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RGMB_MOUSE
ID   RGMB_MOUSE              Reviewed;         436 AA.
AC   Q7TQ33; Q501K0; Q8BNR6; Q8CBM7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Repulsive guidance molecule B {ECO:0000303|PubMed:15053976};
DE   AltName: Full=DRG11-responsive axonal guidance and outgrowth of neurite {ECO:0000303|PubMed:14985445};
DE            Short=DRAGON {ECO:0000303|PubMed:14985445};
DE   Flags: Precursor;
GN   Name=Rgmb {ECO:0000303|PubMed:15053976, ECO:0000312|MGI:MGI:1916049};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=14678836; DOI=10.1016/s1567-133x(03)00144-3;
RA   Schmidtmer J., Engelkamp D.;
RT   "Isolation and expression pattern of three mouse homologues of chick Rgm.";
RL   Gene Expr. Patterns 4:105-110(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15053976; DOI=10.1016/j.modgep.2003.11.008;
RA   Oldekamp J., Kraemer N., Alvarez-Bolado G., Skutella T.;
RT   "Expression pattern of the repulsive guidance molecules RGM A, B and C
RT   during mouse development.";
RL   Gene Expr. Patterns 4:283-288(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14749425; DOI=10.1523/jneurosci.4610-03.2004;
RA   Niederkofler V., Salie R., Sigrist M., Arber S.;
RT   "Repulsive guidance molecule (RGM) gene function is required for neural
RT   tube closure but not retinal topography in the mouse visual system.";
RL   J. Neurosci. 24:808-818(2004).
RN   [6]
RP   FUNCTION, SUBUNIT, INTERACTION WITH DRGX, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND GPI-ANCHOR.
RX   PubMed=14985445; DOI=10.1523/jneurosci.4115-03.2004;
RA   Samad T.A., Srinivasan A., Karchewski L.A., Jeong S.-J., Campagna J.A.,
RA   Ji R.-R., Fabrizio D.A., Zhang Y., Lin H.Y., Bell E., Woolf C.J.;
RT   "DRAGON: a member of the repulsive guidance molecule-related family of
RT   neuronal- and muscle-expressed membrane proteins is regulated by DRG11 and
RT   has neuronal adhesive properties.";
RL   J. Neurosci. 24:2027-2036(2004).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15890774; DOI=10.1210/en.2004-1676;
RA   Xia Y., Sidis Y., Mukherjee A., Samad T.A., Brenner G., Woolf C.J.,
RA   Lin H.Y., Schneyer A.;
RT   "Localization and action of Dragon (repulsive guidance molecule b), a novel
RT   bone morphogenetic protein coreceptor, throughout the reproductive axis.";
RL   Endocrinology 146:3614-3621(2005).
RN   [8]
RP   FUNCTION, INTERACTION WITH ACVR1; ACVR2B; BMP2; BMP4; BMPR1A AND BMPR1B,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=15671031; DOI=10.1074/jbc.m410034200;
RA   Samad T.A., Rebbapragada A., Bell E., Zhang Y., Sidis Y., Jeong S.-J.,
RA   Campagna J.A., Perusini S., Fabrizio D.A., Schneyer A.L., Lin H.Y.,
RA   Brivanlou A.H., Attisano L., Woolf C.J.;
RT   "DRAGON, a bone morphogenetic protein co-receptor.";
RL   J. Biol. Chem. 280:14122-14129(2005).
CC   -!- FUNCTION: Member of the repulsive guidance molecule (RGM) family that
CC       contributes to the patterning of the developing nervous system. Acts as
CC       a bone morphogenetic protein (BMP) coreceptor that potentiates BMP
CC       signaling. Promotes neuronal adhesion. May inhibit neurite outgrowth
CC       (By similarity). {ECO:0000250|UniProtKB:Q6NW40,
CC       ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15671031,
CC       ECO:0000269|PubMed:15890774}.
CC   -!- SUBUNIT: Homooligomer. Interacts with DRGX. Interacts with BMP2 and
CC       BMP4. Interacts with the BMP type I receptors ACVR1, BMPR1A and BMPR1B
CC       and with the BMP type II receptor ACVR2B. The functional complex with
CC       its receptor NEO1/neogenin appears to be a heterotetramer with a 2:2
CC       stoichiometry, RGM molecules acting as staples that bring two NEO1
CC       receptors together without interacting themselves, this arrangement
CC       leads to activation of downstream signaling via RhoA.
CC       {ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15671031}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15890774};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15890774}. Membrane raft
CC       {ECO:0000269|PubMed:15890774}.
CC   -!- TISSUE SPECIFICITY: Detected in neonatal and adult dorsal root ganglion
CC       sensory neurons, spinal cord, and brain (at protein level). Also
CC       expressed at high levels in retinal ganglion cells of developing mouse,
CC       extending to the optic nerve (at protein level). Expressed in testis,
CC       epididymis, ovary, uterus, and pituitary. {ECO:0000269|PubMed:14985445,
CC       ECO:0000269|PubMed:15890774}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing nervous system.
CC       Expression is restricted to a subset of individual neurons in the
CC       mid- and hindbrain regions. At 10.5 dpc, expression level increases and
CC       extends further into the forebrain. The segmented pattern of expression
CC       becomes more refined and is indicative of peripheral nervous system
CC       labelling. Not detected in the area of motoneuron differentiation.
CC       Expression could be restricted to postmitotic neurons. Also expressed
CC       in fetal dorsal root ganglion, dorsal horn, in the dorsomedial mantle
CC       layer of the spinal cord, alar plate of the myelencephalon, marginal
CC       layer of the mesencephalon, basal plate of the pons, and cerebellar
CC       primordia, as well as the cortex of the olfactory lobe, retina, and
CC       olfactory epithelium. In the developing eye, expressed in
CC       differentiating ganglion cells and later in the development, also in
CC       amacrine cells. In adult, expressed in scattered cells throughout the
CC       brain. {ECO:0000269|PubMed:14678836, ECO:0000269|PubMed:14749425,
CC       ECO:0000269|PubMed:14985445, ECO:0000269|PubMed:15053976,
CC       ECO:0000269|PubMed:15671031}.
CC   -!- PTM: GPI-anchored. {ECO:0000269|PubMed:14985445}.
CC   -!- PTM: Autocatalytically cleaved at low pH; the two chains remain linked
CC       via two disulfide bonds. {ECO:0000250|UniProtKB:Q6NW40}.
CC   -!- SIMILARITY: Belongs to the repulsive guidance molecule (RGM) family.
CC       {ECO:0000305}.
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DR   EMBL; AJ557514; CAD89719.1; -; mRNA.
DR   EMBL; AK035713; BAC29163.1; -; mRNA.
DR   EMBL; AK080819; BAC38034.1; -; mRNA.
DR   EMBL; BC096024; AAH96024.2; -; mRNA.
DR   EMBL; BC138890; AAI38891.1; -; mRNA.
DR   CCDS; CCDS37455.1; -.
DR   RefSeq; NP_848730.2; NM_178615.3.
DR   RefSeq; XP_006524928.1; XM_006524865.2.
DR   AlphaFoldDB; Q7TQ33; -.
DR   SMR; Q7TQ33; -.
DR   STRING; 10090.ENSMUSP00000126177; -.
DR   GlyGen; Q7TQ33; 2 sites.
DR   iPTMnet; Q7TQ33; -.
DR   PhosphoSitePlus; Q7TQ33; -.
DR   EPD; Q7TQ33; -.
DR   PaxDb; Q7TQ33; -.
DR   PeptideAtlas; Q7TQ33; -.
DR   PRIDE; Q7TQ33; -.
DR   ProteomicsDB; 255249; -.
DR   Antibodypedia; 2207; 216 antibodies from 30 providers.
DR   DNASU; 68799; -.
DR   Ensembl; ENSMUST00000170578; ENSMUSP00000126177; ENSMUSG00000048027.
DR   GeneID; 68799; -.
DR   KEGG; mmu:68799; -.
DR   UCSC; uc008aow.1; mouse.
DR   CTD; 285704; -.
DR   MGI; MGI:1916049; Rgmb.
DR   VEuPathDB; HostDB:ENSMUSG00000048027; -.
DR   eggNOG; ENOG502QSTJ; Eukaryota.
DR   GeneTree; ENSGT00950000183112; -.
DR   HOGENOM; CLU_032775_1_1_1; -.
DR   InParanoid; Q7TQ33; -.
DR   OMA; SQCHEKM; -.
DR   OrthoDB; 1300661at2759; -.
DR   PhylomeDB; Q7TQ33; -.
DR   TreeFam; TF329836; -.
DR   BioGRID-ORCS; 68799; 9 hits in 73 CRISPR screens.
DR   ChiTaRS; Rgmb; mouse.
DR   PRO; PR:Q7TQ33; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q7TQ33; protein.
DR   Bgee; ENSMUSG00000048027; Expressed in rostral migratory stream and 286 other tissues.
DR   ExpressionAtlas; Q7TQ33; baseline and differential.
DR   Genevisible; Q7TQ33; MM.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:MGI.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015026; F:coreceptor activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR   GO; GO:0007165; P:signal transduction; IDA:HGNC-UCL.
DR   InterPro; IPR033608; DRAGON.
DR   InterPro; IPR040287; RGM.
DR   InterPro; IPR009496; RGM_C.
DR   InterPro; IPR010536; RGM_N.
DR   PANTHER; PTHR31428; PTHR31428; 1.
DR   PANTHER; PTHR31428:SF5; PTHR31428:SF5; 1.
DR   Pfam; PF06534; RGM_C; 1.
DR   Pfam; PF06535; RGM_N; 1.
PE   1: Evidence at protein level;
KW   Autocatalytic cleavage; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..48
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..415
FT                   /note="Repulsive guidance molecule B"
FT                   /id="PRO_0000030396"
FT   PROPEP          416..436
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030397"
FT   SITE            171..172
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NW40"
FT   LIPID           415
FT                   /note="GPI-anchor amidated cysteine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        386
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        142..229
FT                   /evidence="ECO:0000250|UniProtKB:Q6NW40"
FT   DISULFID        166..315
FT                   /evidence="ECO:0000250|UniProtKB:Q6NW40"
FT   CONFLICT        8
FT                   /note="S -> Y (in Ref. 2; BAC38034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="A -> G (in Ref. 2; BAC38034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="A -> G (in Ref. 2; BAC38034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        25
FT                   /note="G -> R (in Ref. 2; BAC38034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="S -> T (in Ref. 2; BAC38034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="P -> T (in Ref. 2; BAC29163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        300
FT                   /note="E -> K (in Ref. 2; BAC29163)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  47181 MW;  F54665575032B830 CRC64;
     MGVRAAPSCA AAPAAAGAEQ SRRPGLWPPS PPPPLLLLLL LSLGLLHAGD CQQPTQCRIQ
     KCTTDFVALT AHLNSAADGF DSEFCKALRA YAGCTQRTSK ACRGNLVYHS AVLGISDLMS
     QRNCSKDGPT SSTNPEVTHD PCNYHSHGGV REHGGGDQRP PNYLFCGLFG DPHLRTFKDH
     FQTCKVEGAW PLIDNNYLSV QVTNVPVVPG SSATATNKVT IIFKAQHECT DQKVYQAVTD
     DLPAAFVDGT TSGGDGDVKS LHIVEKESGR YVEMHARYIG TTVFVRQLGR YLTLAIRMPE
     DLAMSYEESQ DLQLCVNGCP MSECIDDGQG QVSAILGHSL PHTTSVQAWP GYTLETASTQ
     CHEKMPVKDI YFQSCVFDLL TTGDANFTAA AHSALEDVEA LHPRKERWHI FPSSCGGCRD
     LPVGLGLTCL ILIMFL
 
 
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