFGTYTCVAS
LKGGGISDIS IDVNISSSTV PPNLTVPQEK SPLVTREGDT IELQCQVTGK PKPIILWSRA
DKEVAMPDGT MQMESYDGTL RIVNVSREMS GMYRCQTSQY NGFNVKPREA LVQLIVQYPP
AVEPAFLEIR QGQDRSVTMS CRVLRAYPIR VLTYEWRLGN KLLRTGQFDS QEYTEYPLKS
LSNENYGVYN CSIINEAGAG RCSFLVTGKA YAPEFYYDTY NPVWQNRHRV YSYSLQWTQM
NPDAVDRIVA YRLGIRQAGQ QRWWEQEIKI NGNIQKGELI TYNLTELIKP EAYEVRLTPL
TKFGEGDSTI RVIKYTGEFH CGFEDGNICL FTQDDTDNFD WTKQSTATRN TKYTPNTGPS
ADRSGSKEGF YMYIETSRPR LEGEKARLLS PVFSIAPKNP YGPTNSAYCF SFFYHMYGQH
IGVLNVYLRL KGQTTIENPL WSSSGNKGQR WNEAHVNIYP ITSFQLIFEG IRGPGIEGDI
AIDDVSIAEG ECAKQDLPTK NSVDGAVGIL VHIWLFPVII LISILSPRR
