Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anthrax toxin receptor 2

Gene

ANTXR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiREACT_264618. Uptake and function of anthrax toxins.

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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:21732. ANTXR2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 318285ExtracellularSequence AnalysisAdd
BLAST
Transmembranei319 – 34123HelicalSequence AnalysisAdd
BLAST
Topological domaini342 – 489148CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Hyaline fibromatosis syndrome (HFS)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:228600
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.

Polymorphism and mutation databases

BioMutaiANTXR2.
DMDMi306526289.

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

BgeeiP58335.
CleanExiHS_ANTXR2.
ExpressionAtlasiP58335. baseline and differential.
GenevisibleiP58335. HS.

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. 7 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 – 508Combined sources
Helixi53 – 586Combined sources
Helixi59 – 7214Combined sources
Beta strandi78 – 9619Combined sources
Helixi99 – 11012Combined sources
Helixi120 – 13415Combined sources
Helixi136 – 1383Combined sources
Beta strandi141 – 1477Combined sources
Helixi155 – 16814Combined sources
Beta strandi172 – 1776Combined sources
Helixi183 – 1897Combined sources
Beta strandi190 – 1923Combined sources
Helixi193 – 1953Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 21512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00430000031214.
HOVERGENiHBG050514.
InParanoidiP58335.
OMAiTATECSN.
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. AlignAdd to basket

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

        10         20         30         40         50
MVAERSPARS PGSWLFPGLW LLVLSGPGGL LRAQEQPSCR RAFDLYFVLD
60 70 80 90 100
KSGSVANNWI EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG
110 120 130 140 150
KISKGLEDLK RVSPVGETYI HEGLKLANEQ IQKAGGLKTS SIIIALTDGK
160 170 180 190 200
LDGLVPSYAE KEAKISRSLG ASVYCVGVLD FEQAQLERIA DSKEQVFPVK
210 220 230 240 250
GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS GRGFMLGSRN
260 270 280 290 300
GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG
310 320 330 340 350
KSVISGSLIV TATECSNGIA AIIVILVLLL LLGIGLMWWF WPLCCKVVIK
360 370 380 390 400
DPPPPPAPAP KEEEEEPLPT KKWPTVDASY YGGRGVGGIK RMEVRWGDKG
410 420 430 440 450
STEEGARLEK AKNAVVKIPE ETEEPIRPRP PRPKPTHQPP QTKWYTPIKG
460 470 480
RLDALWALLR RQYDRVSLMR PQEGDEVCIW ECIEKELTA
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 AAY40907.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAB70976.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD93150.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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]
GeneIDi118429.
KEGGihsa:118429.
UCSCiuc003hly.4. human. [P58335-4]
uc003hlz.4. human. [P58335-1]
uc010ijn.3. human. [P58335-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi125602. 7 interactions.
DIPiDIP-32476N.
IntActiP58335. 3 interactions.
MINTiMINT-1184613.
STRINGi9606.ENSP00000306185.

PTM databases

PhosphoSiteiP58335.

Polymorphism and mutation databases

BioMutaiANTXR2.
DMDMi306526289.

Proteomic databases

MaxQBiP58335.
PaxDbiP58335.
PRIDEiP58335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi118429.
GeneCardsiGC04M080822.
GeneReviewsiANTXR2.
HGNCiHGNC:21732. ANTXR2.
MIMi228600. phenotype.
608041. gene.
neXtProtiNX_P58335.
Orphaneti2176. Infantile systemic hyalinosis.
2028. Juvenile hyaline fibromatosis.
PharmGKBiPA128394752.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41216.
GeneTreeiENSGT00430000031214.
HOVERGENiHBG050514.
InParanoidiP58335.
OMAiTATECSN.
OrthoDBiEOG7XWPN7.
PhylomeDBiP58335.
TreeFamiTF328943.

Enzyme and pathway databases

ReactomeiREACT_264618. Uptake and function of anthrax toxins.

Miscellaneous databases

ChiTaRSiANTXR2. human.
EvolutionaryTraceiP58335.
GeneWikiiANTXR2.
GenomeRNAii118429.
NextBioi80274.
PROiP58335.
SOURCEiSearch...

Gene expression databases

BgeeiP58335.
CleanExiHS_ANTXR2.
ExpressionAtlasiP58335. baseline and differential.
GenevisibleiP58335. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.