ID   RGMA_MACFA              Reviewed;         458 AA.
AC   Q9N0A6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Repulsive guidance molecule A;
DE   AltName: Full=RGM domain family member A;
DE   Flags: Precursor;
GN   Name=RGMA; ORFNames=QccE-16553;
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;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the repulsive guidance molecule (RGM) family that
CC       performs several functions in the developing and adult nervous system.
CC       Regulates cephalic neural tube closure, inhibits neurite outgrowth and
CC       cortical neuron branching, and the formation of mature synapses.
CC       Binding to its receptor NEO1/neogenin induces activation of RHOA-
CC       ROCK1/Rho-kinase signaling pathway through UNC5B-ARHGEF12/LARG-
CC       PTK2/FAK1 cascade, leading to collapse of the neuronal growth cone and
CC       neurite outgrowth inhibition. Furthermore, RGMA binding to
CC       NEO1/neogenin leads to HRAS inactivation by influencing HRAS-PTK2/FAK1-
CC       AKT1 pathway. It also functions as a bone morphogenetic protein (BMP)
CC       coreceptor that may signal through SMAD1, SMAD5, and SMAD8 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NEO1, BMP2 and BMP4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- PTM: Autocatalytically cleaved at low pH; the two chains remain linked
CC       via two disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family.
CC       {ECO:0000305}.
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DR   EMBL; AB046024; BAB01606.1; -; mRNA.
DR   RefSeq; NP_001270237.1; NM_001283308.1.
DR   AlphaFoldDB; Q9N0A6; -.
DR   SMR; Q9N0A6; -.
DR   STRING; 9541.XP_005560620.1; -.
DR   PRIDE; Q9N0A6; -.
DR   GeneID; 101866018; -.
DR   CTD; 56963; -.
DR   eggNOG; ENOG502QSTJ; Eukaryota.
DR   OrthoDB; 1300661at2759; -.
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   GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR   GO; GO:0030509; P:BMP signaling pathway; IEA:InterPro.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; IEA:InterPro.
DR   InterPro; IPR040287; RGM.
DR   InterPro; IPR009496; RGM_C.
DR   InterPro; IPR010536; RGM_N.
DR   InterPro; IPR033607; RGMA.
DR   PANTHER; PTHR31428; PTHR31428; 1.
DR   PANTHER; PTHR31428:SF4; PTHR31428:SF4; 1.
DR   Pfam; PF06534; RGM_C; 1.
DR   Pfam; PF06535; RGM_N; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..53
FT                   /evidence="ECO:0000255"
FT   PROPEP          54..176
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000285777"
FT   CHAIN           177..433
FT                   /note="Repulsive guidance molecule A"
FT                   /id="PRO_0000285778"
FT   PROPEP          434..458
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000285779"
FT   REGION          121..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            176..177
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           433
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        153..234
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..323
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  50016 MW;  9A7D20ED5793D8B0 CRC64;
     MGGPGPRRAG TSRERLVVTG RAGWMGMGRG AGRSALGFWP TLAFLLCSFP AATSPCKILK
     CNSEFWSATS GSHAPASDDT PEFCAALRSY ALCTRRTART CRGDLAYHSA VHGIEDLMSQ
     HNCSKDGPTS QPRLHTLPPA GDSQERSDSP EICHCEKSFH KHSATPNYTH CGLFGDPHLR
     TFTDRFQTCK VQGAWPLIDN NYLNVQVTNT PVLPGSAATA TSKLTIIFKN FQECVDQKVY
     QAEMDELPAA FVDGSKNGGD KHGANSLKIT EKVSGQHVEI RAKYIGTTIV VRQVGRYLTF
     AVRVPEEVVN AVEDWDSQGL YLCLRGCPLN QQIDFQAFHT NTEGTGARRL AAASPAPTAP
     ETFPYETAVA KCKEKLPVED LYYQACVFDL LTTGDVNFTL AAYYALEDVK MLHSNKDKLH
     LYERTRDLPG RAAAGLPLAP QPLLGALILL LALFPVFC