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P58335 (ANTR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anthrax toxin receptor 2
Alternative name(s):
Capillary morphogenesis gene 2 protein
Short name=CMG-2
Gene names
Name:ANTXR2
Synonyms:CMG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Necessary for cellular interactions with laminin and the extracellular matrix. Ref.1 Ref.15

Subunit structure

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.

Subcellular location

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.

Isoform 3: Secreted.

Tissue specificity

Expressed in prostate, thymus, ovary, testis, pancreas, colon, heart, kidney, lung, liver, peripheral blood leukocytes, placenta, skeletal muscle, small intestine and spleen. Ref.14

Domain

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16

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.

Sequence similarities

Belongs to the ATR family.

Contains 1 VWFA domain.

Sequence caution

The sequence AAY40907.1 differs from that shown. Reason: Erroneous gene model prediction.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pagAP134237EBI-456840,EBI-456868From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P58335-1)

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.
Isoform 2 (identifier: P58335-2)

The sequence of this isoform differs from the canonical sequence as follows:
     213-315: Missing.
Isoform 3 (identifier: P58335-3)

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.
Isoform 4 (identifier: P58335-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 489456Anthrax toxin receptor 2
PRO_0000002694

Regions

Topological domain34 – 318285Extracellular Potential
Transmembrane319 – 34123Helical; Potential
Topological domain342 – 489148Cytoplasmic Potential
Domain44 – 213170VWFA
Compositional bias352 – 3609Poly-Pro
Compositional bias362 – 3665Poly-Glu

Sites

Metal binding521Divalent metal cation
Metal binding541Divalent metal cation
Metal binding1181Divalent metal cation

Amino acid modifications

Modified residue1471Phosphothreonine Ref.10
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Disulfide bond39 ↔ 218

Natural variations

Alternative sequence213 – 315103Missing in isoform 2.
VSP_008343
Alternative sequence290 – 32233TLDVS…GIAAI → WGLTVTQAGVKWHDLTHCTF GLSGSGDPPTSAS in isoform 3.
VSP_008344
Alternative sequence323 – 489167Missing in isoform 3.
VSP_008345
Alternative sequence477 – 48913VCIWE…KELTA → GRCINFSRVPSQ in isoform 4.
VSP_008346
Natural variant451L → P in HFS; infantile form. Ref.14
VAR_022687
Natural variant1051G → D in HFS. Ref.15
VAR_022688
Natural variant1891I → T in HFS; infantile form. Ref.14 Ref.15
VAR_022689
Natural variant2181C → R in HFS; infantile form. Ref.14
VAR_022690
Natural variant2931V → VQ in HFS. Ref.14
VAR_022691
Natural variant3291L → R in HFS. Ref.15
VAR_022692
Natural variant3571A → P. Ref.1 Ref.2 Ref.4 Ref.7 Ref.14
Corresponds to variant rs12647691 [ dbSNP | Ensembl ].
VAR_022693
Natural variant3811Y → C in HFS. Ref.14
VAR_022694

Secondary structure

........................... 489
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 5.
Checksum: B9F66CCE7A13F807

FASTA48953,666
        10         20         30         40         50         60 
MVAERSPARS PGSWLFPGLW LLVLSGPGGL LRAQEQPSCR RAFDLYFVLD KSGSVANNWI 

        70         80         90        100        110        120 
EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG KISKGLEDLK RVSPVGETYI 

       130        140        150        160        170        180 
HEGLKLANEQ IQKAGGLKTS SIIIALTDGK LDGLVPSYAE KEAKISRSLG ASVYCVGVLD 

       190        200        210        220        230        240 
FEQAQLERIA DSKEQVFPVK GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS 

       250        260        270        280        290        300 
GRGFMLGSRN GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG 

       310        320        330        340        350        360 
KSVISGSLIV TATECSNGIA AIIVILVLLL LLGIGLMWWF WPLCCKVVIK DPPPPPAPAP 

       370        380        390        400        410        420 
KEEEEEPLPT KKWPTVDASY YGGRGVGGIK RMEVRWGDKG STEEGARLEK AKNAVVKIPE 

       430        440        450        460        470        480 
ETEEPIRPRP PRPKPTHQPP QTKWYTPIKG RLDALWALLR RQYDRVSLMR PQEGDEVCIW 


ECIEKELTA 

« Hide

Isoform 2 [UniParc].

Checksum: 0F9B3873874FABCA
Show »

FASTA38642,893
Isoform 3 [UniParc].

Checksum: 19D061AAFBE6CFF8
Show »

FASTA32234,763
Isoform 4 [UniParc].

Checksum: 1FE0F51BE9FDE0F6
Show »

FASTA48853,493

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47085.1. [P58335-4]
CCDS47086.1. [P58335-1]
RefSeqNP_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]
UniGeneHs.162963.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP58335.
SMRP58335. Positions 21-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125602. 5 interactions.
DIPDIP-32476N.
IntActP58335. 3 interactions.
MINTMINT-1184613.
STRING9606.ENSP00000306185.

PTM databases

PhosphoSiteP58335.

Polymorphism databases

DMDM306526289.

Proteomic databases

MaxQBP58335.
PaxDbP58335.
PRIDEP58335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295465; ENSP00000295465; ENSG00000163297. [P58335-3]
ENST00000307333; ENSP00000306185; ENSG00000163297. [P58335-1]
ENST00000346652; ENSP00000314883; ENSG00000163297. [P58335-2]
ENST00000403729; ENSP00000385575; ENSG00000163297. [P58335-4]
ENST00000449651; ENSP00000413700; ENSG00000163297.
GeneID118429.
KEGGhsa:118429.
UCSCuc003hly.4. human. [P58335-4]
uc003hlz.4. human. [P58335-1]
uc010ijn.3. human. [P58335-2]

Organism-specific databases

CTD118429.
GeneCardsGC04M080822.
GeneReviewsANTXR2.
HGNCHGNC:21732. ANTXR2.
MIM228600. phenotype.
608041. gene.
neXtProtNX_P58335.
Orphanet2176. Infantile systemic hyalinosis.
2028. Juvenile hyaline fibromatosis.
PharmGKBPA128394752.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41216.
HOVERGENHBG050514.
InParanoidP58335.
OMAGLMWWFW.
OrthoDBEOG7XWPN7.
PhylomeDBP58335.
TreeFamTF328943.

Gene expression databases

ArrayExpressP58335.
BgeeP58335.
CleanExHS_ANTXR2.
GenevestigatorP58335.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR017360. Anthrax_toxin_rcpt.
IPR008399. Anthrax_toxin_rcpt_C.
IPR008400. Anthrax_toxin_rcpt_extracel.
IPR002035. VWF_A.
[Graphical view]
PfamPF05586. Ant_C. 1 hit.
PF05587. Anth_Ig. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF038023. Anthrax_toxin_receptor_2. 1 hit.
ProDomPD377005. Anthrax_toxin_rcpt_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANTXR2. human.
EvolutionaryTraceP58335.
GeneWikiANTXR2.
GenomeRNAi118429.
NextBio80274.
PROP58335.
SOURCESearch...

Entry information

Entry nameANTR2_HUMAN
AccessionPrimary (citable) accession number: P58335
Secondary accession number(s): Q4W5H6 expand/collapse secondary AC list , Q59E98, Q5JPE9, Q86UI1, Q8N4J8, Q8NB13, Q96NC7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 136 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM