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Repulsive guidance molecule A (RGM domain family member A)

 RGMA_MOUSE              Reviewed;         454 AA.
Q6PCX7; Q7TQ34; Q8CIH6;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-JUN-2017, entry version 107.
RecName: Full=Repulsive guidance molecule A;
AltName: Full=RGM domain family member A;
Flags: Precursor;
Name=Rgma;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
PubMed=14678836; DOI=10.1016/S1567-133X(03)00144-3;
Schmidtmer J., Engelkamp D.;
"Isolation and expression pattern of three mouse homologues of chick
Rgm.";
Gene Expr. Patterns 4:105-110(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=14749425; DOI=10.1523/JNEUROSCI.4610-03.2004;
Niederkofler V., Salie R., Sigrist M., Arber S.;
"Repulsive guidance molecule (RGM) gene function is required for
neural tube closure but not retinal topography in the mouse visual
system.";
J. Neurosci. 24:808-818(2004).
[4]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=15084667; DOI=10.1523/JNEUROSCI.5296-03.2004;
Brinks H., Conrad S., Vogt J., Oldekamp J., Sierra A., Deitinghoff L.,
Bechmann I., Alvarez-Bolado G., Heimrich B., Monnier P.P.,
Mueller B.K., Skutella T.;
"The repulsive guidance molecule RGMa is involved in the formation of
afferent connections in the dentate gyrus.";
J. Neurosci. 24:3862-3869(2004).
[5]
FUNCTION, AND INTERACTION WITH BMP2 AND BMP4.
PubMed=15975920; DOI=10.1074/jbc.M503511200;
Babitt J.L., Zhang Y., Samad T.A., Xia Y., Tang J., Campagna J.A.,
Schneyer A.L., Woolf C.J., Lin H.Y.;
"Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone
morphogenetic protein co-receptor.";
J. Biol. Chem. 280:29820-29827(2005).
[6]
FUNCTION, AND INTERACTION WITH NEO1.
PubMed=17389603; DOI=10.1074/jbc.M610901200;
Conrad S., Genth H., Hofmann F., Just I., Skutella T.;
"Neogenin-RGMa signaling at the growth cone is bone morphogenetic
protein-independent and involves RhoA, ROCK, and PKC.";
J. Biol. Chem. 282:16423-16433(2007).
[7]
FUNCTION, AND INTERACTION WITH BMP2 AND BMP4.
PubMed=17472960; DOI=10.1074/jbc.M701679200;
Xia Y., Yu P.B., Sidis Y., Beppu H., Bloch K.D., Schneyer A.L.,
Lin H.Y.;
"Repulsive guidance molecule RGMa alters utilization of bone
morphogenetic protein (BMP) type II receptors by BMP2 and BMP4.";
J. Biol. Chem. 282:18129-18140(2007).
[8]
FUNCTION.
PubMed=17953666; DOI=10.1111/j.1471-4159.2007.04994.x;
Metzger M., Conrad S., Skutella T., Just L.;
"RGMa inhibits neurite outgrowth of neuronal progenitors from murine
enteric nervous system via the neogenin receptor in vitro.";
J. Neurochem. 103:2665-2678(2007).
[9]
FUNCTION.
PubMed=18519029; DOI=10.1016/j.bbrc.2008.05.124;
Yoshida J., Kubo T., Yamashita T.;
"Inhibition of branching and spine maturation by repulsive guidance
molecule in cultured cortical neurons.";
Biochem. Biophys. Res. Commun. 372:725-729(2008).
-!- FUNCTION: Member of the repulsive guidance molecule (RGM) family
that performs several functions in the developing and adult
nervous system. Regulates cephalic neural tube closure, inhibits
neurite outgrowth and cortical neuron branching, and the formation
of mature synapses. Binding to its receptor NEO1/neogenin induces
activation of RHOA-ROCK1/Rho-kinase signaling pathway through
UNC5B-ARHGEF12/LARG-PTK2/FAK1 cascade, leading to collapse of the
neuronal growth cone and neurite outgrowth inhibition.
Furthermore, RGMA binding to NEO1/neogenin leads to HRAS
inactivation by influencing HRAS-PTK2/FAK1-AKT1 pathway. It also
functions as a bone morphogenetic protein (BMP) coreceptor that
may signal through SMAD1, SMAD5, and SMAD8.
{ECO:0000269|PubMed:14749425, ECO:0000269|PubMed:15084667,
ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:17389603,
ECO:0000269|PubMed:17472960, ECO:0000269|PubMed:17953666,
ECO:0000269|PubMed:18519029}.
-!- SUBUNIT: Interacts with NEO1, BMP2 and BMP4.
{ECO:0000269|PubMed:15975920, ECO:0000269|PubMed:17389603,
ECO:0000269|PubMed:17472960}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6PCX7-1; Sequence=Displayed;
Name=2;
IsoId=Q6PCX7-2; Sequence=VSP_011316;
-!- TISSUE SPECIFICITY: Expressed in gradient in periventricular
layers of the developing nervous system. In adult, expressed in
scattered cells throughout the brain.
-!- DEVELOPMENTAL STAGE: Expressed in the early developing nervous
system, with the exception of prominent gaps in the mid-hindbrain
and the fore-midbrain boundaries. By E10.5, expression in the
nervous system decreases slightly and a segmented pattern of
expression appears, marking the ventral sites of somitic buds. At
that stage, the expression shows a strong dorsal to ventral
gradient. In the neural tubes, strong expression is detected at
the level of the floor plate and in the medial portion of the
neural tubes. Lower expression is detected in the dorsal neural
tube and the ventral aspect corresponding to the area of
motoneuron differentiation. In the developing eye, expressed in
the perioptic mesenchyme. {ECO:0000269|PubMed:14678836,
ECO:0000269|PubMed:15084667}.
-!- PTM: Autocatalytically cleaved at low pH; the two chains remain
linked via two disulfide bonds. {ECO:0000250}.
-!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ557513; CAD89718.1; -; mRNA.
EMBL; BC023870; AAH23870.2; -; mRNA.
EMBL; BC059072; AAH59072.1; -; mRNA.
CCDS; CCDS21362.2; -. [Q6PCX7-1]
RefSeq; NP_808408.2; NM_177740.5. [Q6PCX7-1]
RefSeq; XP_006540965.1; XM_006540902.1. [Q6PCX7-2]
UniGene; Mm.333943; -.
ProteinModelPortal; Q6PCX7; -.
SMR; Q6PCX7; -.
STRING; 10090.ENSMUSP00000091870; -.
PhosphoSitePlus; Q6PCX7; -.
SwissPalm; Q6PCX7; -.
PaxDb; Q6PCX7; -.
PeptideAtlas; Q6PCX7; -.
PRIDE; Q6PCX7; -.
Ensembl; ENSMUST00000094312; ENSMUSP00000091870; ENSMUSG00000070509. [Q6PCX7-1]
Ensembl; ENSMUST00000139780; ENSMUSP00000145758; ENSMUSG00000070509. [Q6PCX7-2]
GeneID; 244058; -.
KEGG; mmu:244058; -.
UCSC; uc009hqz.2; mouse. [Q6PCX7-1]
CTD; 56963; -.
MGI; MGI:2679262; Rgma.
eggNOG; ENOG410IFAH; Eukaryota.
eggNOG; ENOG410ZT7E; LUCA.
GeneTree; ENSGT00390000008488; -.
HOGENOM; HOG000013072; -.
HOVERGEN; HBG057627; -.
InParanoid; Q6PCX7; -.
KO; K06847; -.
OMA; PNYTHCG; -.
OrthoDB; EOG091G0NF6; -.
PhylomeDB; Q6PCX7; -.
TreeFam; TF329836; -.
ChiTaRS; Rgma; mouse.
PRO; PR:Q6PCX7; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000070509; -.
CleanEx; MM_RGMA; -.
ExpressionAtlas; Q6PCX7; baseline and differential.
Genevisible; Q6PCX7; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0015026; F:coreceptor activity; IGI:MGI.
GO; GO:0001948; F:glycoprotein binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; IPI:MGI.
GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
GO; GO:0030509; P:BMP signaling pathway; IGI:MGI.
GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
GO; GO:0048671; P:negative regulation of collateral sprouting; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:MGI.
GO; GO:1900121; P:negative regulation of receptor binding; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:MGI.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0030510; P:regulation of BMP signaling pathway; IDA:MGI.
InterPro; IPR009496; RGM_C.
InterPro; IPR010536; RGM_N.
InterPro; IPR033607; RGMA.
PANTHER; PTHR31428:SF10; PTHR31428:SF10; 1.
Pfam; PF06534; RGM_C; 1.
Pfam; PF06535; RGM_N; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Reference proteome; Signal.
SIGNAL 1 47 {ECO:0000255}.
PROPEP 48 169 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000030388.
CHAIN 170 427 Repulsive guidance molecule A.
/FTId=PRO_0000030389.
PROPEP 428 454 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000030390.
COMPBIAS 422 430 Poly-Ala.
SITE 169 170 Cleavage; by autolysis. {ECO:0000250}.
LIPID 427 427 GPI-anchor amidated alanine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 146 227 {ECO:0000250}.
DISULFID 164 316 {ECO:0000250}.
VAR_SEQ 1 16 Missing (in isoform 2).
{ECO:0000303|PubMed:14678836,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011316.
CONFLICT 424 424 Missing (in Ref. 2; AAH23870).
{ECO:0000305}.
SEQUENCE 454 AA; 49676 MW; 3AD1C72D8A70E177 CRC64;
MQPPRERLVV TGRAGWMGMG RGAGRSALGL WPTLAFLLCS FPAAISPCKI LKCNSEFWSA
TSSGSHAPAS DDVPEFCAAL RTYALCTRRT ARTCRGDLAY HSAVHGIEDL MSQHNCSKDG
PTSQPRVRTL PPAGDSQERS DSPEICHYEK SFHKHSAAPN YTHCGLFGDP HLRTFTDHFQ
TCKVQGAWPL IDNNYLNVQV TNTPVLPGSA ATATSKLTII FKNFQECVDQ KVYQAEMDEL
PSAFADGSKN GGDKHGANSL KITEKVSGQH VEIQAKYIGT TIVVRQVGRY LTFAVRMPEE
VVNAVEDRDS QGLYLCLRGC PLNQQIDFQA FRANAESPRR PAAASPSPVV PETFPYETAV
AKCKEKLPVE DLYYQACVFD LLTTGDVNFT LAAYYALEDG KMLHSNKDKL HLFERTRELP
GAVAAAAAAA TTFPLAPQIL LGTIPLLVLL PVLW


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