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Protein

RGM domain family member B

Gene

Rgmb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Member of the repulsive guidance molecule (RGM) family that contributes to the patterning of the developing nervous system. Acts as a bone morphogenetic protein (BMP) coreceptor that potentiates BMP signaling. Promotes neuronal adhesion. May inhibit neurite outgrowth (By similarity).By similarity3 Publications

GO - Molecular functioni

  • coreceptor activity Source: GO_Central
  • identical protein binding Source: MGI

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
RGM domain family member B
Alternative name(s):
DRG11-responsive axonal guidance and outgrowth of neurite
Short name:
DRAGON
Gene namesi
Name:Rgmb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1916049 Rgmb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 48Sequence analysisAdd BLAST48
ChainiPRO_000003039649 – 415RGM domain family member BAdd BLAST367
PropeptideiPRO_0000030397416 – 436Removed in mature formSequence analysisAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi123N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi142 ↔ 229By similarity
Disulfide bondi166 ↔ 315By similarity
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi415GPI-anchor amidated cysteineSequence analysis1

Post-translational modificationi

GPI-anchored.
Autocatalytically cleaved at low pH; the two chains remain linked via two disulfide bonds.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei171 – 172Cleavage; by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ7TQ33
PeptideAtlasiQ7TQ33
PRIDEiQ7TQ33

PTM databases

iPTMnetiQ7TQ33
PhosphoSitePlusiQ7TQ33

Expressioni

Tissue specificityi

Detected in neonatal and adult dorsal root ganglion sensory neurons, spinal cord, and brain (at protein level). Also expressed at high levels in retinal ganglion cells of developing mouse, extending to the optic nerve (at protein level). Expressed in testis, epididymis, ovary, uterus, and pituitary.2 Publications

Developmental stagei

Expressed in the developing nervous system. Expression is restricted to a subset of individual neurons in the mid- and hindbrain regions. At E10.5, expression level increases and extends further into the forebrain. The segmented pattern of expression becomes more refined and is indicative of peripheral nervous system labelling. Not detected in the area of motoneuron differentiation. Expression could be restricted to postmitotic neurons. Also expressed in fetal dorsal root ganglion, dorsal horn, in the dorsomedial mantle layer of the spinal cord, alar plate of the myelencephalon, marginal layer of the mesencephalon, basal plate of the pons, and cerebellar primordia, as well as the cortex of the olfactory lobe, retina, and olfactory epithelium. In the developing eye, expressed in differentiating ganglion cells and later in the development, also in amacrine cells. In adult, expressed in scattered cells throughout the brain.5 Publications

Gene expression databases

BgeeiENSMUSG00000048027 Expressed in 280 organ(s), highest expression level in medial habenular nucleus
CleanExiMM_RGMB
GenevisibleiQ7TQ33 MM

Interactioni

Subunit structurei

Homooligomer. Interacts with DRGX. Interacts with BMP2 and BMP4. Interacts with the BMP type I receptors ACVR1, BMPR1A and BMPR1B and with the BMP type II receptor ACVR2B. The functional complex with its receptor NEO1/neogenin appears to be a heterotetramer with a 2:2 stoichiometry, RGM molecules acting as staples that brings two NEO1 receptors together without interacting themselves, this arrangement leads to activation of downstream signaling via RhoA.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000126177

Structurei

3D structure databases

ProteinModelPortaliQ7TQ33
SMRiQ7TQ33
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFAH Eukaryota
ENOG410ZT7E LUCA
GeneTreeiENSGT00390000008488
HOGENOMiHOG000013072
HOVERGENiHBG057627
InParanoidiQ7TQ33
KOiK06847
OMAiTIIFKPY
OrthoDBiEOG091G0NF6
PhylomeDBiQ7TQ33
TreeFamiTF329836

Family and domain databases

Gene3Di3.40.1000.10, 1 hit
InterProiView protein in InterPro
IPR033608 DRAGON
IPR016123 Mog1/PsbP_a/b/a-sand
IPR009496 RGM_C
IPR010536 RGM_N
PANTHERiPTHR31428:SF5 PTHR31428:SF5, 1 hit
PfamiView protein in Pfam
PF06534 RGM_C, 1 hit
PF06535 RGM_N, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7TQ33-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGVRAAPSCA AAPAAAGAEQ SRRPGLWPPS PPPPLLLLLL LSLGLLHAGD
60 70 80 90 100
CQQPTQCRIQ KCTTDFVALT AHLNSAADGF DSEFCKALRA YAGCTQRTSK
110 120 130 140 150
ACRGNLVYHS AVLGISDLMS QRNCSKDGPT SSTNPEVTHD PCNYHSHGGV
160 170 180 190 200
REHGGGDQRP PNYLFCGLFG DPHLRTFKDH FQTCKVEGAW PLIDNNYLSV
210 220 230 240 250
QVTNVPVVPG SSATATNKVT IIFKAQHECT DQKVYQAVTD DLPAAFVDGT
260 270 280 290 300
TSGGDGDVKS LHIVEKESGR YVEMHARYIG TTVFVRQLGR YLTLAIRMPE
310 320 330 340 350
DLAMSYEESQ DLQLCVNGCP MSECIDDGQG QVSAILGHSL PHTTSVQAWP
360 370 380 390 400
GYTLETASTQ CHEKMPVKDI YFQSCVFDLL TTGDANFTAA AHSALEDVEA
410 420 430
LHPRKERWHI FPSSCGGCRD LPVGLGLTCL ILIMFL
Length:436
Mass (Da):47,181
Last modified:October 1, 2003 - v1
Checksum:iF54665575032B830
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8S → Y in BAC38034 (PubMed:16141072).Curated1
Sequence conflicti12A → G in BAC38034 (PubMed:16141072).Curated1
Sequence conflicti15A → G in BAC38034 (PubMed:16141072).Curated1
Sequence conflicti25G → R in BAC38034 (PubMed:16141072).Curated1
Sequence conflicti30S → T in BAC38034 (PubMed:16141072).Curated1
Sequence conflicti141P → T in BAC29163 (PubMed:16141072).Curated1
Sequence conflicti300E → K in BAC29163 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ557514 mRNA Translation: CAD89719.1
AK035713 mRNA Translation: BAC29163.1
AK080819 mRNA Translation: BAC38034.1
BC096024 mRNA Translation: AAH96024.2
BC138890 mRNA Translation: AAI38891.1
CCDSiCCDS37455.1
RefSeqiNP_848730.2, NM_178615.3
XP_006524928.1, XM_006524865.2
UniGeneiMm.293466

Genome annotation databases

EnsembliENSMUST00000170578; ENSMUSP00000126177; ENSMUSG00000048027
GeneIDi68799
KEGGimmu:68799
UCSCiuc008aow.1 mouse

Similar proteinsi

Entry informationi

Entry nameiRGMB_MOUSE
AccessioniPrimary (citable) accession number: Q7TQ33
Secondary accession number(s): Q501K0, Q8BNR6, Q8CBM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: September 12, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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