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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)DescriptionActionsGraphical viewLength
Metal bindingi52Divalent metal cation1
Metal bindingi54Divalent metal cation1
Metal bindingi118Divalent metal cation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163297-MONOMER.
ReactomeiR-HSA-5210891. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:21732. ANTXR2.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini34 – 318ExtracellularSequence analysisAdd BLAST285
Transmembranei319 – 341HelicalSequence analysisAdd BLAST23
Topological domaini342 – 489CytoplasmicSequence analysisAdd BLAST148

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_02268745L → P in HFS; infantile form. 1 Publication1
Natural variantiVAR_022688105G → D in HFS. 1 PublicationCorresponds to variant rs137852902dbSNPEnsembl.1
Natural variantiVAR_022689189I → T in HFS; infantile form. 2 PublicationsCorresponds to variant rs137852905dbSNPEnsembl.1
Natural variantiVAR_022690218C → R in HFS; infantile form. 1 PublicationCorresponds to variant rs781637328dbSNPEnsembl.1
Natural variantiVAR_022691293V → VQ in HFS. 1 Publication1
Natural variantiVAR_022692329L → R in HFS. 1 PublicationCorresponds to variant rs137852903dbSNPEnsembl.1
Natural variantiVAR_022694381Y → C in HFS. 1 PublicationCorresponds to variant rs137852901dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi118429.
MalaCardsiANTXR2.
MIMi228600. phenotype.
OpenTargetsiENSG00000163297.
Orphaneti2176. Infantile systemic hyalinosis.
2028. Juvenile hyaline fibromatosis.
PharmGKBiPA128394752.

Polymorphism and mutation databases

BioMutaiANTXR2.
DMDMi306526289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000000269434 – 489Anthrax toxin receptor 2Add BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 218
Modified residuei147PhosphothreonineCombined sources1
Glycosylationi250N-linked (GlcNAc...)Sequence analysis1
Glycosylationi260N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP58335.
MaxQBiP58335.
PaxDbiP58335.
PeptideAtlasiP58335.
PRIDEiP58335.

PTM databases

iPTMnetiP58335.
PhosphoSitePlusiP58335.
SwissPalmiP58335.

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

BgeeiENSG00000163297.
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. 9 interactors.
DIPiDIP-32476N.
IntActiP58335. 3 interactors.
MINTiMINT-1184613.
STRINGi9606.ENSP00000306185.

Structurei

Secondary structure

1489
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 50Combined sources8
Helixi53 – 58Combined sources6
Helixi59 – 72Combined sources14
Beta strandi78 – 96Combined sources19
Helixi99 – 110Combined sources12
Helixi120 – 134Combined sources15
Helixi136 – 138Combined sources3
Beta strandi141 – 147Combined sources7
Helixi155 – 168Combined sources14
Beta strandi172 – 177Combined sources6
Helixi183 – 189Combined sources7
Beta strandi190 – 192Combined sources3
Helixi193 – 195Combined sources3
Beta strandi196 – 201Combined sources6
Helixi204 – 215Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58335.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 213VWFAPROSITE-ProRule annotationAdd BLAST170

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi352 – 360Poly-Pro9
Compositional biasi362 – 366Poly-Glu5

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

eggNOGiENOG410IK1W. Eukaryota.
ENOG410YC57. LUCA.
GeneTreeiENSGT00430000031214.
HOVERGENiHBG050514.
InParanoidiP58335.
OMAiGLMWWFW.
OrthoDBiEOG091G08TW.
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 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAB70976 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD93150 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02268745L → P in HFS; infantile form. 1 Publication1
Natural variantiVAR_022688105G → D in HFS. 1 PublicationCorresponds to variant rs137852902dbSNPEnsembl.1
Natural variantiVAR_022689189I → T in HFS; infantile form. 2 PublicationsCorresponds to variant rs137852905dbSNPEnsembl.1
Natural variantiVAR_022690218C → R in HFS; infantile form. 1 PublicationCorresponds to variant rs781637328dbSNPEnsembl.1
Natural variantiVAR_022691293V → VQ in HFS. 1 Publication1
Natural variantiVAR_022692329L → R in HFS. 1 PublicationCorresponds to variant rs137852903dbSNPEnsembl.1
Natural variantiVAR_022693357A → P.5 PublicationsCorresponds to variant rs12647691dbSNPEnsembl.1
Natural variantiVAR_022694381Y → C in HFS. 1 PublicationCorresponds to variant rs137852901dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008343213 – 315Missing in isoform 2. 1 PublicationAdd BLAST103
Alternative sequenceiVSP_008344290 – 322TLDVS…GIAAI → WGLTVTQAGVKWHDLTHCTF GLSGSGDPPTSAS in isoform 3. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_008345323 – 489Missing in isoform 3. 1 PublicationAdd BLAST167
Alternative sequenceiVSP_008346477 – 489VCIWE…KELTA → GRCINFSRVPSQ in isoform 4. 4 PublicationsAdd BLAST13

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.5. human. [P58335-1]

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125602. 9 interactors.
DIPiDIP-32476N.
IntActiP58335. 3 interactors.
MINTiMINT-1184613.
STRINGi9606.ENSP00000306185.

PTM databases

iPTMnetiP58335.
PhosphoSitePlusiP58335.
SwissPalmiP58335.

Polymorphism and mutation databases

BioMutaiANTXR2.
DMDMi306526289.

Proteomic databases

EPDiP58335.
MaxQBiP58335.
PaxDbiP58335.
PeptideAtlasiP58335.
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.5. human. [P58335-1]

Organism-specific databases

CTDi118429.
DisGeNETi118429.
GeneCardsiANTXR2.
GeneReviewsiANTXR2.
HGNCiHGNC:21732. ANTXR2.
MalaCardsiANTXR2.
MIMi228600. phenotype.
608041. gene.
neXtProtiNX_P58335.
OpenTargetsiENSG00000163297.
Orphaneti2176. Infantile systemic hyalinosis.
2028. Juvenile hyaline fibromatosis.
PharmGKBiPA128394752.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IK1W. Eukaryota.
ENOG410YC57. LUCA.
GeneTreeiENSGT00430000031214.
HOVERGENiHBG050514.
InParanoidiP58335.
OMAiGLMWWFW.
OrthoDBiEOG091G08TW.
PhylomeDBiP58335.
TreeFamiTF328943.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163297-MONOMER.
ReactomeiR-HSA-5210891. Uptake and function of anthrax toxins.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000163297.
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...

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: November 2, 2016
This is version 159 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

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 one 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.