ID H3DGH9_TETNG Unreviewed; 534 AA.
AC H3DGH9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Anthrax toxin receptor {ECO:0000256|PIRNR:PIRNR038023};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019623.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019623.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the ATR family. {ECO:0000256|ARBA:ARBA00008095,
CC ECO:0000256|PIRNR:PIRNR038023}.
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DR AlphaFoldDB; H3DGH9; -.
DR Ensembl; ENSTNIT00000019853.1; ENSTNIP00000019623.1; ENSTNIG00000016523.1.
DR GeneTree; ENSGT00940000157727; -.
DR HOGENOM; CLU_029760_0_0_1; -.
DR InParanoid; H3DGH9; -.
DR OMA; RCISFQR; -.
DR TreeFam; TF328943; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR CDD; cd01474; vWA_ATR; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; ANTHRAX TOXIN RECEPTOR; 1.
DR PANTHER; PTHR16059:SF16; ANTHRAX TOXIN RECEPTOR-LIKE; 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; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR038023-2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR038023};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR038023,
KW ECO:0000256|PIRSR:PIRSR038023-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|PIRNR:PIRNR038023};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..175
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 314..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR038023-1"
FT BINDING 17
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR038023-1"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR038023-1"
FT DISULFID 2..180
FT /evidence="ECO:0000256|PIRSR:PIRSR038023-2"
SQ SEQUENCE 534 AA; 59249 MW; 4EE25CA3E6919BA6 CRC64;
SCHGAFDLYF VLDKSGSVKH HWTEIYSFVK QLAEKFISPM LRMSFIVFST RGNIIMKLTE
DREAIKGGLM ALKNVIPGGD TLMNLGLEMA NMQIYQERYG TASVIIALTD GELNEWQFDL
AQQEAQRARS MGAIVYCVGV KDFNQTQLAT IADTVEHVFP VWGGFQALRG IIDSIIKKSC
IEILAAEPSS VCAGESFEVV VKGNGFLHAR NIDQVLCSFK LNNTLSVDER PARIEDTFLL
CPAPVVEEPG RVIYLQVSMN EGLSYITSSV HITTTECFDG TIVLISLLVV FLLLALLLMW
WFWPLCCTVV IKEPPPPPPP EPESDEDDGM PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE
KGSTEEGAKL DKPKNAVVKM PDQEFEPYEP KPRKPPRHRP QQRRWYTPIK GKLDAIWALF
RRGYDQVSLM RPHPGDQGRC INFQRVKDGE PTRTNQAPPR TSHSSSLPPP PPAAVERPLI
SNSVPRTKPP SRGPRTEPPA RAPPSVATPA PGPPPARAPP GPRAPPPSRP PPKL
//