ID   MDGA2_MACFA             Reviewed;         451 AA.
AC   Q9GMT4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=MAM domain-containing glycosylphosphatidylinositol anchor protein 2;
DE   AltName: Full=MAM domain-containing protein 1;
DE   Flags: Precursor; Fragment;
GN   Name=MDGA2; Synonyms=MAMDC1; ORFNames=QccE-16296;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA   Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA   Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT   "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT   chromosomes.";
RL   Gene 275:31-37(2001).
RN   [2]
RP   ERRATUM OF PUBMED:11574149.
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA   Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K., Kususda J.;
RL   Gene 278:267-267(2001).
CC   -!- FUNCTION: May be involved in cell-cell interactions. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (through the Ig-like domains) with NLGN2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB047834; BAB12260.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q9GMT4; -.
DR   SMR; Q9GMT4; -.
DR   STRING; 9541.XP_005561242.1; -.
DR   eggNOG; ENOG502QSMD; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.40.10; -; 2.
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; IPR000998; MAM_dom.
DR   Pfam; PF00629; MAM; 1.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50060; MAM_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome.
FT   CHAIN           <1..426
FT                   /note="MAM domain-containing glycosylphosphatidylinositol
FT                   anchor protein 2"
FT                   /id="PRO_0000072681"
FT   PROPEP          427..451
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000292046"
FT   DOMAIN          35..122
FT                   /note="Ig-like"
FT   DOMAIN          133..234
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          241..416
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   LIPID           426
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        56..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         1
SQ   SEQUENCE   451 AA;  51552 MW;  250BD3A38A6F7564 CRC64;
     AREMSGMYRC QTSQYNGFNV KPREALVQLI VQYPPAVEPA FLEIRQGQDR SVTMSCRVLR
     AYPIRVLTYE WRLGNKLLRT GQFDSQEYTE YPVKSLSNEN YGVYNCSIIN EAGAGRCSFL
     VTGKAYAPEF YYDTYNPVWQ NRHRVYSYSL QWTQMNPDAV DRIVAYRLGI RQAGQQRWWE
     QEIKINGNIQ KGELITYNLT ELIKPEAYEV RLTPLTKFGE GDSTIRVIKY SAPVNPHLRE
     FHCGFEDGNI CLFTQDDTDN FDWTKQSTAT RNTKYTPNTG PNADRSGSKE GFYMYIETSR
     PRLEGEKARL LSPVFSIAPK NPYGPTNTAY CFSFFYHMYG QHIGVLNVYL RLKGQTTIEN
     PLWSSSGNKG QRWNEAHVNI YPITSFQLIF EGIRGPGIEG DIAIDDVSIA EGECAKQDLA
     TKNSVDGAVG ILVHIWLFPI IVLISILSPR R