P58335 (ANTR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthrax toxin receptor 2

Alternative name(s):
Capillary morphogenesis gene 2 protein
Short name=CMG-2

Gene names

Name:	ANTXR2
Synonyms:	CMG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	489 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Cellular component	Cell membrane Endoplasmic reticulum Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal Transmembrane Transmembrane helix
Ligand	Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	reproductive process Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
pagA	P13423	7	EBI-456840,EBI-456868	From 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

33

Potential

Chain

34 – 489

456

Anthrax toxin receptor 2

PRO_0000002694

Regions

Topological domain

34 – 318

285

Extracellular Potential

Transmembrane

319 – 341

23

Helical; Potential

Topological domain

342 – 489

148

Cytoplasmic Potential

Domain

44 – 213

170

VWFA

Compositional bias

352 – 360

9

Poly-Pro

Compositional bias

362 – 366

5

Poly-Glu

Sites

Metal binding

52

1

Divalent metal cation

Metal binding

54

1

Divalent metal cation

Metal binding

118

1

Divalent metal cation

Amino acid modifications

Modified residue

147

1

Phosphothreonine Ref.10

Glycosylation

250

1

N-linked (GlcNAc...) Potential

Glycosylation

260

1

N-linked (GlcNAc...) Potential

Disulfide bond

39 ↔ 218

Natural variations

Alternative sequence

213 – 315

103

Missing in isoform 2.

VSP_008343

Alternative sequence

290 – 322

33

TLDVS…GIAAI → WGLTVTQAGVKWHDLTHCTF GLSGSGDPPTSAS in isoform 3.

VSP_008344

Alternative sequence

323 – 489

167

Missing in isoform 3.

VSP_008345

Alternative sequence

477 – 489

13

VCIWE…KELTA → GRCINFSRVPSQ in isoform 4.

VSP_008346

Natural variant

45

1

L → P in HFS; infantile form. Ref.14

VAR_022687

Natural variant

105

1

G → D in HFS. Ref.15

VAR_022688

Natural variant

189

1

I → T in HFS; infantile form. Ref.14 Ref.15

VAR_022689

Natural variant

218

1

C → R in HFS; infantile form. Ref.14

VAR_022690

Natural variant

293

1

V → VQ in HFS. Ref.14

VAR_022691

Natural variant

329

1

L → R in HFS. Ref.15

VAR_022692

Natural variant

357

1

A → P. Ref.1 Ref.2 Ref.4 Ref.7 Ref.14
Corresponds to variant rs12647691 [ dbSNP | Ensembl ].

VAR_022693

Natural variant

381

1

Y → C in HFS. Ref.14

VAR_022694

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

489

Helix Strand Turn

Details...

Beta strand

43 – 50

8

Helix

53 – 58

6

Helix

59 – 72

14

Beta strand

78 – 96

19

Helix

99 – 110

12

Helix

120 – 134

15

Helix

136 – 138

3

Beta strand

141 – 147

7

Helix

155 – 168

14

Beta strand

172 – 177

6

Helix

183 – 189

7

Beta strand

190 – 192

3

Helix

193 – 195

3

Beta strand

196 – 201

6

Helix

204 – 215

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 5. Checksum: B9F66CCE7A13F807	FASTA	489	53,666
	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
	Isoform 2 [UniParc]. Checksum: 0F9B3873874FABCA	FASTA	386	42,893
	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 NSSNGIAAII VILVLLLLLG IGLMWWFWPL 250 260 270 280 290 300 CCKVVIKDPP PPPAPAPKEE EEEPLPTKKW PTVDASYYGG RGVGGIKRME VRWGDKGSTE 310 320 330 340 350 360 EGARLEKAKN AVVKIPEETE EPIRPRPPRP KPTHQPPQTK WYTPIKGRLD ALWALLRRQY 370 380 DRVSLMRPQE GDEVCIWECI EKELTA
	Isoform 3 [UniParc]. Checksum: 19D061AAFBE6CFF8	FASTA	322	34,763
	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 APILNKAGEW GLTVTQAGVK 310 320 WHDLTHCTFG LSGSGDPPTS AS
	Isoform 4 [UniParc]. Checksum: 1FE0F51BE9FDE0F6	FASTA	488	53,493
	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 PQEGDEGRCI NFSRVPSQ

References

	« Hide 'large scale' referencesShow '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. , 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]	"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, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00036552.
IPI00375552.
IPI00375555.
IPI00375556.

RefSeq

NP_001139266.1. NM_001145794.1.
NP_477520.2. NM_058172.5.

UniGene

Hs.162963.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P58335.

SMR

P58335. Positions 37-255.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32476N.

IntAct

P58335. 2 interactions.

MINT

MINT-1184613.

STRING

9606.ENSP00000306185.

PTM databases

PhosphoSite

P58335.

Polymorphism databases

DMDM

306526289.

Proteomic databases

PaxDb

P58335.

PRIDE

P58335.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295465; ENSP00000295465; ENSG00000163297.
ENST00000307333; ENSP00000306185; ENSG00000163297.
ENST00000346652; ENSP00000314883; ENSG00000163297.
ENST00000403729; ENSP00000385575; ENSG00000163297.
ENST00000449651; ENSP00000413700; ENSG00000163297.

GeneID

118429.

KEGG

hsa:118429.

UCSC

uc003hly.4. human.
uc003hlz.4. human.
uc010ijn.3. human.

Organism-specific databases

CTD

118429.

GeneCards

GC04M080822.

HGNC

HGNC:21732. ANTXR2.

MIM

228600. phenotype.
608041. gene.

neXtProt

NX_P58335.

Orphanet

2176. Infantile systemic hyalinosis.
2028. Juvenile hyaline fibromatosis.

PharmGKB

PA128394752.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41216.

HOVERGEN

HBG050514.

InParanoid

P58335.

OMA

QLTERFV.

Enzyme and pathway databases

Pathway_Interaction_DB

anthraxpathway. Cellular roles of Anthrax toxin.

Gene expression databases

Bgee

P58335.

CleanEx

HS_ANTXR2.

Genevestigator

P58335.

GermOnline

ENSG00000163297. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR017360. Anthrax_toxin_rcpt.
IPR008399. Anthrax_toxin_rcpt_C.
IPR008400. Anthrax_toxin_rcpt_extracel.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF05586. Ant_C. 1 hit.
PF05587. Anth_Ig. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

PIRSF

PIRSF038023. Anthrax_toxin_receptor_2. 1 hit.

ProDom

PD377005. Anthrax_toxin_rcpt_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00327. VWA. 1 hit.
[Graphical view]

PROSITE

PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ANTXR2. human.

EvolutionaryTrace

P58335.

GenomeRNAi

118429.

NextBio

80274.

SOURCE

Search...

Entry information

Entry name

ANTR2_HUMAN

Accession

Primary (citable) accession number: P58335
Secondary accession number(s): Q4W5H6 , Q59E98, Q5JPE9, Q86UI1, Q8N4J8, Q8NB13, Q96NC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	October 5, 2010
Last modified:	May 29, 2013
This is version 124 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.