Q9CZ52 (ANTR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Anthrax toxin receptor 1

Alternative name(s):
Tumor endothelial marker 8

Gene names

Name:	Antxr1
Synonyms:	Atr, Tem8

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 By similarity.
Subunit structure	Interacts with gelatin and type 1 collagen. Interacts with the actin cytoskeleton. Binds to the protective antigen (PA) of Bacillus anthracis. Binding does not occur in the presence of calcium By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Cell projection › lamellipodium membrane; Single-pass type I membrane protein By similarity. Cell projection › filopodium membrane; Single-pass type I membrane protein By similarity. Note: At the membrane of lamellipodia and at the tip of actin-enriched filopodia. Colocalizes with actin at the base of lamellipodia By similarity.
Domain	Binding to PA occurs through the VWA domain By similarity.
Sequence similarities	Belongs to the ATR family. Contains 1 VWFA domain.
Sequence caution	The sequence BAB28591.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Ligand	Metal-binding
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB substrate adhesion-dependent cell spreading Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	filopodium membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lamellipodium membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB collagen binding Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane signaling receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9CZ52-1)

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: Q9CZ52-2)

The sequence of this isoform differs from the canonical sequence as follows:
     477-562: GRCINFTRVK...PSRPPPRPSV → RFRGWRLTIC...FSSFLERAFQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Potential
	Chain	31 – 562	532	Anthrax toxin receptor 1		PRO_0000002693
Regions
	Topological domain	31 – 319	289	Extracellular Potential
	Transmembrane	320 – 340	21	Helical; Potential
	Topological domain	341 – 562	222	Cytoplasmic Potential
	Domain	42 – 213	172	VWFA
	Region	152 – 158	7	Interaction with PA By similarity
	Compositional bias	358 – 366	9	Asp/Glu-rich (highly acidic)
	Compositional bias	501 – 562	62	Pro-rich
Sites
	Metal binding	50	1	Divalent metal cation By similarity
	Metal binding	52	1	Divalent metal cation By similarity
	Metal binding	116	1	Divalent metal cation By similarity
Amino acid modifications
	Modified residue	360	1	Phosphoserine By similarity
	Modified residue	423	1	Phosphotyrosine By similarity
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	182	1	N-linked (GlcNAc...) Potential
	Glycosylation	260	1	N-linked (GlcNAc...) Potential
	Disulfide bond	37 ↔ 218		By similarity
Natural variations
	Alternative sequence	477 – 562	86	GRCIN…PRPSV → RFRGWRLTICLGSKHVHPGR HDKGPETPLLKQAWMFSSFL ERAFQ in isoform 2.		VSP_000450

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 2, 2001. Version 2. Checksum: 6AC92049B4BB4F7C	FASTA	562	62,308
	10 20 30 40 50 60 MDRAGRLGAG LRGLCVAALV LVCAGHGGRR EDGGPACYGG FDLYFILDKS GSVLHHWNEI 70 80 90 100 110 120 YYFVEQLAHR FISPQLRMSF IVFSTRGTTL MKLTEDREQI RQGLEELQKV LPGGDTYMHE 130 140 150 160 170 180 GFERASEQIY YENSQGYRTA SVIIALTDGE LHEDLFFYSE REANRSRDLG AIVYCVGVKD 190 200 210 220 230 240 FNETQLARIA DSKDHVFPVN DGFQALQGII HSILKKSCIE ILAAEPSTIC AGESFQVVVR 250 260 270 280 290 300 GNGFRHARNV DRVLCSFKIN DSVTLNEKPF AVEDTYLLCP APILKEVGMK AALQVSMNDG 310 320 330 340 350 360 LSFISSSVII TTTHCSDGSI LAIALLVLFL LLALALLWWF WPLCCTVIIK EVPPPPVEES 370 380 390 400 410 420 EEEDDDGLPK KKWPTVDASY YGGRGVGGIK RMEVRWGEKG STEEGAKLEK AKNARVKMPE 430 440 450 460 470 480 QEYEFPEPRN LNNNMRRPSS PRKWYSPIKG KLDALWVLLR KGYDRVSVMR PQPGDTGRCI 490 500 510 520 530 540 NFTRVKNSQP AKYPLNNTYH PSSPPPAPIY TPPPPAPHCP PPAPSAPTPP IPSPPSTLPP 550 560 PPQAPPPNRA PPPSRPPPRP SV
	Isoform 2 [UniParc]. Checksum: 95FC613140B6B790	FASTA	521	58,615
	10 20 30 40 50 60 MDRAGRLGAG LRGLCVAALV LVCAGHGGRR EDGGPACYGG FDLYFILDKS GSVLHHWNEI 70 80 90 100 110 120 YYFVEQLAHR FISPQLRMSF IVFSTRGTTL MKLTEDREQI RQGLEELQKV LPGGDTYMHE 130 140 150 160 170 180 GFERASEQIY YENSQGYRTA SVIIALTDGE LHEDLFFYSE REANRSRDLG AIVYCVGVKD 190 200 210 220 230 240 FNETQLARIA DSKDHVFPVN DGFQALQGII HSILKKSCIE ILAAEPSTIC AGESFQVVVR 250 260 270 280 290 300 GNGFRHARNV DRVLCSFKIN DSVTLNEKPF AVEDTYLLCP APILKEVGMK AALQVSMNDG 310 320 330 340 350 360 LSFISSSVII TTTHCSDGSI LAIALLVLFL LLALALLWWF WPLCCTVIIK EVPPPPVEES 370 380 390 400 410 420 EEEDDDGLPK KKWPTVDASY YGGRGVGGIK RMEVRWGEKG STEEGAKLEK AKNARVKMPE 430 440 450 460 470 480 QEYEFPEPRN LNNNMRRPSS PRKWYSPIKG KLDALWVLLR KGYDRVSVMR PQPGDTRFRG 490 500 510 520 WRLTICLGSK HVHPGRHDKG PETPLLKQAW MFSSFLERAF Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell surface tumor endothelial markers are conserved in mice and humans." Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W., St Croix B. Cancer Res. 61:6649-6655(2001) [PubMed: 11559528] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Brain.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-562 (ISOFORM 2). Strain: C57BL/6J. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF378762 mRNA. Translation: AAL11999.1. BC094544 mRNA. Translation: AAH94544.1. AK013005 mRNA. Translation: BAB28591.1. Different initiation.
IPI	IPI00229069. IPI00318636.
RefSeq	NP_473382.1. NM_054041.2.
UniGene	Mm.232525.
3D structure databases
ProteinModelPortal	Q9CZ52.
SMR	Q9CZ52. Positions 35-294.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9CZ52.
PTM databases
PhosphoSite	Q9CZ52.
Proteomic databases
PRIDE	Q9CZ52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000042025; ENSMUSP00000045634; ENSMUSG00000033420. ENSMUST00000113646; ENSMUSP00000109276; ENSMUSG00000033420.
GeneID	69538.
KEGG	mmu:69538.
UCSC	uc009cte.1. mouse. uc009ctf.1. mouse.
Organism-specific databases
CTD	84168.
MGI	MGI:1916788. Antxr1.
Phylogenomic databases
GeneTree	ENSGT00430000031214.
HOGENOM	HBG443624.
HOVERGEN	HBG050514.
InParanoid	Q9CZ52.
OMA	HCSDGTI.
OrthoDB	EOG45TCN4.
Gene expression databases
ArrayExpress	Q9CZ52.
Bgee	Q9CZ52.
CleanEx	MM_ANTXR1. MM_ATR.
Genevestigator	Q9CZ52.
GermOnline	ENSMUSG00000033420. Mus musculus.
Family and domain databases
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
NextBio	329708.
SOURCE	Search...

Entry information

Entry name

ANTR1_MOUSE

Accession

Primary (citable) accession number: Q9CZ52
Secondary accession number(s): Q505H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	November 2, 2001
Last modified:	January 25, 2012
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program