ANTRL_MACFA
ID ANTRL_MACFA Reviewed; 557 AA.
AC Q4R7B7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Anthrax toxin receptor-like;
DE Flags: Precursor;
GN Name=ANTXRL; ORFNames=QtsA-15671;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
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DR EMBL; AB168903; BAE01005.1; -; mRNA.
DR AlphaFoldDB; Q4R7B7; -.
DR SMR; Q4R7B7; -.
DR STRING; 9541.XP_005565180.1; -.
DR eggNOG; ENOG502QSKR; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
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 2: Evidence at transcript level;
KW Membrane; Metal-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..557
FT /note="Anthrax toxin receptor-like"
FT /id="PRO_0000332167"
FT TOPO_DOM 26..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 74..244
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 380..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
SQ SEQUENCE 557 AA; 62019 MW; B524252DEBE18FAC CRC64;
MRSHGRWGPC FLLFLLLLPP PLFRAGSLRY HGPGWRMFQR LALGSRRANH HHGPGWRQQL
RQGQAGHRCQ GSFDLYFILD KSGSVNNNWI DLYMWVEETV ARFQSSDIRM CFITYSTDGQ
TVLPLTSDKN RIKNGLDQLR KIVPDGHTFM QAGFRKAIQQ IETFNSGNKV PSMIIAMTDG
ELVAHAFQDT LREAQKARKL GANVYTVDVA DYKLDQITAI ADSPEHVFAV ENGFKAMRDT
VDALTSKVCL DVTSVEPPTV CVGEPYHVVV HGNGFQNLKK QDEVICRFIF NETTIVDEKP
TSIDNNSMNC PGPKLEKPGE EYFIEVSLNN GKTFFKSNVS VTSSTCGIFS NWLYFLLPLL
LLPLLLCCLW RLCRKKTVKE PPPVQKPEKE PEQEKPPPPP PPSPPPPLPP PPPPPPPVNT
CPTVIVCCCA CQGVCGIRGI EGNLDTFCDL SHPSCCQVPW MWCQRRDQGR YLSLALAQSQ
YAQAPCCPRI GFPHSQESPS LPETQPGVLF PSTDSVQPKE LPSTWPAVPP HCSGTLQNPL
CPSLPRSPTS KAPNTQD