ANTR1_HUMAN
ID ANTR1_HUMAN Reviewed; 564 AA.
AC Q9H6X2; A8K7U8; J7K7G4; J7KF88; Q4ZFV6; Q53QD8; Q96P02; Q9NVP3;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Anthrax toxin receptor 1 {ECO:0000305};
DE AltName: Full=Tumor endothelial marker 8 {ECO:0000303|PubMed:10947988};
DE Flags: Precursor;
GN Name=ANTXR1 {ECO:0000303|PubMed:22912819, ECO:0000312|HGNC:HGNC:21014};
GN Synonyms=ATR {ECO:0000303|PubMed:11700562},
GN TEM8 {ECO:0000303|PubMed:10947988};
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 1).
RX PubMed=10947988; DOI=10.1126/science.289.5482.1197;
RA St Croix B., Rago C., Velculescu V.E., Traverso G., Romans K.E.,
RA Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B.,
RA Kinzler K.W.;
RT "Genes expressed in human tumor endothelium.";
RL Science 289:1197-1202(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (MICROBIAL INFECTION), AND
RP INTERACTION WITH ANTHRAX TOXIN PA (MICROBIAL INFECTION).
RX PubMed=11700562; DOI=10.1038/n35101999;
RA Bradley K.A., Mogridge J., Mourez M., Collier R.J., Young J.A.T.;
RT "Identification of the cellular receptor for anthrax toxin.";
RL Nature 414:225-229(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND ALTERNATIVE SPLICING.
RC TISSUE=Brain, and Prostate;
RX PubMed=22912819; DOI=10.1371/journal.pone.0043174;
RA Vargas M., Karamsetty R., Leppla S.H., Chaudry G.J.;
RT "Broad expression analysis of human ANTXR1/TEM8 transcripts reveals
RT differential expression and novel splizce variants.";
RL PLoS ONE 7:E43174-E43174(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-564 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT LYS-7.
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 [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] (ISOFORM 4).
RC TISSUE=Kidney;
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 [7]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ANTHRAX TOXIN PA
RP (MICROBIAL INFECTION).
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 [8]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [9]
RP FUNCTION, INDUCTION, INTERACTION WITH TYPE 1 COLLAGEN AND GELATIN, AND
RP TISSUE SPECIFICITY.
RX PubMed=15777794; DOI=10.1016/j.yexcr.2004.12.025;
RA Hotchkiss K.A., Basile C.M., Spring S.C., Bonuccelli G., Lisanti M.P.,
RA Terman B.I.;
RT "TEM8 expression stimulates endothelial cell adhesion and migration by
RT regulating cell-matrix interactions on collagen.";
RL Exp. Cell Res. 305:133-144(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TYPE 1 COLLAGEN AND THE
RP ACTIN CYTOSKELETON, FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH
RP ANTHRAX TOXIN PA (MICROBIAL INFECTION).
RX PubMed=16762926; DOI=10.1074/jbc.m603676200;
RA Werner E., Kowalczyk A.P., Faundez V.;
RT "Anthrax toxin receptor 1/tumor endothelium marker 8 mediates cell
RT spreading by coupling extracellular ligands to the actin cytoskeleton.";
RL J. Biol. Chem. 281:23227-23236(2006).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [13]
RP INVOLVEMENT IN GAPOS.
RX PubMed=23602711; DOI=10.1016/j.ajhg.2013.03.023;
RA Stranecky V., Hoischen A., Hartmannova H., Zaki M.S., Chaudhary A.,
RA Zudaire E., Noskova L., Baresova V., Pristoupilova A., Hodanova K.,
RA Sovova J., Hulkova H., Piherova L., Hehir-Kwa J.Y., de Silva D.,
RA Senanayake M.P., Farrag S., Zeman J., Martasek P., Baxova A., Afifi H.H.,
RA St Croix B., Brunner H.G., Temtamy S., Kmoch S.;
RT "Mutations in ANTXR1 cause GAPO syndrome.";
RL Am. J. Hum. Genet. 92:792-799(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-220 IN COMPLEX WITH MAGNESIUM,
RP SUBUNIT, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH ANTHRAX TOXIN PA
RP (MICROBIAL INFECTION), AND DISULFIDE BOND.
RX PubMed=20585457; DOI=10.1371/journal.pone.0011203;
RA Fu S., Tong X., Cai C., Zhao Y., Wu Y., Li Y., Xu J., Zhang X.C., Xu L.,
RA Chen W., Rao Z.;
RT "The structure of tumor endothelial marker 8 (TEM8) extracellular domain
RT and implications for its receptor function for recognizing anthrax toxin.";
RL PLoS ONE 5:E11203-E11203(2010).
RN [15]
RP VARIANT HCI SUSCEPTIBILITY THR-326.
RX PubMed=18931684; DOI=10.1038/nm.1877;
RA Jinnin M., Medici D., Park L., Limaye N., Liu Y., Boscolo E., Bischoff J.,
RA Vikkula M., Boye E., Olsen B.R.;
RT "Suppressed NFAT-dependent VEGFR1 expression and constitutive VEGFR2
RT signaling in infantile hemangioma.";
RL Nat. Med. 14:1236-1246(2008).
CC -!- FUNCTION: Plays a role in cell attachment and migration. Interacts with
CC extracellular matrix proteins and with the actin cytoskeleton. Mediates
CC adhesion of cells to type 1 collagen and gelatin, reorganization of the
CC actin cytoskeleton and promotes cell spreading. Plays a role in the
CC angiogenic response of cultured umbilical vein endothelial cells.
CC {ECO:0000269|PubMed:15777794, ECO:0000269|PubMed:16762926}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for protective
CC antigen (PA) of B.anthracis. {ECO:0000269|PubMed:11700562,
CC ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:16762926,
CC ECO:0000269|PubMed:20585457}.
CC -!- SUBUNIT: Interacts with gelatin and type 1 collagen. Interacts with the
CC actin cytoskeleton. {ECO:0000269|PubMed:15777794,
CC ECO:0000269|PubMed:16762926}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via VWFA domain) with the
CC protective antigen (PA) of B.anthracis (PubMed:11700562,
CC PubMed:12700348, PubMed:16762926, PubMed:20585457). Binding does not
CC occur in the presence of calcium (PubMed:11700562, PubMed:12700348,
CC PubMed:16762926, PubMed:20585457). {ECO:0000269|PubMed:11700562,
CC ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:16762926,
CC ECO:0000269|PubMed:20585457}.
CC -!- INTERACTION:
CC Q9H6X2; O75581: LRP6; NbExp=3; IntAct=EBI-905643, EBI-910915;
CC Q9H6X2-2; P13423: pagA; Xeno; NbExp=3; IntAct=EBI-905659, EBI-456868;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16762926};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell
CC projection, lamellipodium membrane {ECO:0000269|PubMed:16762926};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}. Cell
CC projection, filopodium membrane {ECO:0000269|PubMed:16762926}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:16762926}. Note=At the
CC membrane of lamellipodia and at the tip of actin-enriched filopodia
CC (PubMed:16762926). Colocalizes with actin at the base of lamellipodia
CC (PubMed:16762926). {ECO:0000269|PubMed:16762926}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9H6X2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6X2-2; Sequence=VSP_000444, VSP_000445;
CC Name=3;
CC IsoId=Q9H6X2-3; Sequence=VSP_000446, VSP_000447;
CC Name=4;
CC IsoId=Q9H6X2-4; Sequence=VSP_000448, VSP_000449;
CC Name=5; Synonyms=V4;
CC IsoId=Q9H6X2-5; Sequence=VSP_047865;
CC Name=6; Synonyms=V5;
CC IsoId=Q9H6X2-6; Sequence=VSP_047863, VSP_047864;
CC -!- TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells (at
CC protein level). Highly expressed in tumor endothelial cells.
CC {ECO:0000269|PubMed:15777794}.
CC -!- INDUCTION: Up-regulated in cultured angiogenic umbilical vein
CC endothelial cells. {ECO:0000269|PubMed:15777794}.
CC -!- DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A
CC condition characterized by dull red, firm, dome-shaped hemangiomas,
CC sharply demarcated from surrounding skin, usually presenting at birth
CC or occurring within the first two or three months of life. They result
CC from highly proliferative, localized growth of capillary endothelium
CC and generally undergo regression and involution without scarring.
CC {ECO:0000269|PubMed:18931684}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- DISEASE: GAPO syndrome (GAPOS) [MIM:230740]: An autosomal recessive
CC disease characterized by growth retardation, alopecia, failure of tooth
CC eruption, and progressive optic atrophy in some patients.
CC {ECO:0000269|PubMed:23602711}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- MISCELLANEOUS: [Isoform 6]: Prostate-specific. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91707.1; Type=Miscellaneous discrepancy; Note=Erroneous initiation (Translation N-terminally extended) due to a conflict with the genome, including a frameshift.; Evidence={ECO:0000305};
CC Sequence=BAB15128.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF279145; AAK52094.1; -; mRNA.
DR EMBL; AF421380; AAL26496.1; -; mRNA.
DR EMBL; JX424838; AFQ94038.1; -; mRNA.
DR EMBL; JX424839; AFQ94039.1; -; mRNA.
DR EMBL; AK001463; BAA91707.1; ALT_SEQ; mRNA.
DR EMBL; AK025429; BAB15128.1; ALT_INIT; mRNA.
DR EMBL; AK292113; BAF84802.1; -; mRNA.
DR EMBL; AC112230; AAX88860.1; -; Genomic_DNA.
DR EMBL; AC114802; AAY24067.1; -; Genomic_DNA.
DR EMBL; BC012074; AAH12074.1; -; mRNA.
DR CCDS; CCDS1892.1; -. [Q9H6X2-1]
DR CCDS; CCDS46313.1; -. [Q9H6X2-2]
DR CCDS; CCDS46314.1; -. [Q9H6X2-4]
DR RefSeq; NP_060623.2; NM_018153.3. [Q9H6X2-4]
DR RefSeq; NP_115584.1; NM_032208.2. [Q9H6X2-1]
DR RefSeq; NP_444262.1; NM_053034.2. [Q9H6X2-2]
DR PDB; 3N2N; X-ray; 1.80 A; A/B/C/D/E/F=38-220.
DR PDB; 6ADL; EM; 3.08 A; R=38-220.
DR PDB; 6ADM; EM; 2.84 A; R=38-220.
DR PDB; 6ADR; EM; 3.38 A; R=38-220.
DR PDB; 6CX1; EM; 3.80 A; E=39-220.
DR PDBsum; 3N2N; -.
DR PDBsum; 6ADL; -.
DR PDBsum; 6ADM; -.
DR PDBsum; 6ADR; -.
DR PDBsum; 6CX1; -.
DR AlphaFoldDB; Q9H6X2; -.
DR SMR; Q9H6X2; -.
DR BioGRID; 123924; 150.
DR IntAct; Q9H6X2; 53.
DR MINT; Q9H6X2; -.
DR STRING; 9606.ENSP00000301945; -.
DR DrugBank; DB05945; MDX-1303.
DR GlyGen; Q9H6X2; 3 sites.
DR iPTMnet; Q9H6X2; -.
DR PhosphoSitePlus; Q9H6X2; -.
DR SwissPalm; Q9H6X2; -.
DR BioMuta; ANTXR1; -.
DR DMDM; 17366074; -.
DR EPD; Q9H6X2; -.
DR jPOST; Q9H6X2; -.
DR MassIVE; Q9H6X2; -.
DR MaxQB; Q9H6X2; -.
DR PaxDb; Q9H6X2; -.
DR PeptideAtlas; Q9H6X2; -.
DR PRIDE; Q9H6X2; -.
DR ProteomicsDB; 81048; -. [Q9H6X2-1]
DR ProteomicsDB; 81049; -. [Q9H6X2-2]
DR ProteomicsDB; 81050; -. [Q9H6X2-3]
DR ProteomicsDB; 81051; -. [Q9H6X2-4]
DR Antibodypedia; 16201; 629 antibodies from 38 providers.
DR DNASU; 84168; -.
DR Ensembl; ENST00000303714.9; ENSP00000301945.4; ENSG00000169604.21. [Q9H6X2-1]
DR Ensembl; ENST00000409349.7; ENSP00000386494.3; ENSG00000169604.21. [Q9H6X2-2]
DR Ensembl; ENST00000409829.7; ENSP00000387058.3; ENSG00000169604.21. [Q9H6X2-4]
DR Ensembl; ENST00000463335.2; ENSP00000506719.1; ENSG00000169604.21. [Q9H6X2-3]
DR GeneID; 84168; -.
DR KEGG; hsa:84168; -.
DR MANE-Select; ENST00000303714.9; ENSP00000301945.4; NM_032208.3; NP_115584.1.
DR UCSC; uc002sfe.4; human. [Q9H6X2-1]
DR CTD; 84168; -.
DR DisGeNET; 84168; -.
DR GeneCards; ANTXR1; -.
DR HGNC; HGNC:21014; ANTXR1.
DR HPA; ENSG00000169604; Low tissue specificity.
DR MalaCards; ANTXR1; -.
DR MIM; 230740; phenotype.
DR MIM; 602089; phenotype.
DR MIM; 606410; gene.
DR neXtProt; NX_Q9H6X2; -.
DR OpenTargets; ENSG00000169604; -.
DR Orphanet; 2067; GAPO syndrome.
DR Orphanet; 464293; NON RARE IN EUROPE: Infantile capillary hemangioma.
DR PharmGKB; PA134956382; -.
DR VEuPathDB; HostDB:ENSG00000169604; -.
DR eggNOG; ENOG502QSKR; Eukaryota.
DR GeneTree; ENSGT00940000156522; -.
DR HOGENOM; CLU_029760_0_0_1; -.
DR InParanoid; Q9H6X2; -.
DR OMA; PRNLANN; -.
DR PhylomeDB; Q9H6X2; -.
DR TreeFam; TF328943; -.
DR PathwayCommons; Q9H6X2; -.
DR Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
DR SignaLink; Q9H6X2; -.
DR BioGRID-ORCS; 84168; 17 hits in 1074 CRISPR screens.
DR ChiTaRS; ANTXR1; human.
DR GeneWiki; ANTXR1; -.
DR GenomeRNAi; 84168; -.
DR Pharos; Q9H6X2; Tbio.
DR PRO; PR:Q9H6X2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H6X2; protein.
DR Bgee; ENSG00000169604; Expressed in stromal cell of endometrium and 185 other tissues.
DR ExpressionAtlas; Q9H6X2; baseline and differential.
DR Genevisible; Q9H6X2; HS.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
DR GO; GO:0022414; P:reproductive process; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
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:SF11; PTHR16059:SF11; 1.
DR Pfam; PF05586; Ant_C; 1.
DR Pfam; PF05587; Anth_Ig; 1.
DR Pfam; PF00092; VWA; 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; Cell projection;
KW Disulfide bond; Glycoprotein; Hypotrichosis; Membrane; Metal-binding;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..564
FT /note="Anthrax toxin receptor 1"
FT /id="PRO_0000002692"
FT TOPO_DOM 33..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..215
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 154..160
FT /note="Interaction with PA"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..564
FT /note="Pro residues"
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:20585457,
FT ECO:0007744|PDB:3N2N"
FT BINDING 54
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20585457,
FT ECO:0007744|PDB:3N2N"
FT BINDING 118
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20585457,
FT ECO:0007744|PDB:3N2N"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..220
FT /evidence="ECO:0000269|PubMed:20585457"
FT VAR_SEQ 268..297
FT /note="NEKPFSVEDTYLLCPAPILKEVGMKAALQV -> SKSLQSPWVSSTSGFKEG
FT NSHPCLPARPHT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000446"
FT VAR_SEQ 298..564
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_000447"
FT VAR_SEQ 315..358
FT /note="THCSDGSILAIALLILFLLLALALLWWFWPLCCTVIIKEVPPPP -> FHPS
FT PSSPGSTSQQGTSSLPPSSKAFCLEPKVPALGSLRNFRRC (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:22912819"
FT /id="VSP_047863"
FT VAR_SEQ 319..333
FT /note="DGSILAIALLILFLL -> LHKIASGPTTAACME (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000448"
FT VAR_SEQ 334..564
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000449"
FT VAR_SEQ 359..564
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:22912819"
FT /id="VSP_047864"
FT VAR_SEQ 365..368
FT /note="EDDD -> NKIK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11700562"
FT /id="VSP_000444"
FT VAR_SEQ 369..564
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11700562"
FT /id="VSP_000445"
FT VAR_SEQ 522..557
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:22912819"
FT /id="VSP_047865"
FT VARIANT 7
FT /note="R -> K (in dbSNP:rs28365986)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_053015"
FT VARIANT 326
FT /note="A -> T (in HCI susceptibility; expression of FLT1 in
FT hemangioma endothelial cells is markedly reduced compared
FT to controls; low FLT1 expression in hemangioma cells is
FT caused by reduced activity of a pathway involving ITGB1,
FT ANTXR1, KDR and NFATC2IP; the mutation disrupts interaction
FT of these molecules in a dominant-negative manner;
FT dbSNP:rs119475040)"
FT /evidence="ECO:0000269|PubMed:18931684"
FT /id="VAR_063146"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:3N2N"
FT STRAND 78..96
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:3N2N"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:3N2N"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:3N2N"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:3N2N"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3N2N"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3N2N"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:3N2N"
SQ SEQUENCE 564 AA; 62789 MW; B118A00AD5DF2233 CRC64;
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD KSGSVLHHWN
EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE QIRQGLEELQ KVLPGGDTYM
HEGFERASEQ IYYENRQGYR TASVIIALTD GELHEDLFFY SEREANRSRD LGAIVYCVGV
KDFNETQLAR IADSKDHVFP VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV
VRGNGFRHAR NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI IKEVPPPPAE
ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE KGSTEEGAKL EKAKNARVKM
PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI KGKLDALWVL LRKGYDRVSV MRPQPGDTGR
CINFTRVKNN QPAKYPLNNA YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL
PPPPQAPPPN RAPPPSRPPP RPSV
