RGMB_CAEEL
ID RGMB_CAEEL Reviewed; 408 AA.
AC G5EDE5;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Repulsive guidance molecule B homolog drag-1 {ECO:0000305};
DE AltName: Full=DRAGON homolog {ECO:0000312|WormBase:Y71G12B.16};
DE Flags: Precursor;
GN Name=drag-1 {ECO:0000312|WormBase:Y71G12B.16};
GN ORFNames=Y71G12B.16 {ECO:0000312|WormBase:Y71G12B.16};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=20534671; DOI=10.1242/dev.051615;
RA Tian C., Sen D., Shi H., Foehr M.L., Plavskin Y., Vatamaniuk O.K., Liu J.;
RT "The RGM protein DRAG-1 positively regulates a BMP-like signaling pathway
RT in Caenorhabditis elegans.";
RL Development 137:2375-2384(2010).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-40; DBL-1 AND SMA-6, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-68; ASP-127 AND GLY-272.
RX PubMed=24004951; DOI=10.1242/dev.099838;
RA Tian C., Shi H., Xiong S., Hu F., Xiong W.C., Liu J.;
RT "The neogenin/DCC homolog UNC-40 promotes BMP signaling via the RGM protein
RT DRAG-1 in C. elegans.";
RL Development 140:4070-4080(2013).
CC -!- FUNCTION: Probably in association with the cell surface receptor unc-
CC 40, positively modulates the BMP-like Sma/Mab signaling pathway through
CC interaction with both the ligand dbl-1 and its type I receptor sma-6
CC (PubMed:24004951). Regulates body size and this may be through
CC modulation of the Sma/Mab signaling pathway (PubMed:20534671,
CC PubMed:24004951). {ECO:0000269|PubMed:20534671,
CC ECO:0000269|PubMed:24004951}.
CC -!- SUBUNIT: Interacts with unc-40 (via FN6 domain), dbl-1 and sma-6.
CC {ECO:0000269|PubMed:24004951}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20534671};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q7TQ33}.
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal, hypodermal and intestinal
CC cells. {ECO:0000269|PubMed:20534671}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the 1-M to 4-M stage of mesodermal
CC M lineage development during the larval development.
CC {ECO:0000269|PubMed:20534671}.
CC -!- DISRUPTION PHENOTYPE: Smaller body size compared to wild-type.
CC {ECO:0000269|PubMed:20534671, ECO:0000269|PubMed:24004951}.
CC -!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family.
CC {ECO:0000305}.
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DR EMBL; HM154523; ADI88500.1; -; mRNA.
DR EMBL; HM154524; ADI88501.1; -; mRNA.
DR EMBL; BX284601; CCD67994.1; -; Genomic_DNA.
DR RefSeq; NP_490881.4; NM_058480.4.
DR AlphaFoldDB; G5EDE5; -.
DR SMR; G5EDE5; -.
DR STRING; 6239.Y71G12B.16; -.
DR PaxDb; G5EDE5; -.
DR EnsemblMetazoa; Y71G12B.16.1; Y71G12B.16.1; WBGene00022154.
DR GeneID; 190602; -.
DR KEGG; cel:CELE_Y71G12B.16; -.
DR CTD; 190602; -.
DR WormBase; Y71G12B.16; CE45612; WBGene00022154; drag-1.
DR eggNOG; ENOG502QSTJ; Eukaryota.
DR GeneTree; ENSGT00950000183112; -.
DR HOGENOM; CLU_032775_1_1_1; -.
DR InParanoid; G5EDE5; -.
DR OMA; QRCNADY; -.
DR OrthoDB; 1300661at2759; -.
DR PhylomeDB; G5EDE5; -.
DR PRO; PR:G5EDE5; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00022154; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IMP:WormBase.
DR GO; GO:0043235; C:receptor complex; IPI:WormBase.
DR GO; GO:0015026; F:coreceptor activity; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0007501; P:mesodermal cell fate specification; IMP:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IGI:WormBase.
DR GO; GO:0061065; P:regulation of dauer larval development; IGI:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:1901048; P:transforming growth factor beta receptor signaling pathway involved in regulation of multicellular organism growth; IGI:UniProtKB.
DR InterPro; IPR040287; RGM.
DR InterPro; IPR009496; RGM_C.
DR InterPro; IPR010536; RGM_N.
DR PANTHER; PTHR31428; PTHR31428; 1.
DR Pfam; PF06534; RGM_C; 1.
DR Pfam; PF06535; RGM_N; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..408
FT /note="Repulsive guidance molecule B homolog drag-1"
FT /evidence="ECO:0000305"
FT /id="PRO_5007191963"
FT TOPO_DOM 23..387
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 68
FT /note="G->V: Reduced function, and only partially rescues
FT the small body phenotype of the null mutant."
FT /evidence="ECO:0000269|PubMed:24004951"
FT MUTAGEN 127
FT /note="D->E: Rescues small body size phenotype of null
FT mutants."
FT /evidence="ECO:0000269|PubMed:24004951"
FT MUTAGEN 272
FT /note="G->V: Loss of function and reduced binding to unc-
FT 40."
FT /evidence="ECO:0000269|PubMed:24004951"
SQ SEQUENCE 408 AA; 47413 MW; 5C3EA5117758EE7C CRC64;
MSIVYLVSIT FIFSVFKPIT SCRVEECAAW FQKTKDYENL VPKATERYCQ VLQTYLKCMN
DTQRYCHGNL RFHSSELIMR RHWKEFECEK WESCNDNSHV KRKHVNTCYF NPPPSNRKLK
YCSLFGDPHL IMFNGSVQTC SEEGARPLVD NRYFLVQVTN RNVRGEALTT TVTKVTVLVR
KHNCTASLRY EASSDEEGLP RGFVDGTTFQ MTSKHSVEVL WQDDNYVEIA LHFIHSSIHI
RRQGPYLSVS VRAPTIVLET GGDVARELCW SGCRKSSRIP AELAVEMTKK FAECYRRRVH
VPKKVAEDRC KDIGNIGVFF DACVFDLMFT GDDYLVHLSR AAESDFRRLA PHHFQSHVTQ
QHARFQKENQ HKNHINQSEI FKKCIPSKSI RFYPFLAIFF FALLSLLC
