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P58335

- ANTR2_HUMAN

UniProt

P58335 - ANTR2_HUMAN

Protein

Anthrax toxin receptor 2

Gene

ANTXR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 5 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Necessary for cellular interactions with laminin and the extracellular matrix.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi52 – 521Divalent metal cation
    Metal bindingi54 – 541Divalent metal cation
    Metal bindingi118 – 1181Divalent metal cation

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. receptor activity Source: InterPro

    GO - Biological processi

    1. reproductive process Source: Ensembl

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthrax toxin receptor 2
    Alternative name(s):
    Capillary morphogenesis gene 2 protein
    Short name:
    CMG-2
    Gene namesi
    Name:ANTXR2
    Synonyms:CMG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:21732. ANTXR2.

    Subcellular locationi

    Isoform 1 : Cell membrane; Single-pass type I membrane protein
    Note: Expressed at the cell surface.
    Isoform 2 : Endoplasmic reticulum membrane; Single-pass type I membrane protein
    Note: Expressed predominantly within the endoplasmic reticulum and not at the plasma membrane.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Hyaline fibromatosis syndrome (HFS) [MIM:228600]: An autosomal recessive syndrome characterized by abnormal growth of hyalinized fibrous tissue usually affecting subcutaneous regions on the scalp, ears, neck, face, hands, and feet. The lesions appear as pearly papules or fleshy nodules. Additional features include gingival hypertrophy, progressive joint contractures resulting in severe limitation of mobility, osteopenia, and osteoporosis. Disease severity is variable. Some individuals manifest symptoms in infancy and have additional visceral or systemic involvement. Hyaline deposits in multiple organs, recurrent infections and intractable diarrhea often lead to early death. Surviving children may suffer from severely reduced mobility due to joint contractures. Other patients have later onset of a milder disorder affecting only the face and digits.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451L → P in HFS; infantile form. 1 Publication
    VAR_022687
    Natural varianti105 – 1051G → D in HFS. 1 Publication
    VAR_022688
    Natural varianti189 – 1891I → T in HFS; infantile form. 2 Publications
    VAR_022689
    Natural varianti218 – 2181C → R in HFS; infantile form. 1 Publication
    VAR_022690
    Natural varianti293 – 2931V → VQ in HFS. 1 Publication
    VAR_022691
    Natural varianti329 – 3291L → R in HFS. 1 Publication
    VAR_022692
    Natural varianti381 – 3811Y → C in HFS. 1 Publication
    VAR_022694

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi228600. phenotype.
    Orphaneti2176. Infantile systemic hyalinosis.
    2028. Juvenile hyaline fibromatosis.
    PharmGKBiPA128394752.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 489456Anthrax toxin receptor 2PRO_0000002694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi39 ↔ 218
    Modified residuei147 – 1471Phosphothreonine1 Publication
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP58335.
    PaxDbiP58335.
    PRIDEiP58335.

    PTM databases

    PhosphoSiteiP58335.

    Expressioni

    Tissue specificityi

    Expressed in prostate, thymus, ovary, testis, pancreas, colon, heart, kidney, lung, liver, peripheral blood leukocytes, placenta, skeletal muscle, small intestine and spleen.1 Publication

    Gene expression databases

    ArrayExpressiP58335.
    BgeeiP58335.
    CleanExiHS_ANTXR2.
    GenevestigatoriP58335.

    Interactioni

    Subunit structurei

    Binds laminin, and possibly also collagen type IV. Binds to the protective antigen (PA) of Bacillus anthracis in a divalent cation-dependent manner, with the following preference: calcium > manganese > magnesium > zinc. Binding of PA leads to heptamerization of the receptor-PA complex.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    pagAP134237EBI-456840,EBI-456868From a different organism.

    Protein-protein interaction databases

    BioGridi125602. 6 interactions.
    DIPiDIP-32476N.
    IntActiP58335. 3 interactions.
    MINTiMINT-1184613.
    STRINGi9606.ENSP00000306185.

    Structurei

    Secondary structure

    1
    489
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 508
    Helixi53 – 586
    Helixi59 – 7214
    Beta strandi78 – 9619
    Helixi99 – 11012
    Helixi120 – 13415
    Helixi136 – 1383
    Beta strandi141 – 1477
    Helixi155 – 16814
    Beta strandi172 – 1776
    Helixi183 – 1897
    Beta strandi190 – 1923
    Helixi193 – 1953
    Beta strandi196 – 2016
    Helixi204 – 21512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SHTX-ray1.81X38-217[»]
    1SHUX-ray1.50X38-218[»]
    1T6BX-ray2.50Y40-212[»]
    1TZNX-ray4.30a/b/c/d/e/f/g/h/i/j/k/l/m/o38-218[»]
    ProteinModelPortaliP58335.
    SMRiP58335. Positions 21-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP58335.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 318285ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini342 – 489148CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei319 – 34123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 213170VWFAPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi352 – 3609Poly-Pro
    Compositional biasi362 – 3665Poly-Glu

    Domaini

    Binding to PA seems to be effected through the VWA domain.

    Sequence similaritiesi

    Belongs to the ATR family.Curated
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41216.
    HOVERGENiHBG050514.
    InParanoidiP58335.
    OMAiGLMWWFW.
    OrthoDBiEOG7XWPN7.
    PhylomeDBiP58335.
    TreeFamiTF328943.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR017360. Anthrax_toxin_rcpt.
    IPR008399. Anthrax_toxin_rcpt_C.
    IPR008400. Anthrax_toxin_rcpt_extracel.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF05586. Ant_C. 1 hit.
    PF05587. Anth_Ig. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038023. Anthrax_toxin_receptor_2. 1 hit.
    ProDomiPD377005. Anthrax_toxin_rcpt_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P58335-1) [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

    MVAERSPARS PGSWLFPGLW LLVLSGPGGL LRAQEQPSCR RAFDLYFVLD    50
    KSGSVANNWI EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG 100
    KISKGLEDLK RVSPVGETYI HEGLKLANEQ IQKAGGLKTS SIIIALTDGK 150
    LDGLVPSYAE KEAKISRSLG ASVYCVGVLD FEQAQLERIA DSKEQVFPVK 200
    GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS GRGFMLGSRN 250
    GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG 300
    KSVISGSLIV TATECSNGIA AIIVILVLLL LLGIGLMWWF WPLCCKVVIK 350
    DPPPPPAPAP KEEEEEPLPT KKWPTVDASY YGGRGVGGIK RMEVRWGDKG 400
    STEEGARLEK AKNAVVKIPE ETEEPIRPRP PRPKPTHQPP QTKWYTPIKG 450
    RLDALWALLR RQYDRVSLMR PQEGDEVCIW ECIEKELTA 489
    Length:489
    Mass (Da):53,666
    Last modified:October 5, 2010 - v5
    Checksum:iB9F66CCE7A13F807
    GO
    Isoform 2 (identifier: P58335-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         213-315: Missing.

    Show »
    Length:386
    Mass (Da):42,893
    Checksum:i0F9B3873874FABCA
    GO
    Isoform 3 (identifier: P58335-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         290-322: TLDVSVSFNGGKSVISGSLIVTATECSNGIAAI → WGLTVTQAGVKWHDLTHCTFGLSGSGDPPTSAS
         323-489: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:322
    Mass (Da):34,763
    Checksum:i19D061AAFBE6CFF8
    GO
    Isoform 4 (identifier: P58335-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         477-489: VCIWECIEKELTA → GRCINFSRVPSQ

    Show »
    Length:488
    Mass (Da):53,493
    Checksum:i1FE0F51BE9FDE0F6
    GO

    Sequence cautioni

    The sequence BAB70976.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD93150.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAY40907.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451L → P in HFS; infantile form. 1 Publication
    VAR_022687
    Natural varianti105 – 1051G → D in HFS. 1 Publication
    VAR_022688
    Natural varianti189 – 1891I → T in HFS; infantile form. 2 Publications
    VAR_022689
    Natural varianti218 – 2181C → R in HFS; infantile form. 1 Publication
    VAR_022690
    Natural varianti293 – 2931V → VQ in HFS. 1 Publication
    VAR_022691
    Natural varianti329 – 3291L → R in HFS. 1 Publication
    VAR_022692
    Natural varianti357 – 3571A → P.5 Publications
    Corresponds to variant rs12647691 [ dbSNP | Ensembl ].
    VAR_022693
    Natural varianti381 – 3811Y → C in HFS. 1 Publication
    VAR_022694

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei213 – 315103Missing in isoform 2. 1 PublicationVSP_008343Add
    BLAST
    Alternative sequencei290 – 32233TLDVS…GIAAI → WGLTVTQAGVKWHDLTHCTF GLSGSGDPPTSAS in isoform 3. 1 PublicationVSP_008344Add
    BLAST
    Alternative sequencei323 – 489167Missing in isoform 3. 1 PublicationVSP_008345Add
    BLAST
    Alternative sequencei477 – 48913VCIWE…KELTA → GRCINFSRVPSQ in isoform 4. 4 PublicationsVSP_008346Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040326 mRNA. Translation: AAK77222.1.
    AY233452 mRNA. Translation: AAP04016.1.
    AK055636 mRNA. Translation: BAB70976.1. Different initiation.
    AK091721 mRNA. Translation: BAC03731.1.
    AB209913 mRNA. Translation: BAD93150.1. Different initiation.
    AC097711 Genomic DNA. Translation: AAY40907.1. Sequence problems.
    AC109518 Genomic DNA. No translation available.
    AC114773 Genomic DNA. No translation available.
    AL832851 mRNA. Translation: CAI46157.2.
    BC034001 mRNA. Translation: AAH34001.2.
    CCDSiCCDS47085.1. [P58335-4]
    CCDS47086.1. [P58335-1]
    RefSeqiNP_001139266.1. NM_001145794.1. [P58335-1]
    NP_001273709.1. NM_001286780.1.
    NP_001273710.1. NM_001286781.1.
    NP_477520.2. NM_058172.5. [P58335-4]
    UniGeneiHs.162963.

    Genome annotation databases

    EnsembliENST00000307333; ENSP00000306185; ENSG00000163297. [P58335-1]
    ENST00000346652; ENSP00000314883; ENSG00000163297. [P58335-2]
    ENST00000403729; ENSP00000385575; ENSG00000163297. [P58335-4]
    ENST00000449651; ENSP00000413700; ENSG00000163297.
    GeneIDi118429.
    KEGGihsa:118429.
    UCSCiuc003hly.4. human. [P58335-4]
    uc003hlz.4. human. [P58335-1]
    uc010ijn.3. human. [P58335-2]

    Polymorphism databases

    DMDMi306526289.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040326 mRNA. Translation: AAK77222.1 .
    AY233452 mRNA. Translation: AAP04016.1 .
    AK055636 mRNA. Translation: BAB70976.1 . Different initiation.
    AK091721 mRNA. Translation: BAC03731.1 .
    AB209913 mRNA. Translation: BAD93150.1 . Different initiation.
    AC097711 Genomic DNA. Translation: AAY40907.1 . Sequence problems.
    AC109518 Genomic DNA. No translation available.
    AC114773 Genomic DNA. No translation available.
    AL832851 mRNA. Translation: CAI46157.2 .
    BC034001 mRNA. Translation: AAH34001.2 .
    CCDSi CCDS47085.1. [P58335-4 ]
    CCDS47086.1. [P58335-1 ]
    RefSeqi NP_001139266.1. NM_001145794.1. [P58335-1 ]
    NP_001273709.1. NM_001286780.1.
    NP_001273710.1. NM_001286781.1.
    NP_477520.2. NM_058172.5. [P58335-4 ]
    UniGenei Hs.162963.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SHT X-ray 1.81 X 38-217 [» ]
    1SHU X-ray 1.50 X 38-218 [» ]
    1T6B X-ray 2.50 Y 40-212 [» ]
    1TZN X-ray 4.30 a/b/c/d/e/f/g/h/i/j/k/l/m/o 38-218 [» ]
    ProteinModelPortali P58335.
    SMRi P58335. Positions 21-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125602. 6 interactions.
    DIPi DIP-32476N.
    IntActi P58335. 3 interactions.
    MINTi MINT-1184613.
    STRINGi 9606.ENSP00000306185.

    PTM databases

    PhosphoSitei P58335.

    Polymorphism databases

    DMDMi 306526289.

    Proteomic databases

    MaxQBi P58335.
    PaxDbi P58335.
    PRIDEi P58335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307333 ; ENSP00000306185 ; ENSG00000163297 . [P58335-1 ]
    ENST00000346652 ; ENSP00000314883 ; ENSG00000163297 . [P58335-2 ]
    ENST00000403729 ; ENSP00000385575 ; ENSG00000163297 . [P58335-4 ]
    ENST00000449651 ; ENSP00000413700 ; ENSG00000163297 .
    GeneIDi 118429.
    KEGGi hsa:118429.
    UCSCi uc003hly.4. human. [P58335-4 ]
    uc003hlz.4. human. [P58335-1 ]
    uc010ijn.3. human. [P58335-2 ]

    Organism-specific databases

    CTDi 118429.
    GeneCardsi GC04M080822.
    GeneReviewsi ANTXR2.
    HGNCi HGNC:21732. ANTXR2.
    MIMi 228600. phenotype.
    608041. gene.
    neXtProti NX_P58335.
    Orphaneti 2176. Infantile systemic hyalinosis.
    2028. Juvenile hyaline fibromatosis.
    PharmGKBi PA128394752.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41216.
    HOVERGENi HBG050514.
    InParanoidi P58335.
    OMAi GLMWWFW.
    OrthoDBi EOG7XWPN7.
    PhylomeDBi P58335.
    TreeFami TF328943.

    Miscellaneous databases

    ChiTaRSi ANTXR2. human.
    EvolutionaryTracei P58335.
    GeneWikii ANTXR2.
    GenomeRNAii 118429.
    NextBioi 80274.
    PROi P58335.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P58335.
    Bgeei P58335.
    CleanExi HS_ANTXR2.
    Genevestigatori P58335.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR017360. Anthrax_toxin_rcpt.
    IPR008399. Anthrax_toxin_rcpt_C.
    IPR008400. Anthrax_toxin_rcpt_extracel.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF05586. Ant_C. 1 hit.
    PF05587. Anth_Ig. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038023. Anthrax_toxin_receptor_2. 1 hit.
    ProDomi PD377005. Anthrax_toxin_rcpt_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential gene expression during capillary morphogenesis in 3D collagen matrices: regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling."
      Bell S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S., Maxwell S.A., Davis G.E.
      J. Cell Sci. 114:2755-2773(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, VARIANT PRO-357.
    2. "Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor."
      Scobie H.M., Rainey G.J.A., Bradley K.A., Young J.A.T.
      Proc. Natl. Acad. Sci. U.S.A. 100:5170-5174(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ANTHRAX TOXIN, VARIANT PRO-357.
      Tissue: Placenta.
    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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-489 (ISOFORM 3).
      Tissue: Synovial cell.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT PRO-357.
      Tissue: Aortic endothelium.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-489 (ISOFORM 4).
      Tissue: Lymph node.
    7. "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] OF 248-489 (ISOFORM 4), VARIANT PRO-357.
      Tissue: Brain.
    8. "Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process."
      Abrami L., Liu S., Cosson P., Leppla S.H., van der Goot F.G.
      J. Cell Biol. 160:321-328(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANTHRAX TOXIN, CLATHRIN-DEPENDENT INTERNALIZATION.
    9. "Membrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathway."
      Abrami L., Lindsay M., Parton R.G., Leppla S.H., van der Goot F.G.
      J. Cell Biol. 166:645-651(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERNALIZATION.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Crystal structure of a complex between anthrax toxin and its host cell receptor."
      Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.
      Nature 430:905-908(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-212 OF COMPLEX WITH THE PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS.
    12. "Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor."
      Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., Collier R.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:6367-6372(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-217.
    13. "Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation."
      Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 38-218 OF COMPLEX WITH THE PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS.
    14. "Mutations in the gene encoding capillary morphogenesis protein 2 cause juvenile hyaline fibromatosis and infantile systemic hyalinosis."
      Hanks S., Adams S., Douglas J., Arbour L., Atherton D.J., Balci S., Bode H., Campbell M.E., Feingold M., Keser G., Kleijer W., Mancini G., McGrath J.A., Muntoni F., Nanda A., Teare M.D., Warman M., Pope F.M.
      , Superti-Furga A., Futreal P.A., Rahman N.
      Am. J. Hum. Genet. 73:791-800(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HFS PRO-45; THR-189; ARG-218; GLN-293 INS AND CYS-381, VARIANT PRO-357, TISSUE SPECIFICITY.
    15. "Mutations in capillary morphogenesis gene-2 result in the allelic disorders juvenile hyaline fibromatosis and infantile systemic hyalinosis."
      Dowling O., Difeo A., Ramirez M.C., Tukel T., Narla G., Bonafe L., Kayserili H., Yuksel-Apak M., Paller A.S., Norton K., Teebi A.S., Grum-Tokars V., Martin G.S., Davis G.E., Glucksman M.J., Martignetti J.A.
      Am. J. Hum. Genet. 73:957-966(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HFS ASP-105; THR-189 AND ARG-329, FUNCTION.
    16. "Capillary morphogenesis gene-2 mutation in infantile systemic hyalinosis: ultrastructural study and mutation analysis in a Taiwanese infant."
      Lee J.Y.-Y., Tsai Y.-M., Chao S.-C., Tu Y.-F.
      Clin. Exp. Dermatol. 30:176-179(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HFS.

    Entry informationi

    Entry nameiANTR2_HUMAN
    AccessioniPrimary (citable) accession number: P58335
    Secondary accession number(s): Q4W5H6
    , Q59E98, Q5JPE9, Q86UI1, Q8N4J8, Q8NB13, Q96NC7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 138 of the entry and version 5 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

    Miscellaneous

    Upon binding of the protective antigen (PA) of Bacillus anthracis the complex moves to glycosphingolipid-rich lipid rafts, where it is internalized via a clathrin-dependent pathway. In the endosomal membrane, at pH under 7, the complex then rearranges and forms a pore allowing the other components of anthrax toxin to escape to the cytoplasm.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3