ANTR2_HUMAN
ID ANTR2_HUMAN Reviewed; 489 AA.
AC P58335; Q4W5H6; Q59E98; Q5JPE9; Q86UI1; Q8N4J8; Q8NB13; Q96NC7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 5.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Anthrax toxin receptor 2 {ECO:0000305};
DE AltName: Full=Capillary morphogenesis gene 2 protein {ECO:0000303|PubMed:11683410};
DE Short=CMG-2 {ECO:0000303|PubMed:11683410};
DE Flags: Precursor;
GN Name=ANTXR2 {ECO:0000312|HGNC:HGNC:21732};
GN Synonyms=CMG2 {ECO:0000303|PubMed:11683410};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP VARIANT PRO-357.
RX PubMed=11683410; DOI=10.1242/jcs.114.15.2755;
RA Bell S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S., Maxwell S.A.,
RA Davis G.E.;
RT "Differential gene expression during capillary morphogenesis in 3D collagen
RT matrices: regulated expression of genes involved in basement membrane
RT matrix assembly, cell cycle progression, cellular differentiation and G-
RT protein signaling.";
RL J. Cell Sci. 114:2755-2773(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, INTERACTION WITH ANTHRAX TOXIN PA (MICROBIAL
RP INFECTION), AND VARIANT PRO-357.
RC TISSUE=Placenta;
RX PubMed=12700348; DOI=10.1073/pnas.0431098100;
RA Scobie H.M., Rainey G.J.A., Bradley K.A., Young J.A.T.;
RT "Human capillary morphogenesis protein 2 functions as an anthrax toxin
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5170-5174(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 63-489 (ISOFORM 3).
RC TISSUE=Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT PRO-357.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-489 (ISOFORM 4).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-489 (ISOFORM 4), AND VARIANT
RP PRO-357.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ANTHRAX TOXIN PA
RP (MICROBIAL INFECTION).
RX PubMed=12551953; DOI=10.1083/jcb.200211018;
RA Abrami L., Liu S., Cosson P., Leppla S.H., van der Goot F.G.;
RT "Anthrax toxin triggers endocytosis of its receptor via a lipid raft-
RT mediated clathrin-dependent process.";
RL J. Cell Biol. 160:321-328(2003).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ANTHRAX TOXIN PA
RP (MICROBIAL INFECTION).
RX PubMed=15337774; DOI=10.1083/jcb.200312072;
RA Abrami L., Lindsay M., Parton R.G., Leppla S.H., van der Goot F.G.;
RT "Membrane insertion of anthrax protective antigen and cytoplasmic delivery
RT of lethal factor occur at different stages of the endocytic pathway.";
RL J. Cell Biol. 166:645-651(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11] {ECO:0007744|PDB:1T6B}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-212 IN COMPLEX WITH THE
RP PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS AND MANGANESE, FUNCTION (MICROBIAL
RP INFECTION), AND INTERACTION WITH ANTHRAX TOXIN PA (MICROBIAL INFECTION).
RX PubMed=15243628; DOI=10.1038/nature02763;
RA Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.;
RT "Crystal structure of a complex between anthrax toxin and its host cell
RT receptor.";
RL Nature 430:905-908(2004).
RN [12] {ECO:0007744|PDB:1SHT, ECO:0007744|PDB:1SHU}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-217 IN COMPLEX WITH MAGNESIUM,
RP AND DISULFIDE BOND.
RX PubMed=15079089; DOI=10.1073/pnas.0401506101;
RA Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., Collier R.J.;
RT "Crystal structure of the von Willebrand factor A domain of human capillary
RT morphogenesis protein 2: an anthrax toxin receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6367-6372(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 38-218 OF COMPLEX WITH THE
RP PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS, FUNCTION (MICROBIAL INFECTION),
RP AND INTERACTION WITH ANTHRAX TOXIN PA (MICROBIAL INFECTION).
RX PubMed=15326297; DOI=10.1073/pnas.0405405101;
RA Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.;
RT "Structure of heptameric protective antigen bound to an anthrax toxin
RT receptor: a role for receptor in pH-dependent pore formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004).
RN [14]
RP VARIANTS HFS PRO-45; THR-189; ARG-218; GLN-293 INS AND CYS-381, VARIANT
RP PRO-357, AND TISSUE SPECIFICITY.
RX PubMed=14508707; DOI=10.1086/378418;
RA Hanks S., Adams S., Douglas J., Arbour L., Atherton D.J., Balci S.,
RA Bode H., Campbell M.E., Feingold M., Keser G., Kleijer W., Mancini G.,
RA McGrath J.A., Muntoni F., Nanda A., Teare M.D., Warman M., Pope F.M.,
RA Superti-Furga A., Futreal P.A., Rahman N.;
RT "Mutations in the gene encoding capillary morphogenesis protein 2 cause
RT juvenile hyaline fibromatosis and infantile systemic hyalinosis.";
RL Am. J. Hum. Genet. 73:791-800(2003).
RN [15]
RP VARIANTS HFS ASP-105; THR-189 AND ARG-329, AND FUNCTION.
RX PubMed=12973667; DOI=10.1086/378781;
RA Dowling O., Difeo A., Ramirez M.C., Tukel T., Narla G., Bonafe L.,
RA Kayserili H., Yuksel-Apak M., Paller A.S., Norton K., Teebi A.S.,
RA Grum-Tokars V., Martin G.S., Davis G.E., Glucksman M.J., Martignetti J.A.;
RT "Mutations in capillary morphogenesis gene-2 result in the allelic
RT disorders juvenile hyaline fibromatosis and infantile systemic
RT hyalinosis.";
RL Am. J. Hum. Genet. 73:957-966(2003).
RN [16]
RP INVOLVEMENT IN HFS.
RX PubMed=15725249; DOI=10.1111/j.1365-2230.2004.01698.x;
RA Lee J.Y.-Y., Tsai Y.-M., Chao S.-C., Tu Y.-F.;
RT "Capillary morphogenesis gene-2 mutation in infantile systemic hyalinosis:
RT ultrastructural study and mutation analysis in a Taiwanese infant.";
RL Clin. Exp. Dermatol. 30:176-179(2005).
CC -!- FUNCTION: Necessary for cellular interactions with laminin and the
CC extracellular matrix. {ECO:0000269|PubMed:11683410,
CC ECO:0000269|PubMed:12973667}.
CC -!- FUNCTION: (Microbial infection) Receptor for the protective antigen
CC (PA) of B.anthracis (PubMed:12700348, PubMed:15243628,
CC PubMed:15326297). Binding of PA leads to heptamerization of the
CC receptor-PA complex (PubMed:12700348, PubMed:15243628,
CC PubMed:15326297). Upon binding of the PA of B.anthracis, the complex
CC moves to glycosphingolipid-rich lipid rafts, where it is internalized
CC via a clathrin-dependent pathway (PubMed:12551953, PubMed:15337774). In
CC the endosomal membrane, at pH under 7, the complex then rearranges and
CC forms a pore allowing the other components of anthrax toxin to escape
CC to the cytoplasm (PubMed:12551953, PubMed:15337774).
CC {ECO:0000269|PubMed:12551953, ECO:0000269|PubMed:12700348,
CC ECO:0000269|PubMed:15243628, ECO:0000269|PubMed:15326297,
CC ECO:0000269|PubMed:15337774}.
CC -!- SUBUNIT: Binds laminin, and possibly also collagen type IV.
CC {ECO:0000269|PubMed:11683410}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via VWFA domain) with the
CC protective antigen (PA) of B.anthracis. {ECO:0000269|PubMed:12551953,
CC ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:15243628,
CC ECO:0000269|PubMed:15326297, ECO:0000269|PubMed:15337774}.
CC -!- INTERACTION:
CC P58335; P13423: pagA; Xeno; NbExp=7; IntAct=EBI-456840, EBI-456868;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:12700348}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Expressed at the cell surface.
CC {ECO:0000269|PubMed:12700348}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11683410}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Expressed predominantly within the endoplasmic
CC reticulum and not at the plasma membrane.
CC {ECO:0000269|PubMed:11683410}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P58335-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58335-2; Sequence=VSP_008343;
CC Name=3;
CC IsoId=P58335-3; Sequence=VSP_008344, VSP_008345;
CC Name=4;
CC IsoId=P58335-4; Sequence=VSP_008346;
CC -!- TISSUE SPECIFICITY: Expressed in prostate, thymus, ovary, testis,
CC pancreas, colon, heart, kidney, lung, liver, peripheral blood
CC leukocytes, placenta, skeletal muscle, small intestine and spleen.
CC {ECO:0000269|PubMed:14508707}.
CC -!- DISEASE: Hyaline fibromatosis syndrome (HFS) [MIM:228600]: An autosomal
CC recessive syndrome characterized by abnormal growth of hyalinized
CC fibrous tissue usually affecting subcutaneous regions on the scalp,
CC ears, neck, face, hands, and feet. The lesions appear as pearly papules
CC or fleshy nodules. Additional features include gingival hypertrophy,
CC progressive joint contractures resulting in severe limitation of
CC mobility, osteopenia, and osteoporosis. Disease severity is variable.
CC Some individuals manifest symptoms in infancy and have additional
CC visceral or systemic involvement. Hyaline deposits in multiple organs,
CC recurrent infections and intractable diarrhea often lead to early
CC death. Surviving children may suffer from severely reduced mobility due
CC to joint contractures. Other patients have later onset of a milder
CC disorder affecting only the face and digits.
CC {ECO:0000269|PubMed:12973667, ECO:0000269|PubMed:14508707,
CC ECO:0000269|PubMed:15725249}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY40907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB70976.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD93150.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY040326; AAK77222.1; -; mRNA.
DR EMBL; AY233452; AAP04016.1; -; mRNA.
DR EMBL; AK055636; BAB70976.1; ALT_INIT; mRNA.
DR EMBL; AK091721; BAC03731.1; -; mRNA.
DR EMBL; AB209913; BAD93150.1; ALT_INIT; mRNA.
DR EMBL; AC097711; AAY40907.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC109518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL832851; CAI46157.2; -; mRNA.
DR EMBL; BC034001; AAH34001.2; -; mRNA.
DR CCDS; CCDS47085.1; -. [P58335-4]
DR CCDS; CCDS47086.1; -. [P58335-1]
DR RefSeq; NP_001139266.1; NM_001145794.1. [P58335-1]
DR RefSeq; NP_001273709.1; NM_001286780.1.
DR RefSeq; NP_001273710.1; NM_001286781.1.
DR RefSeq; NP_477520.2; NM_058172.5. [P58335-4]
DR PDB; 1SHT; X-ray; 1.81 A; X=38-217.
DR PDB; 1SHU; X-ray; 1.50 A; X=38-218.
DR PDB; 1T6B; X-ray; 2.50 A; Y=40-212.
DR PDB; 1TZN; X-ray; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/o=38-218.
DR PDB; 7N1O; X-ray; 2.77 A; A=42-217.
DR PDBsum; 1SHT; -.
DR PDBsum; 1SHU; -.
DR PDBsum; 1T6B; -.
DR PDBsum; 1TZN; -.
DR PDBsum; 7N1O; -.
DR AlphaFoldDB; P58335; -.
DR SMR; P58335; -.
DR BioGRID; 125602; 17.
DR DIP; DIP-32476N; -.
DR IntAct; P58335; 8.
DR MINT; P58335; -.
DR STRING; 9606.ENSP00000306185; -.
DR BindingDB; P58335; -.
DR ChEMBL; CHEMBL4296326; -.
DR DrugBank; DB05945; MDX-1303.
DR GlyGen; P58335; 2 sites.
DR iPTMnet; P58335; -.
DR PhosphoSitePlus; P58335; -.
DR SwissPalm; P58335; -.
DR BioMuta; ANTXR2; -.
DR DMDM; 306526289; -.
DR EPD; P58335; -.
DR jPOST; P58335; -.
DR MassIVE; P58335; -.
DR MaxQB; P58335; -.
DR PaxDb; P58335; -.
DR PeptideAtlas; P58335; -.
DR PRIDE; P58335; -.
DR ProteomicsDB; 57060; -. [P58335-1]
DR ProteomicsDB; 57061; -. [P58335-2]
DR ProteomicsDB; 57062; -. [P58335-3]
DR ProteomicsDB; 57063; -. [P58335-4]
DR Antibodypedia; 24968; 191 antibodies from 34 providers.
DR DNASU; 118429; -.
DR Ensembl; ENST00000307333.7; ENSP00000306185.6; ENSG00000163297.18. [P58335-1]
DR Ensembl; ENST00000346652.10; ENSP00000314883.6; ENSG00000163297.18. [P58335-2]
DR Ensembl; ENST00000403729.7; ENSP00000385575.2; ENSG00000163297.18. [P58335-4]
DR Ensembl; ENST00000681115.1; ENSP00000505618.1; ENSG00000163297.18. [P58335-4]
DR GeneID; 118429; -.
DR KEGG; hsa:118429; -.
DR MANE-Select; ENST00000403729.7; ENSP00000385575.2; NM_058172.6; NP_477520.2. [P58335-4]
DR UCSC; uc003hly.5; human. [P58335-1]
DR CTD; 118429; -.
DR DisGeNET; 118429; -.
DR GeneCards; ANTXR2; -.
DR GeneReviews; ANTXR2; -.
DR HGNC; HGNC:21732; ANTXR2.
DR HPA; ENSG00000163297; Low tissue specificity.
DR MalaCards; ANTXR2; -.
DR MIM; 228600; phenotype.
DR MIM; 608041; gene.
DR neXtProt; NX_P58335; -.
DR OpenTargets; ENSG00000163297; -.
DR Orphanet; 2176; Infantile systemic hyalinosis.
DR Orphanet; 2028; Juvenile hyaline fibromatosis.
DR PharmGKB; PA128394752; -.
DR VEuPathDB; HostDB:ENSG00000163297; -.
DR eggNOG; ENOG502QT7Y; Eukaryota.
DR GeneTree; ENSGT00940000156320; -.
DR HOGENOM; CLU_029760_0_0_1; -.
DR InParanoid; P58335; -.
DR OMA; QAENKWY; -.
DR OrthoDB; 613698at2759; -.
DR PhylomeDB; P58335; -.
DR TreeFam; TF328943; -.
DR PathwayCommons; P58335; -.
DR Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
DR SignaLink; P58335; -.
DR BioGRID-ORCS; 118429; 19 hits in 1084 CRISPR screens.
DR ChiTaRS; ANTXR2; human.
DR EvolutionaryTrace; P58335; -.
DR GeneWiki; ANTXR2; -.
DR GenomeRNAi; 118429; -.
DR Pharos; P58335; Tchem.
DR PRO; PR:P58335; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P58335; protein.
DR Bgee; ENSG00000163297; Expressed in mucosa of stomach and 175 other tissues.
DR ExpressionAtlas; P58335; baseline and differential.
DR Genevisible; P58335; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR017360; Anthrax_toxin_rcpt.
DR InterPro; IPR008399; Anthrax_toxin_rcpt_C.
DR InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR16059:SF13; PTHR16059:SF13; 1.
DR Pfam; PF05586; Ant_C; 1.
DR Pfam; PF05587; Anth_Ig; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF038023; Anthrax_toxin_receptor_2; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..489
FT /note="Anthrax toxin receptor 2"
FT /id="PRO_0000002694"
FT TOPO_DOM 34..318
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..213
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 419..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15079089,
FT ECO:0007744|PDB:1SHU, ECO:0007744|PDB:1T6B"
FT BINDING 54
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15079089,
FT ECO:0007744|PDB:1SHU, ECO:0007744|PDB:1T6B"
FT BINDING 118
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:15079089,
FT ECO:0007744|PDB:1SHU, ECO:0007744|PDB:1T6B"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..218
FT /evidence="ECO:0000269|PubMed:15079089"
FT VAR_SEQ 213..315
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11683410"
FT /id="VSP_008343"
FT VAR_SEQ 290..322
FT /note="TLDVSVSFNGGKSVISGSLIVTATECSNGIAAI -> WGLTVTQAGVKWHDL
FT THCTFGLSGSGDPPTSAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008344"
FT VAR_SEQ 323..489
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008345"
FT VAR_SEQ 477..489
FT /note="VCIWECIEKELTA -> GRCINFSRVPSQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.4"
FT /id="VSP_008346"
FT VARIANT 45
FT /note="L -> P (in HFS; infantile form; dbSNP:rs886041401)"
FT /evidence="ECO:0000269|PubMed:14508707"
FT /id="VAR_022687"
FT VARIANT 105
FT /note="G -> D (in HFS; dbSNP:rs137852902)"
FT /evidence="ECO:0000269|PubMed:12973667"
FT /id="VAR_022688"
FT VARIANT 189
FT /note="I -> T (in HFS; infantile form; dbSNP:rs137852905)"
FT /evidence="ECO:0000269|PubMed:12973667,
FT ECO:0000269|PubMed:14508707"
FT /id="VAR_022689"
FT VARIANT 218
FT /note="C -> R (in HFS; infantile form; dbSNP:rs781637328)"
FT /evidence="ECO:0000269|PubMed:14508707"
FT /id="VAR_022690"
FT VARIANT 293
FT /note="V -> VQ (in HFS)"
FT /evidence="ECO:0000269|PubMed:14508707"
FT /id="VAR_022691"
FT VARIANT 329
FT /note="L -> R (in HFS; dbSNP:rs137852903)"
FT /evidence="ECO:0000269|PubMed:12973667"
FT /id="VAR_022692"
FT VARIANT 357
FT /note="A -> P (in dbSNP:rs12647691)"
FT /evidence="ECO:0000269|PubMed:11683410,
FT ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:14508707,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_022693"
FT VARIANT 381
FT /note="Y -> C (in HFS; dbSNP:rs137852901)"
FT /evidence="ECO:0000269|PubMed:14508707"
FT /id="VAR_022694"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:1SHU"
FT STRAND 78..96
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1SHU"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:1SHU"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:1SHU"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1SHU"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1SHU"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:1SHU"
SQ SEQUENCE 489 AA; 53666 MW; B9F66CCE7A13F807 CRC64;
MVAERSPARS PGSWLFPGLW LLVLSGPGGL LRAQEQPSCR RAFDLYFVLD KSGSVANNWI
EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG KISKGLEDLK RVSPVGETYI
HEGLKLANEQ IQKAGGLKTS SIIIALTDGK LDGLVPSYAE KEAKISRSLG ASVYCVGVLD
FEQAQLERIA DSKEQVFPVK GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS
GRGFMLGSRN GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG
KSVISGSLIV TATECSNGIA AIIVILVLLL LLGIGLMWWF WPLCCKVVIK DPPPPPAPAP
KEEEEEPLPT KKWPTVDASY YGGRGVGGIK RMEVRWGDKG STEEGARLEK AKNAVVKIPE
ETEEPIRPRP PRPKPTHQPP QTKWYTPIKG RLDALWALLR RQYDRVSLMR PQEGDEVCIW
ECIEKELTA
