Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00560
Entry Name
UniProt Accession
Theoretical PI
7.54
Molecular Weight
62788.98
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Anthrax toxin receptor 1
Protein Synonyms/Alias
Tumor endothelial marker 8;
Gene Name
ANTXR1
Gene Synonyms/Alias
ATR; TEM8;
Created Date
02-NOV-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
347
Canonical
WWFWPLCCTVIIKEV
[1]
S-Palmitoylation
481
Canonical
QPGDTGRCINFTRVK
[1]
S-Palmitoylation
521
Canonical
PPPPAPHCPPPPPSA
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Abrami L, Leppla SH, van der Goot FG. Receptor palmitoylation andubiquitination regulate anthrax toxin endocytosis. J Cell Biol. 2006 Jan16;172(2):309-20. Epub 2006 Jan 9.[PMID:16401723]
Functional Description
Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells.
Sequence Annotation
Topological domain: 33 321 Extracellular.
Transmembrane: 322 342 Helical.
Topological domain: 343 564 Cytoplasmic.
Domain: 44 215 VWFA.
Region: 154 160 Interaction with PA.
Metal binding site: 52 52 Divalent metal cation.
Metal binding site: 54 54 Divalent metal cation.
Metal binding site: 118 118 Divalent metal cation.
Modified residue: 362 362 Phosphoserine.
Protein Length
564 AA.
Protein Sequence
(Canonical)
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD KSGSVLHHWN  60
EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE QIRQGLEELQ KVLPGGDTYM  120
HEGFERASEQ IYYENRQGYR TASVIIALTD GELHEDLFFY SEREANRSRD LGAIVYCVGV  180
KDFNETQLAR IADSKDHVFP VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV  240
VRGNGFRHAR NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN  300
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI IKEVPPPPAE  360
ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE KGSTEEGAKL EKAKNARVKM  420
PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI KGKLDALWVL LRKGYDRVSV MRPQPGDTGR  480
CINFTRVKNN QPAKYPLNNA YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL  540
PPPPQAPPPN RAPPPSRPPP RPSV                                         564
FASTA
(Canonical)
>LipidDB-9606-00560|Q9H6X2
MATAERRALGIGFQWLSLATLVLICAGQGGRREDGGPACYGGFDLYFILDKSGSVLHHWN
EIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDREQIRQGLEELQKVLPGGDTYM
HEGFERASEQIYYENRQGYRTASVIIALTDGELHEDLFFYSEREANRSRDLGAIVYCVGV
KDFNETQLARIADSKDHVFPVNDGFQALQGIIHSILKKSCIEILAAEPSTICAGESFQVV
VRGNGFRHARNVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQVSMN
DGLSFISSSVIITTTHCSDGSILAIALLILFLLLALALLWWFWPLCCTVIIKEVPPPPAE
ESEEEDDDGLPKKKWPTVDASYYGGRGVGGIKRMEVRWGEKGSTEEGAKLEKAKNARVKM
PEQEYEFPEPRNLNNNMRRPSSPRKWYSPIKGKLDALWVLLRKGYDRVSVMRPQPGDTGR
CINFTRVKNNQPAKYPLNNAYHTSSPPPAPIYTPPPPAPHCPPPPPSAPTPPIPSPPSTL
PPPPQAPPPNRAPPPSRPPPRPSV
Gene Ontology
GO:0009986; C:cell surface; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0031527; C:filopodium membrane; IDA:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0031258; C:lamellipodium membrane; IDA:UniProtKB
GO:0051015; F:actin filament binding; IDA:UniProtKB
GO:0005518; F:collagen binding; IDA:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB
GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB
GO:0022414; P:reproductive process; IEA:Ensembl
GO:0007165; P:signal transduction; IDA:GOC
GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB
Interpro
InterPro; IPR017360; Anthrax_toxin_rcpt
InterPro; IPR008399; Anthrax_toxin_rcpt_C
InterPro; IPR008400; Anthrax_toxin_rcpt_extracel
InterPro; IPR002035; VWF_A
Pfam
Pfam; PF05586; Ant_C;
Pfam; PF05587; Anth_Ig;
Pfam; PF00092; VWA;
SMART
SMART; SM00327; VWA;
PROSITE
PROSITE; PS50234; VWFA;
PRINTS