ID B7QN63_IXOSC Unreviewed; 255 AA.
AC B7QN63;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Secreted beta amyloid protein, putative {ECO:0000313|EMBL:EEC20285.1};
DE Flags: Fragment;
GN ORFNames=IscW_ISCW015537 {ECO:0000313|EMBL:EEC20285.1};
OS Ixodes scapularis (Black-legged tick) (Deer tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=6945;
RN [1] {ECO:0000313|EMBL:EEC20285.1, ECO:0000313|Proteomes:UP000001555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC {ECO:0000313|EMBL:EEC20285.1};
RG Ixodes scapularis Genome Project Consortium;
RA Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT "Annotation of Ixodes scapularis.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ISCW015537-PA}
RP IDENTIFICATION.
RC STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW015537-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 APP family. {ECO:0000256|PROSITE-
CC ProRule:PRU01217}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABJB010128303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ABJB010645886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS976702; EEC20285.1; -; Genomic_DNA.
DR RefSeq; XP_002400743.1; XM_002400699.1.
DR AlphaFoldDB; B7QN63; -.
DR STRING; 6945.B7QN63; -.
DR PaxDb; 6945-B7QN63; -.
DR EnsemblMetazoa; ISCW015537-RA; ISCW015537-PA; ISCW015537.
DR KEGG; isc:IscW_ISCW015537; -.
DR VEuPathDB; VectorBase:ISCI015537; -.
DR VEuPathDB; VectorBase:ISCP_016833; -.
DR VEuPathDB; VectorBase:ISCW015537; -.
DR HOGENOM; CLU_1092251_0_0_1; -.
DR InParanoid; B7QN63; -.
DR OMA; STEXELL; -.
DR Proteomes; UP000001555; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 1.
DR Gene3D; 3.30.1490.140; Amyloidogenic glycoprotein, copper-binding domain; 1.
DR Gene3D; 3.90.570.10; Amyloidogenic glycoprotein, heparin-binding domain; 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR PANTHER; PTHR23103; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR PANTHER; PTHR23103:SF15; AMYLOID-BETA-LIKE PROTEIN; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF109843; CAPPD, an extracellular domain of amyloid beta A4 protein; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01217}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B7QN63};
KW Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 8..172
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 224..255
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 8..106
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 114..172
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 173..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 116..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 127..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 141..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEC20285.1"
FT NON_TER 255
FT /evidence="ECO:0000313|EMBL:EEC20285.1"
SQ SEQUENCE 255 AA; 28998 MW; CD07BC11AB820164 CRC64;
GSVDPDLGHF QPMVALLCGH GRINNQYLAE GQRWVSDPDP KAVCSKDKLS ILEYCRKVYP
KRDIRNIVES SRYYHVDGWC KVGQRGRSCR GSHWVKPYRC LEGDFQSDAL LVPEHCLFDH
IHNQSVCQSF DDWNQTAAHS CQGRSMRLRS FAMLLPCGVD IFSGVEFVCC PTEGKSSKEE
GKGTSSEEDE DYDDYSSVEE EEETTSTTPS TTTSTTPGTT TERPVDHYFS HFDSKHEHDS
FKEAQRNLEE GHREK
//
