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Q96B86

- RGMA_HUMAN

UniProt

Q96B86 - RGMA_HUMAN

Protein

Repulsive guidance molecule A

Gene

RGMA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    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 SMAD8.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei168 – 1692Cleavage; by autolysisBy similarity

    GO - Biological processi

    1. axon guidance Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_22237. Netrin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Repulsive guidance molecule A
    Alternative name(s):
    RGM domain family member A
    Gene namesi
    Name:RGMA
    Synonyms:RGM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:30308. RGMA.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. endoplasmic reticulum Source: LIFEdb
    3. extracellular vesicular exosome Source: UniProt
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394693.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4747Sequence AnalysisAdd
    BLAST
    Propeptidei48 – 168121Removed in mature formBy similarityPRO_0000030385Add
    BLAST
    Chaini169 – 424256Repulsive guidance molecule APRO_0000030386Add
    BLAST
    Propeptidei425 – 45026Removed in mature formSequence AnalysisPRO_0000030387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi145 ↔ 226By similarity
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi163 ↔ 315By similarity
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis
    Lipidationi424 – 4241GPI-anchor amidated alanineSequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiQ96B86.
    PRIDEiQ96B86.

    PTM databases

    PhosphoSiteiQ96B86.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96B86.
    BgeeiQ96B86.
    CleanExiHS_RGMA.
    GenevestigatoriQ96B86.

    Organism-specific databases

    HPAiCAB012343.

    Interactioni

    Subunit structurei

    Interacts with NEO1, BMP2 and BMP4.By similarity

    Protein-protein interaction databases

    BioGridi121284. 3 interactions.
    IntActiQ96B86. 2 interactions.
    MINTiMINT-1420050.
    STRINGi9606.ENSP00000330005.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96B86.
    SMRiQ96B86. Positions 169-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG87951.
    HOGENOMiHOG000013072.
    HOVERGENiHBG057627.
    InParanoidiQ96B86.
    KOiK06847.
    OMAiPLNQQID.
    OrthoDBiEOG7VQJDC.
    PhylomeDBiQ96B86.
    TreeFamiTF329836.

    Family and domain databases

    InterProiIPR009496. RGM_C.
    IPR010536. RGM_N.
    [Graphical view]
    PfamiPF06534. RGM_C. 1 hit.
    PF06535. RGM_N. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96B86-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQPPRERLVV TGRAGWMGMG RGAGRSALGF WPTLAFLLCS FPAATSPCKI    50
    LKCNSEFWSA TSGSHAPASD DTPEFCAALR SYALCTRRTA RTCRGDLAYH 100
    SAVHGIEDLM SQHNCSKDGP TSQPRLRTLP PAGDSQERSD SPEICHYEKS 150
    FHKHSATPNY THCGLFGDPH LRTFTDRFQT CKVQGAWPLI DNNYLNVQVT 200
    NTPVLPGSAA TATSKLTIIF KNFQECVDQK VYQAEMDELP AAFVDGSKNG 250
    GDKHGANSLK ITEKVSGQHV EIQAKYIGTT IVVRQVGRYL TFAVRMPEEV 300
    VNAVEDWDSQ GLYLCLRGCP LNQQIDFQAF HTNAEGTGAR RLAAASPAPT 350
    APETFPYETA VAKCKEKLPV EDLYYQACVF DLLTTGDVNF TLAAYYALED 400
    VKMLHSNKDK LHLYDRTRDL PGRAAAGLPL APRPLLGALV PLLALLPVFC 450
    Length:450
    Mass (Da):49,347
    Last modified:May 18, 2010 - v3
    Checksum:iE3244FA43A029DCF
    GO
    Isoform 2 (identifier: Q96B86-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: Missing.

    Show »
    Length:434
    Mass (Da):47,512
    Checksum:i219D630DAEF61745
    GO
    Isoform 3 (identifier: Q96B86-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-4: MQPP → MGGLGPRRAGTS

    Note: No experimental confirmation available.

    Show »
    Length:458
    Mass (Da):50,035
    Checksum:iE01D353C68437163
    GO

    Sequence cautioni

    The sequence AAH15886.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAB98207.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 1991V → A in BAC11285. (PubMed:14702039)Curated
    Sequence conflicti314 – 3141L → P in BAH13014. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti415 – 4151D → E.5 Publications
    Corresponds to variant rs4238485 [ dbSNP | Ensembl ].
    VAR_062144
    Natural varianti431 – 4311A → V.
    Corresponds to variant rs4778078 [ dbSNP | Ensembl ].
    VAR_060105

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1616Missing in isoform 2. 3 PublicationsVSP_054070Add
    BLAST
    Alternative sequencei1 – 44MQPP → MGGLGPRRAGTS in isoform 3. 1 PublicationVSP_054071

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL390083 mRNA. Translation: CAB98207.1. Different initiation.
    AL136826 mRNA. Translation: CAB66760.1.
    AK074910 mRNA. Translation: BAC11285.1.
    AK074966 mRNA. Translation: BAC11321.1.
    AK074980 mRNA. Translation: BAC11330.1.
    AK299363 mRNA. Translation: BAH13014.1.
    AC087641 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02167.1.
    BC015886 mRNA. Translation: AAH15886.2. Different initiation.
    BC140838 mRNA. Translation: AAI40839.1.
    BC151132 mRNA. Translation: AAI51133.1.
    CCDSiCCDS45357.1. [Q96B86-1]
    CCDS53973.1. [Q96B86-3]
    CCDS53974.1. [Q96B86-4]
    RefSeqiNP_001159755.1. NM_001166283.1.
    NP_001159758.1. NM_001166286.1.
    NP_001159759.1. NM_001166287.1.
    NP_001159760.1. NM_001166288.1.
    NP_001159761.1. NM_001166289.1.
    NP_064596.2. NM_020211.2.
    UniGeneiHs.271277.

    Genome annotation databases

    EnsembliENST00000329082; ENSP00000330005; ENSG00000182175. [Q96B86-1]
    ENST00000425933; ENSP00000404442; ENSG00000182175. [Q96B86-3]
    ENST00000542321; ENSP00000440025; ENSG00000182175. [Q96B86-3]
    ENST00000543599; ENSP00000442498; ENSG00000182175. [Q96B86-3]
    ENST00000557301; ENSP00000452126; ENSG00000182175. [Q96B86-4]
    GeneIDi56963.
    KEGGihsa:56963.
    UCSCiuc002bsq.2. human. [Q96B86-1]

    Polymorphism databases

    DMDMi296452979.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL390083 mRNA. Translation: CAB98207.1 . Different initiation.
    AL136826 mRNA. Translation: CAB66760.1 .
    AK074910 mRNA. Translation: BAC11285.1 .
    AK074966 mRNA. Translation: BAC11321.1 .
    AK074980 mRNA. Translation: BAC11330.1 .
    AK299363 mRNA. Translation: BAH13014.1 .
    AC087641 Genomic DNA. No translation available.
    CH471101 Genomic DNA. Translation: EAX02167.1 .
    BC015886 mRNA. Translation: AAH15886.2 . Different initiation.
    BC140838 mRNA. Translation: AAI40839.1 .
    BC151132 mRNA. Translation: AAI51133.1 .
    CCDSi CCDS45357.1. [Q96B86-1 ]
    CCDS53973.1. [Q96B86-3 ]
    CCDS53974.1. [Q96B86-4 ]
    RefSeqi NP_001159755.1. NM_001166283.1.
    NP_001159758.1. NM_001166286.1.
    NP_001159759.1. NM_001166287.1.
    NP_001159760.1. NM_001166288.1.
    NP_001159761.1. NM_001166289.1.
    NP_064596.2. NM_020211.2.
    UniGenei Hs.271277.

    3D structure databases

    ProteinModelPortali Q96B86.
    SMRi Q96B86. Positions 169-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121284. 3 interactions.
    IntActi Q96B86. 2 interactions.
    MINTi MINT-1420050.
    STRINGi 9606.ENSP00000330005.

    PTM databases

    PhosphoSitei Q96B86.

    Polymorphism databases

    DMDMi 296452979.

    Proteomic databases

    PaxDbi Q96B86.
    PRIDEi Q96B86.

    Protocols and materials databases

    DNASUi 56963.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329082 ; ENSP00000330005 ; ENSG00000182175 . [Q96B86-1 ]
    ENST00000425933 ; ENSP00000404442 ; ENSG00000182175 . [Q96B86-3 ]
    ENST00000542321 ; ENSP00000440025 ; ENSG00000182175 . [Q96B86-3 ]
    ENST00000543599 ; ENSP00000442498 ; ENSG00000182175 . [Q96B86-3 ]
    ENST00000557301 ; ENSP00000452126 ; ENSG00000182175 . [Q96B86-4 ]
    GeneIDi 56963.
    KEGGi hsa:56963.
    UCSCi uc002bsq.2. human. [Q96B86-1 ]

    Organism-specific databases

    CTDi 56963.
    GeneCardsi GC15M093586.
    HGNCi HGNC:30308. RGMA.
    HPAi CAB012343.
    MIMi 607362. gene.
    neXtProti NX_Q96B86.
    PharmGKBi PA128394693.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG87951.
    HOGENOMi HOG000013072.
    HOVERGENi HBG057627.
    InParanoidi Q96B86.
    KOi K06847.
    OMAi PLNQQID.
    OrthoDBi EOG7VQJDC.
    PhylomeDBi Q96B86.
    TreeFami TF329836.

    Enzyme and pathway databases

    Reactomei REACT_22237. Netrin-1 signaling.

    Miscellaneous databases

    ChiTaRSi RGMA. human.
    GeneWikii RGMA.
    GenomeRNAii 56963.
    NextBioi 62595.
    PROi Q96B86.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96B86.
    Bgeei Q96B86.
    CleanExi HS_RGMA.
    Genevestigatori Q96B86.

    Family and domain databases

    InterProi IPR009496. RGM_C.
    IPR010536. RGM_N.
    [Graphical view ]
    Pfami PF06534. RGM_C. 1 hit.
    PF06535. RGM_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. The European IMAGE consortium
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLU-415.
      Tissue: Retina.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-415.
      Tissue: Testis.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANT GLU-415.
      Tissue: Teratocarcinoma.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-415.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT GLU-415.
      Tissue: Brain and Uterus.
    7. "Unc5B associates with LARG to mediate the action of repulsive guidance molecule."
      Hata K., Kaibuchi K., Inagaki S., Yamashita T.
      J. Cell Biol. 184:737-750(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Inactivation of Ras by p120GAP via focal adhesion kinase dephosphorylation mediates RGMa-induced growth cone collapse."
      Endo M., Yamashita T.
      J. Neurosci. 29:6649-6662(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiRGMA_HUMAN
    AccessioniPrimary (citable) accession number: Q96B86
    Secondary accession number(s): B2RTW1
    , B7Z5S8, F5GXQ7, F5GZU6, G3V518, Q0JV97, Q8NC80, Q9H0E6, Q9NPM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 93 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3